entry created 2011-02-08 dataset Swiss-Prot modified 2023-02-22 version 62 accession Q9AQI0 name HMGA_PSEOC protein recommendedName fullName 4-hydroxy-4-methyl-2-oxoglutarate-aldolase/4-carboxy-4-hydroxy-2-oxoadipate-aldolase shortName HMG/CHA-aldolase ecNumber evidence 2-4 4.1.3.16 ecNumber evidence 2-4 4.1.3.17 alternativeName fullName 4-hydroxy-2-oxoglutarate-aldolase alternativeName fullName Oxaloacetate-decarboxylase shortName OAA-decarboxylase ecNumber evidence 4 4.1.1.112 gene name evidence 7 type primary proA organism name type scientific Pseudomonas-straminea dbReference id 47882 type NCBI-Taxonomy lineage taxon Bacteria taxon Proteobacteria taxon Gammaproteobacteria taxon Pseudomonadales taxon Pseudomonadaceae taxon Pseudomonas reference key 1 citation date 2001 first 2701 last 2709 name Biosci.-Biotechnol.-Biochem. type journal-article volume 65 title Cloning,-sequencing,-and-expression-of-the-gene-encoding-4-hydroxy-4-methyl-2-oxoglutarate-aldolase-from-Pseudomonas-ochraceae-NGJ1. authorList person name Maruyama-K. person name Miwa-M. person name Tsujii-N. person name Nagai-T. person name Tomita-N. person name Harada-T. person name Sobajima-H. person name Sugisaki-H. dbReference id 11826967 type PubMed dbReference id 10.1271/bbb.65.2701 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope PROTEIN-SEQUENCE-OF-1-22 scope FUNCTION scope CATALYTIC-ACTIVITY scope COFACTOR scope BIOPHYSICOCHEMICAL-PROPERTIES source strain evidence 7 NGJ1 reference key 2 citation date 1990 first 327 last 333 name J.-Biochem. type journal-article volume 108 title Purification-and-properties-of-4-hydroxy-4-methyl-2-oxoglutarate-aldolase-from-Pseudomonas-ochraceae-grown-on-phthalate. authorList person name Maruyama-K. dbReference id 2229032 type PubMed dbReference id 10.1093/oxfordjournals.jbchem.a123201 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY scope COFACTOR scope ACTIVITY-REGULATION scope BIOPHYSICOCHEMICAL-PROPERTIES scope SUBUNIT scope INDUCTION reference key 3 citation date 1990 first 334 last 340 name J.-Biochem. type journal-article volume 108 title Activation-of-Pseudomonas-ochraceae-4-hydroxy-4-methyl-2-oxoglutarate-aldolase-by-inorganic-phosphate. authorList person name Maruyama-K. dbReference id 2229033 type PubMed dbReference id 10.1093/oxfordjournals.jbchem.a123202 type DOI scope ACTIVITY-REGULATION scope BIOPHYSICOCHEMICAL-PROPERTIES reference key 4 citation date 1991 first 976 last 981 name J.-Biochem. type journal-article volume 110 title Chemical-modification-of-Pseudomonas-ochraceae-4-hydroxy-4-methyl-2-oxoglutarate-aldolase-by-diethyl-pyrocarbonate. authorList person name Maruyama-K. dbReference id 1794988 type PubMed dbReference id 10.1093/oxfordjournals.jbchem.a123699 type DOI scope ACTIVITY-REGULATION comment type function text evidence 2-4 Catalyzes-the-last-step-of-the-bacterial-protocatechuate-4,5-cleavage-pathway.-Has-a-broad-substrate-specificity-and-catalyzes-the-aldol-cleavage-of-4-hydroxy-4-methyl-2-oxoglutarate,-4-hydroxy-2-oxoglutarate-and-4-carboxy-4-hydroxy-2-oxoadipate,-and-the-decarboxylation-of-oxaloacetate.-Preferentially-cleaves-the-L-isomer-of-4-carboxy-4-hydroxy-2-oxoadipate,-and-has-lower-activity-towards-4-hydroxy-4-methyl-2-oxoglutarate-and-4-Hydroxy-2-oxoglutarate.-Does-not-cleave-4-hydroxy-2-oxovalerate,-citrate,-4-hydroxy-2-oxobutyrate,-2-oxoglutarate-or-fructose-1,6-bisphosphate. comment type catalytic-activity reaction evidence 2-4 text (4S)-4-hydroxy-2-oxoglutarate-=-glyoxylate-+-pyruvate dbReference id RHEA:35639 type Rhea dbReference id CHEBI:15361 type ChEBI dbReference id CHEBI:36655 type ChEBI dbReference id CHEBI:71685 type ChEBI dbReference id 4.1.3.16 type EC comment type catalytic-activity reaction evidence 2-4 text (4R)-4-hydroxy-2-oxoglutarate-=-glyoxylate-+-pyruvate dbReference id RHEA:30687 type Rhea dbReference id CHEBI:15361 type ChEBI dbReference id CHEBI:36655 type ChEBI dbReference id CHEBI:62213 type ChEBI dbReference id 4.1.3.16 type EC comment type catalytic-activity reaction evidence 2-4 text 4-hydroxy-4-methyl-2-oxoglutarate-=-2-pyruvate dbReference id RHEA:22748 type Rhea dbReference id CHEBI:15361 type ChEBI dbReference id CHEBI:58276 type ChEBI dbReference id 4.1.3.17 type EC comment type catalytic-activity reaction evidence 2-4 text 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate-=-oxaloacetate-+-pyruvate dbReference id RHEA:28935 type Rhea dbReference id CHEBI:15361 type ChEBI dbReference id CHEBI:16452 type ChEBI dbReference id CHEBI:58075 type ChEBI dbReference id 4.1.3.17 type EC comment type catalytic-activity reaction evidence 4 text H(+)-+-oxaloacetate-=-CO2-+-pyruvate dbReference id RHEA:15641 type Rhea dbReference id CHEBI:15361 type ChEBI dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:16452 type ChEBI dbReference id CHEBI:16526 type ChEBI dbReference id 4.1.1.112 type EC comment type cofactor cofactor evidence 2-4 name Mg(2+) dbReference id CHEBI:18420 type ChEBI text evidence 2-4 Divalent-metal-cations.-Probably-Mg(2+). comment type activity-regulation text evidence 3-4-5 Cleavage-of-4-carboxy-4-hydroxy-2-oxoadipate,-and-to-a-lesser-extent-4-hydroxy-4-methyl-2-oxoglutarate,-is-inhibited-by-lysine-modification-caused-by-diethyl-pyrocarbonate.-Decarboxylation-of-oxaloacetate-is-unaffected-by-diethyl-pyrocarbonate.-Inhibited-by-BeCl(2),-CaCl(2),-NiCl(2),-BaCl(2),-HgCl(2),-SrSO(4),-CrCl(3)-and-FeCl(3).-Partially-inhibited-by-p-chloromercuribenzoate-and-N-ethylmaleimide.-Activated-by-inorganic-phosphate,-arsenate,-phosphorous-acid,-acetyl-phosphate,-thiamine-diphosphate,-ADP,-ATP-and-diphosphate. comment type biophysicochemical-properties kinetics KM evidence 2-4-5 0.044-mM-for-DL-4-carboxy-4-hydroxy-2-oxoadipate KM evidence 2-4-5 0.019-mM-for-L-4-carboxy-4-hydroxy-2-oxoadipate KM evidence 2-4-5 0.15-mM-for-D-4-carboxy-4-hydroxy-2-oxoadipate KM evidence 2-4-5 1.25-mM-for-DL-4-hydroxy-4-methyl-2-oxoglutarate KM evidence 2-4-5 0.24-mM-for-DL-4-hydroxy-2-oxoglutarate KM evidence 2-4-5 0.5-mM-for-oxaloacetate Vmax evidence 2-4-5 1250.0-umol/min/mg-enzyme-with-DL-4-carboxy-4-hydroxy-2-oxoadipate-as-substrate Vmax evidence 2-4-5 1220.0-umol/min/mg-enzyme-with-L-4-carboxy-4-hydroxy-2-oxoadipate-as-substrate Vmax evidence 2-4-5 67.6-umol/min/mg-enzyme-with-D-4-carboxy-4-hydroxy-2-oxoadipate-as-substrate Vmax evidence 2-4-5 213.0-umol/min/mg-enzyme-with-DL-4-hydroxy-4-methyl-2-oxoglutarate-as-substrate Vmax evidence 2-4-5 1.3-umol/min/mg-enzyme-with-DL-4-hydroxy-2-oxoglutarate-as-substrate Vmax evidence 2-4-5 20.8-umol/min/mg-enzyme-with-oxaloacetate-as-substrate phDependence text evidence 2-4-5 Optimum-pH-varies-depending-on-the-substrate-used-and-phosphate-concentration.-In-the-absence-of-inorganic-phosphate-pH-optima-are-6.6-for-L-4-carboxy-4-hydroxy-2-oxoadipate,-8.0-for-D-4-carboxy-4-hydroxy-2-oxoadipate,-6.7-and-8.0-for-DL-4-carboxy-4-hydroxy-2-oxoadipate,-8.3-for-DL-4-hydroxy-4-methyl-2-oxoglutarate,-9.3-for-DL-4-hydroxy-2-oxoglutarate-and-8.8-for-oxaloacetate.-In-the-presence-of-3-mM-inorganic-phosphate-pH-optima-are-more-alkaline:-8.2-for-L-4-carboxy-4-hydroxy-2-oxoadipate,-8.6-for-D-4-carboxy-4-hydroxy-2-oxoadipate,-8.2-for-DL-4-carboxy-4-hydroxy-2-oxoadipate,-8.9-for-DL-4-hydroxy-4-methyl-2-oxoglutarate,-9.4-for-DL-4-hydroxy-2-oxoglutarate-and-8.9-for-oxaloacetate.-Stable-at-pH-6.0-to-pH-9.5. temperatureDependence text evidence 2-4-5 Retains-50%-of-maximum-activity-after-incubation-at-54-degrees-Celsius-for-10-minutes. comment type subunit text evidence 4 Homohexamer. comment type induction text evidence 4 By-growth-on-aromatic-carboxylates-such-as-phthalate,-terephthalate,-m-hydroxybenzoate-and-p-hydroxybenzoate. comment type similarity text evidence 6 Belongs-to-the-LigK/PcmE-family. dbReference evidence 2-4 id 4.1.3.16 type EC dbReference evidence 2-4 id 4.1.3.17 type EC dbReference evidence 4 id 4.1.1.112 type EC dbReference id AB050935 type EMBL property type protein-sequence-ID value BAB21456.3 property type molecule-type value Genomic_DNA dbReference id Q9AQI0 type AlphaFoldDB dbReference id Q9AQI0 type SMR dbReference id MetaCyc:MON-3244 type BioCyc dbReference id GO:0106009 type GO property type term value F:(4S)-4-hydroxy-2-oxoglutarate-aldolase-activity property type evidence value ECO:0007669 property type project value RHEA dbReference id GO:0008700 type GO property type term value F:4-hydroxy-2-oxoglutarate-aldolase-activity property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0047443 type GO property type term value F:4-hydroxy-4-methyl-2-oxoglutarate-aldolase-activity property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0046872 type GO property type term value F:metal-ion-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0008948 type GO property type term value F:oxaloacetate-decarboxylase-activity property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0019619 type GO property type term value P:3,4-dihydroxybenzoate-catabolic-process property type evidence value ECO:0000314 property type project value UniProtKB dbReference id cd16841 type CDD property type entry-name value RraA_family property type match-status value 1 dbReference id 3.50.30.40 type Gene3D property type entry-name value Ribonuclease-E-inhibitor-RraA/RraA-like property type match-status value 1 dbReference id IPR014165 type InterPro property type entry-name value LigK_PcmE dbReference id IPR005493 type InterPro property type entry-name value RraA/RraA-like dbReference id IPR036704 type InterPro property type entry-name value RraA/RraA-like_sf dbReference id PTHR33254 type PANTHER property type entry-name value 4-HYDROXY-4-METHYL-2-OXOGLUTARATE-ALDOLASE-3-RELATED property type match-status value 1 dbReference id PTHR33254:SF16 type PANTHER property type entry-name value BLR3842-PROTEIN property type match-status value 1 dbReference id PF03737 type Pfam property type entry-name value RraA-like property type match-status value 1 dbReference id SSF89562 type SUPFAM property type entry-name value RraA-like property type match-status value 1 dbReference id TIGR02798 type TIGRFAMs property type entry-name value ligK_PcmE property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0903 Direct-protein-sequencing keyword id KW-0456 Lyase keyword id KW-0460 Magnesium keyword id KW-0479 Metal-binding feature description 4-hydroxy-4-methyl-2-oxoglutarate-aldolase/4-carboxy-4-hydroxy-2-oxoadipate-aldolase id PRO_0000403973 type chain location begin position 1 end position 227 feature evidence 1 type binding-site location begin position 97 end position 100 ligand name substrate feature evidence 1 type binding-site location position position 119 ligand name substrate feature evidence 1 type binding-site location position position 120 ligand name Mg(2+) dbReference id CHEBI:18420 type ChEBI evidence key 1 type ECO:0000250 source dbReference id A5W059 type UniProtKB evidence key 2 type ECO:0000269 source dbReference id 11826967 type PubMed evidence key 3 type ECO:0000269 source dbReference id 1794988 type PubMed evidence key 4 type ECO:0000269 source dbReference id 2229032 type PubMed evidence key 5 type ECO:0000269 source dbReference id 2229033 type PubMed evidence key 6 type ECO:0000305 evidence key 7 type ECO:0000312 source dbReference id BAB21456.3 type EMBL sequence checksum F56501D5BDD0262F length 227 mass 24068 modified 2001-06-01 version 1 MYELGVVYRNIQRADRAAADGLAALGSATVHEAMGRVGLLKPYMRPIYAGKQVSGTAVTVLLQPGDNWMMHVAAEQIQPGDIVVAAVTAECTDGYFGDLLATSFQARGARALIIDAGVRDVKTLQEMDFPVWSKAISSKGTIKATLGSVNIPIVCAGMLVTPGDVIVADDDGVVCVPAARAVEVLAAAQKRESFEGEKRAKLASGVLGLDMYKMREPLEKAGLKYID 
entry created 2011-05-03 dataset Swiss-Prot modified 2023-02-22 version 102 accession Q6FUD8 name HEK2_CANGB protein recommendedName fullName Heterogeneous-nuclear-rnp-K-like-protein-2 alternativeName fullName KH-domain-containing-protein-1 gene name type primary HEK2 name type synonym KHD1 name type ordered-locus CAGL0F04257g organism name type scientific Candida-glabrata name type common Yeast name type synonym Torulopsis-glabrata dbReference id 5478 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Saccharomycotina taxon Saccharomycetes taxon Saccharomycetales taxon Saccharomycetaceae taxon Nakaseomyces taxon Nakaseomyces/Candida-clade reference key 1 citation date 2004 first 35 last 44 name Nature type journal-article volume 430 title Genome-evolution-in-yeasts. authorList person name Dujon-B. person name Sherman-D. person name Fischer-G. person name Durrens-P. person name Casaregola-S. person name Lafontaine-I. person name de-Montigny-J. person name Marck-C. person name Neuveglise-C. person name Talla-E. person name Goffard-N. person name Frangeul-L. person name Aigle-M. person name Anthouard-V. person name Babour-A. person name Barbe-V. person name Barnay-S. person name Blanchin-S. person name Beckerich-J.-M. person name Beyne-E. person name Bleykasten-C. person name Boisrame-A. person name Boyer-J. person name Cattolico-L. person name Confanioleri-F. person name de-Daruvar-A. person name Despons-L. person name Fabre-E. person name Fairhead-C. person name Ferry-Dumazet-H. person name Groppi-A. person name Hantraye-F. person name Hennequin-C. person name Jauniaux-N. person name Joyet-P. person name Kachouri-R. person name Kerrest-A. person name Koszul-R. person name Lemaire-M. person name Lesur-I. person name Ma-L. person name Muller-H. person name Nicaud-J.-M. person name Nikolski-M. person name Oztas-S. person name Ozier-Kalogeropoulos-O. person name Pellenz-S. person name Potier-S. person name Richard-G.-F. person name Straub-M.-L. person name Suleau-A. person name Swennen-D. person name Tekaia-F. person name Wesolowski-Louvel-M. person name Westhof-E. person name Wirth-B. person name Zeniou-Meyer-M. person name Zivanovic-Y. person name Bolotin-Fukuhara-M. person name Thierry-A. person name Bouchier-C. person name Caudron-B. person name Scarpelli-C. person name Gaillardin-C. person name Weissenbach-J. person name Wincker-P. person name Souciet-J.-L. dbReference id 15229592 type PubMed dbReference id 10.1038/nature02579 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-2001-/-CBS-138-/-JCM-3761-/-NBRC-0622-/-NRRL-Y-65 comment type function text evidence 1 RNA-binding-protein-involved-in-the-correct-localization-of-transcripts-in-the-cell.-RNA-localization-is-a-widespread-mechanism-for-achieving-localized-protein-synthesis.-Involved-in-structural-and-functional-organization-of-telomeric-chromatin-and-regulates-silencing-at-the-HMR-locus-(By-similarity). comment type subunit text evidence 1 Binds-RNA. comment type subcellular-location subcellularLocation location evidence 1 Cytoplasm subcellularLocation location evidence 1 Cytoplasm location evidence 1 P-body subcellularLocation location evidence 1 Nucleus subcellularLocation location evidence 1 Chromosome location evidence 1 Telomere comment type similarity text evidence 4 Belongs-to-the-HEK2-family. dbReference id CR380952 type EMBL property type protein-sequence-ID value CAG59080.1 property type molecule-type value Genomic_DNA dbReference id XP_446156.1 type RefSeq property type nucleotide-sequence-ID value XM_446156.1 dbReference id Q6FUD8 type AlphaFoldDB dbReference id Q6FUD8 type SMR dbReference id 5478.XP_446156.1 type STRING dbReference id CAGL0F04257g-T type EnsemblFungi property type protein-sequence-ID value CAGL0F04257g-T-p1 property type gene-ID value CAGL0F04257g dbReference id 2887647 type GeneID dbReference id cgr:CAGL0F04257g type KEGG dbReference id CAL0131408 type CGD property type gene-designation value CAGL0F04257g dbReference id FungiDB:CAGL0F04257g type VEuPathDB dbReference id KOG2190 type eggNOG property type taxonomic-scope value Eukaryota dbReference id CLU_022670_2_0_1 type HOGENOM dbReference id Q6FUD8 type InParanoid dbReference id SIAKEPH type OMA dbReference id UP000002428 type Proteomes property type component value Chromosome-F dbReference id GO:0000781 type GO property type term value C:chromosome,-telomeric-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0005634 type GO property type term value C:nucleus property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0000932 type GO property type term value C:P-body property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0003729 type GO property type term value F:mRNA-binding property type evidence value ECO:0007669 property type project value EnsemblFungi dbReference id GO:0006325 type GO property type term value P:chromatin-organization property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0008298 type GO property type term value P:intracellular-mRNA-localization property type evidence value ECO:0007669 property type project value EnsemblFungi dbReference id GO:0048255 type GO property type term value P:mRNA-stabilization property type evidence value ECO:0007669 property type project value EnsemblFungi dbReference id GO:0051028 type GO property type term value P:mRNA-transport property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0006417 type GO property type term value P:regulation-of-translation property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0007004 type GO property type term value P:telomere-maintenance-via-telomerase property type evidence value ECO:0007669 property type project value EnsemblFungi dbReference id cd00105 type CDD property type entry-name value KH-I property type match-status value 1 dbReference id cd02396 type CDD property type entry-name value PCBP_like_KH property type match-status value 2 dbReference id 3.30.1370.10 type Gene3D property type entry-name value K-Homology-domain,-type-1 property type match-status value 3 dbReference id IPR004087 type InterPro property type entry-name value KH_dom dbReference id IPR004088 type InterPro property type entry-name value KH_dom_type_1 dbReference id IPR036612 type InterPro property type entry-name value KH_dom_type_1_sf dbReference id PTHR10288:SF309 type PANTHER property type entry-name value HETEROGENEOUS-NUCLEAR-RNP-K-LIKE-PROTEIN-2 property type match-status value 1 dbReference id PTHR10288 type PANTHER property type entry-name value KH-DOMAIN-CONTAINING-RNA-BINDING-PROTEIN property type match-status value 1 dbReference id PF00013 type Pfam property type entry-name value KH_1 property type match-status value 3 dbReference id SM00322 type SMART property type entry-name value KH property type match-status value 3 dbReference id SSF54791 type SUPFAM property type entry-name value Eukaryotic-type-KH-domain-(KH-domain-type-I) property type match-status value 3 dbReference id PS50084 type PROSITE property type entry-name value KH_TYPE_1 property type match-status value 3 proteinExistence type inferred-from-homology keyword id KW-0156 Chromatin-regulator keyword id KW-0158 Chromosome keyword id KW-0963 Cytoplasm keyword id KW-0509 mRNA-transport keyword id KW-0539 Nucleus keyword id KW-1185 Reference-proteome keyword id KW-0677 Repeat keyword id KW-0694 RNA-binding keyword id KW-0779 Telomere keyword id KW-0810 Translation-regulation keyword id KW-0813 Transport feature description Heterogeneous-nuclear-rnp-K-like-protein-2 id PRO_0000408188 type chain location begin position 1 end position 349 feature description KH-1 evidence 2 type domain location begin position 2 end position 67 feature description KH-2 evidence 2 type domain location begin position 120 end position 185 feature description KH-3 evidence 2 type domain location begin position 244 end position 324 feature description Disordered evidence 3 type region-of-interest location begin position 194 end position 214 evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000255 source dbReference id PRU00117 type PROSITE-ProRule evidence key 3 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 4 type ECO:0000305 sequence checksum F146EB5FE9C92BAF length 349 mass 38915 modified 2004-07-19 version 1 MPVSHRILLSLKEAAKVIGTQGNSIQSVRDNNNNVKIGISEKVPGCSDRVLTCSGEVEDVCSALGDVVTLLNKPSENEEETDNHHFYFLNHLLPVPTLDDLKATDPEASEEALHEQLQNIGYLRLLVFNSQLSSIIGKGGNQIKSLIEKHGVKLVASRAFLPDSTERMLEIQGVPSAIKQVLLDICEIIAKEEEEEEKARAENNNGESTGRKRFERKYYPHLQRNNTNSSSNNGSVGNSANSQEYTATVMIPESYVGALAGKKGNRLANLRKFTKTKILMESRPNDLDNEHEDENDMEEDDGRLRKFTIIGSSSRSVNLAESMLQRNLATEIERRKERLRNLSENNESA 
entry created 2011-06-28 dataset Swiss-Prot modified 2023-02-22 version 49 accession P0CR64 accession Q55VX2 accession Q5KKB9 name SNX41_CRYNJ protein recommendedName fullName Sorting-nexin-41 gene name type primary SNX41 name type ordered-locus CNC03560 organism name type scientific Cryptococcus-neoformans-var.-neoformans-serotype-D-(strain-JEC21-/-ATCC-MYA-565) name type common Filobasidiella-neoformans dbReference id 214684 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Basidiomycota taxon Agaricomycotina taxon Tremellomycetes taxon Tremellales taxon Cryptococcaceae taxon Cryptococcus taxon Cryptococcus-neoformans-species-complex reference key 1 citation date 2005 first 1321 last 1324 name Science type journal-article volume 307 title The-genome-of-the-basidiomycetous-yeast-and-human-pathogen-Cryptococcus-neoformans. authorList person name Loftus-B.J. person name Fung-E. person name Roncaglia-P. person name Rowley-D. person name Amedeo-P. person name Bruno-D. person name Vamathevan-J. person name Miranda-M. person name Anderson-I.J. person name Fraser-J.A. person name Allen-J.E. person name Bosdet-I.E. person name Brent-M.R. person name Chiu-R. person name Doering-T.L. person name Donlin-M.J. person name D'Souza-C.A. person name Fox-D.S. person name Grinberg-V. person name Fu-J. person name Fukushima-M. person name Haas-B.J. person name Huang-J.C. person name Janbon-G. person name Jones-S.J.M. person name Koo-H.L. person name Krzywinski-M.I. person name Kwon-Chung-K.J. person name Lengeler-K.B. person name Maiti-R. person name Marra-M.A. person name Marra-R.E. person name Mathewson-C.A. person name Mitchell-T.G. person name Pertea-M. person name Riggs-F.R. person name Salzberg-S.L. person name Schein-J.E. person name Shvartsbeyn-A. person name Shin-H. person name Shumway-M. person name Specht-C.A. person name Suh-B.B. person name Tenney-A. person name Utterback-T.R. person name Wickes-B.L. person name Wortman-J.R. person name Wye-N.H. person name Kronstad-J.W. person name Lodge-J.K. person name Heitman-J. person name Davis-R.W. person name Fraser-C.M. person name Hyman-R.W. dbReference id 15653466 type PubMed dbReference id 10.1126/science.1103773 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain JEC21-/-ATCC-MYA-565 comment type function text evidence 1 May-be-required-for-cytoplasm-to-vacuole-transport-(Cvt)-and-pexophagy. comment type subcellular-location subcellularLocation location evidence 1 Endosome-membrane topology evidence 1 Peripheral-membrane-protein subcellularLocation location evidence 1 Endomembrane-system topology evidence 1 Peripheral-membrane-protein text evidence 1 Endosome-and-other-perivacuolar-punctate-structures. comment type domain text evidence 1 The-PX-domain-binds-phosphatidylinositol-3-phosphate-which-is-necessary-for-peripheral-membrane-localization-to-the-perivacuolar-punctate-structures. comment type similarity text evidence 4 Belongs-to-the-sorting-nexin-family. dbReference id AE017343 type EMBL property type protein-sequence-ID value AAW42383.1 property type molecule-type value Genomic_DNA dbReference id XP_569690.1 type RefSeq property type nucleotide-sequence-ID value XM_569690.1 dbReference id P0CR64 type AlphaFoldDB dbReference id 5207.AAW42383 type STRING dbReference id P0CR64 type PaxDb dbReference id AAW42383 type EnsemblFungi property type protein-sequence-ID value AAW42383 property type gene-ID value CNC03560 dbReference id 3256123 type GeneID dbReference id cne:CNC03560 type KEGG dbReference id KOG2273 type eggNOG property type taxonomic-scope value Eukaryota dbReference id CLU_014456_1_1_1 type HOGENOM dbReference id P0CR64 type InParanoid dbReference id CRRMKEV type OMA dbReference id UP000002149 type Proteomes property type component value Chromosome-3 dbReference id GO:0005829 type GO property type term value C:cytosol property type evidence value ECO:0007669 property type project value GOC dbReference id GO:0010008 type GO property type term value C:endosome-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0035091 type GO property type term value F:phosphatidylinositol-binding property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0006914 type GO property type term value P:autophagy property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0015031 type GO property type term value P:protein-transport property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0042147 type GO property type term value P:retrograde-transport,-endosome-to-Golgi property type evidence value ECO:0007669 property type project value InterPro dbReference id cd07629 type CDD property type entry-name value BAR_Atg20p property type match-status value 1 dbReference id cd06867 type CDD property type entry-name value PX_SNX41_42 property type match-status value 1 dbReference id 1.20.1270.60 type Gene3D property type entry-name value Arfaptin-homology-(AH)-domain/BAR-domain property type match-status value 1 dbReference id 3.30.1520.10 type Gene3D property type entry-name value Phox-like-domain property type match-status value 1 dbReference id IPR027267 type InterPro property type entry-name value AH/BAR_dom_sf dbReference id IPR001683 type InterPro property type entry-name value PX_dom dbReference id IPR036871 type InterPro property type entry-name value PX_dom_sf dbReference id IPR044106 type InterPro property type entry-name value PX_Snx41/Atg20 dbReference id PTHR46979 type PANTHER property type entry-name value SORTING-NEXIN-41 property type match-status value 1 dbReference id PTHR46979:SF2 type PANTHER property type entry-name value SORTING-NEXIN-41 property type match-status value 1 dbReference id PF00787 type Pfam property type entry-name value PX property type match-status value 1 dbReference id SM00312 type SMART property type entry-name value PX property type match-status value 1 dbReference id SSF64268 type SUPFAM property type entry-name value PX-domain property type match-status value 1 dbReference id PS50195 type PROSITE property type entry-name value PX property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0072 Autophagy keyword id KW-0967 Endosome keyword id KW-0446 Lipid-binding keyword id KW-0472 Membrane keyword id KW-0653 Protein-transport keyword id KW-1185 Reference-proteome keyword id KW-0813 Transport feature description Sorting-nexin-41 id PRO_0000213827 type chain location begin position 1 end position 638 feature description PX evidence 2 type domain location begin position 84 end position 201 feature description Disordered evidence 3 type region-of-interest location begin position 1 end position 69 feature description Disordered evidence 3 type region-of-interest location begin position 215 end position 239 feature description Disordered evidence 3 type region-of-interest location begin position 408 end position 432 feature description Disordered evidence 3 type region-of-interest location begin position 545 end position 638 feature description Pro-residues evidence 3 type compositionally-biased-region location begin position 11 end position 32 feature description Polar-residues evidence 3 type compositionally-biased-region location begin position 217 end position 239 feature description Polar-residues evidence 3 type compositionally-biased-region location begin position 548 end position 574 feature description Basic-and-acidic-residues evidence 3 type compositionally-biased-region location begin position 576 end position 598 feature evidence 1 type binding-site location position position 118 ligand name a-1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) dbReference id CHEBI:58088 type ChEBI feature evidence 1 type binding-site location position position 120 ligand name a-1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) dbReference id CHEBI:58088 type ChEBI feature evidence 1 type binding-site location position position 144 ligand name a-1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) dbReference id CHEBI:58088 type ChEBI feature evidence 1 type binding-site location position position 168 ligand name a-1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) dbReference id CHEBI:58088 type ChEBI evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000255 source dbReference id PRU00147 type PROSITE-ProRule evidence key 3 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 4 type ECO:0000305 sequence checksum ADD408ED8DE4248A length 638 mass 70714 modified 2011-06-28 version 1 MDSDTSPNPFASSPPSSPSPRPSLPPPVPRKPSSLVSAASGSPPPTHRASFPDPARHPKMGATVPGPKPKTGYCCSIDKDISAGEQVHIVDALKTTEGGTASYITYVIRLGTHTVRRRYSAFLSLHQSLTGLYPVLIIPPIPSKQSLTDYAVKGQSKAREDATIIARRKRLLEDFLQRLIRHPILGGEHVLHRFLEEDVSWSEVLHSPPISLLSKNPLHAPSHNPTFQPTTPTSPSEAPATTSYIAHHLLPTPSPSHPLRQPDQRFMDSEAFTEKFQSHFSGTMEKVNRRVTKRWGERAHDMSELGGIWNGFSLVEQGKLGDAIEKVGRAVDAEYLATAALLQSWEKTTTEPLHIYSQFATLIRARLSFRHQKHVQYELVQEALETQRDKLEILENAEREARRLEEALERGGSVLASPQLEPEAARDERERAQRRARASQGFGLLSAVKHSLSGMIDMDPEATRRANIAKTRDNISQLEDSYQAAAQDLKYASMTLQADLDRFQRQKVADLREMAINLSQVHRDWCKQNLEAWKAAQAAVREIDPHPNRPAQTQTQVQSQQSHAGPSTLHAQTEDDVSKLGVDAMKNEIERVEIEIADKPLPKPSLAETGGDGVVPSPQPRQENDTEEQEGHGPLGPL 
entry created 2011-06-28 dataset Swiss-Prot modified 2023-02-22 version 55 accession P0CO51 accession Q55MT9 accession Q5KB66 name KU70_CRYNB protein recommendedName fullName ATP-dependent-DNA-helicase-II-subunit-1 ecNumber 3.6.4.12 alternativeName fullName ATP-dependent-DNA-helicase-II-subunit-Ku70 gene name type primary KU70 name type ordered-locus CNBH3450 organism name type scientific Cryptococcus-neoformans-var.-neoformans-serotype-D-(strain-B-3501A) name type common Filobasidiella-neoformans dbReference id 283643 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Basidiomycota taxon Agaricomycotina taxon Tremellomycetes taxon Tremellales taxon Cryptococcaceae taxon Cryptococcus taxon Cryptococcus-neoformans-species-complex reference key 1 citation date 2005 first 1321 last 1324 name Science type journal-article volume 307 title The-genome-of-the-basidiomycetous-yeast-and-human-pathogen-Cryptococcus-neoformans. authorList person name Loftus-B.J. person name Fung-E. person name Roncaglia-P. person name Rowley-D. person name Amedeo-P. person name Bruno-D. person name Vamathevan-J. person name Miranda-M. person name Anderson-I.J. person name Fraser-J.A. person name Allen-J.E. person name Bosdet-I.E. person name Brent-M.R. person name Chiu-R. person name Doering-T.L. person name Donlin-M.J. person name D'Souza-C.A. person name Fox-D.S. person name Grinberg-V. person name Fu-J. person name Fukushima-M. person name Haas-B.J. person name Huang-J.C. person name Janbon-G. person name Jones-S.J.M. person name Koo-H.L. person name Krzywinski-M.I. person name Kwon-Chung-K.J. person name Lengeler-K.B. person name Maiti-R. person name Marra-M.A. person name Marra-R.E. person name Mathewson-C.A. person name Mitchell-T.G. person name Pertea-M. person name Riggs-F.R. person name Salzberg-S.L. person name Schein-J.E. person name Shvartsbeyn-A. person name Shin-H. person name Shumway-M. person name Specht-C.A. person name Suh-B.B. person name Tenney-A. person name Utterback-T.R. person name Wickes-B.L. person name Wortman-J.R. person name Wye-N.H. person name Kronstad-J.W. person name Lodge-J.K. person name Heitman-J. person name Davis-R.W. person name Fraser-C.M. person name Hyman-R.W. dbReference id 15653466 type PubMed dbReference id 10.1126/science.1103773 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain B-3501A comment type function text evidence 1 Single-stranded-DNA-dependent-ATP-dependent-helicase.-Involved-in-non-homologous-end-joining-(NHEJ)-DNA-double-strand-break-repair.-DNA-binding-is-sequence-independent-but-has-a-high-affinity-to-nicks-in-double-stranded-DNA-and-to-the-ends-of-duplex-DNA.-Binds-to-naturally-occurring-chromosomal-ends,-and-therefore-provides-chromosomal-end-protection.-Required-also-for-telomere-recombination-to-repair-telomeric-ends-in-the-absence-of-telomerase.-KU70,-of-the-KU70/KU80-heterodimer,-binds-to-the-stem-loop-of-TLC1,-the-RNA-component-of-telomerase.-Involved-in-telomere-maintenance.-Interacts-with-telomeric-repeats-and-subtelomeric-sequences-thereby-controlling-telomere-length-and-protecting-against-subtelomeric-rearrangement.-Maintains-telomeric-chromatin,-which-is-involved-in-silencing-the-expression-of-genes-located-at-the-telomere.-Required-for-mating-type-switching-(By-similarity). comment type catalytic-activity reaction text ATP-+-H2O-=-ADP-+-H(+)-+-phosphate dbReference id RHEA:13065 type Rhea dbReference id CHEBI:15377 type ChEBI dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:30616 type ChEBI dbReference id CHEBI:43474 type ChEBI dbReference id CHEBI:456216 type ChEBI dbReference id 3.6.4.12 type EC comment type subunit text evidence 1 Heterodimer-of-Ku70-and-Ku80. comment type subcellular-location subcellularLocation location evidence 1 Nucleus subcellularLocation location evidence 1 Chromosome location evidence 1 Telomere comment type similarity text evidence 3 Belongs-to-the-ku70-family. comment evidence 3 type sequence-caution conflict type erroneous-gene-model-prediction sequence id EAL19246 resource EMBL-CDS version 1 dbReference id 3.6.4.12 type EC dbReference id AAEY01000042 type EMBL property type protein-sequence-ID value EAL19246.1 property type status value ALT_SEQ property type molecule-type value Genomic_DNA dbReference id XP_773893.1 type RefSeq property type nucleotide-sequence-ID value XM_768800.1 dbReference id P0CO51 type AlphaFoldDB dbReference id P0CO51 type SMR dbReference id 4937872 type GeneID dbReference id cnb:CNBH3450 type KEGG dbReference id CLU_014815_3_0_1 type HOGENOM dbReference id 21093at2759 type OrthoDB dbReference id UP000001435 type Proteomes property type component value Chromosome-8 dbReference id GO:0000781 type GO property type term value C:chromosome,-telomeric-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0043564 type GO property type term value C:Ku70:Ku80-complex property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0005524 type GO property type term value F:ATP-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0016887 type GO property type term value F:ATP-hydrolysis-activity property type evidence value ECO:0007669 property type project value RHEA dbReference id GO:0003684 type GO property type term value F:damaged-DNA-binding property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0003678 type GO property type term value F:DNA-helicase-activity property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0042162 type GO property type term value F:telomeric-DNA-binding property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0006310 type GO property type term value P:DNA-recombination property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0006303 type GO property type term value P:double-strand-break-repair-via-nonhomologous-end-joining property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0000723 type GO property type term value P:telomere-maintenance property type evidence value ECO:0007669 property type project value InterPro dbReference id cd00788 type CDD property type entry-name value KU70 property type match-status value 1 dbReference id 1.10.1600.10 type Gene3D property type match-status value 1 dbReference id 2.40.290.10 type Gene3D property type match-status value 1 dbReference id 3.40.50.410 type Gene3D property type entry-name value von-Willebrand-factor,-type-A-domain property type match-status value 1 dbReference id IPR006165 type InterPro property type entry-name value Ku70 dbReference id IPR006164 type InterPro property type entry-name value Ku70/Ku80_beta-barrel_dom dbReference id IPR005160 type InterPro property type entry-name value Ku_C dbReference id IPR005161 type InterPro property type entry-name value Ku_N dbReference id IPR016194 type InterPro property type entry-name value SPOC-like_C_dom_sf dbReference id IPR036465 type InterPro property type entry-name value vWFA_dom_sf dbReference id PTHR12604 type PANTHER property type entry-name value KU-AUTOANTIGEN-DNA-HELICASE property type match-status value 1 dbReference id PTHR12604:SF2 type PANTHER property type entry-name value X-RAY-REPAIR-CROSS-COMPLEMENTING-PROTEIN-6 property type match-status value 1 dbReference id PF02735 type Pfam property type entry-name value Ku property type match-status value 1 dbReference id PF03730 type Pfam property type entry-name value Ku_C property type match-status value 1 dbReference id PF03731 type Pfam property type entry-name value Ku_N property type match-status value 1 dbReference id PIRSF003033 type PIRSF property type entry-name value Ku70 property type match-status value 1 dbReference id SM00559 type SMART property type entry-name value Ku78 property type match-status value 1 dbReference id SSF100939 type SUPFAM property type entry-name value SPOC-domain-like property type match-status value 1 dbReference id SSF53300 type SUPFAM property type entry-name value vWA-like property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0067 ATP-binding keyword id KW-0158 Chromosome keyword id KW-0227 DNA-damage keyword id KW-0233 DNA-recombination keyword id KW-0234 DNA-repair keyword id KW-0238 DNA-binding keyword id KW-0347 Helicase keyword id KW-0378 Hydrolase keyword id KW-0547 Nucleotide-binding keyword id KW-0539 Nucleus keyword id KW-0779 Telomere feature description ATP-dependent-DNA-helicase-II-subunit-1 id PRO_0000410130 type chain location begin position 1 end position 560 feature description Ku type domain location begin position 224 end position 413 feature description Disordered evidence 2 type region-of-interest location begin position 541 end position 560 evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 3 type ECO:0000305 sequence checksum 082D9D300EFE4667 length 560 mass 63992 modified 2011-06-28 version 1 MSSYYNKGDAPSWEALDQDGLDDVIDTSEPSAVAEDPGNYQPGNYVFQTLRTINAEEMKRLVKLMQTAKEQYEAQDDDETVETTEPEILRKTFPPIEESHEMNIANVIQTCNFLFRDGGTQLRGNKRVFWITDNDMPPGMNNRQPARTSYGDLTTYGVTAETFFIDRPDHRFNPNIFWNDILDREAIDYNDDQPDPEGLSSLADLMKDLVIKTSPKRTHFHVPLKLGKDGEIVIGVSGCSMVSEQGKGASRYVKMRGQVVEEVQSKTEYTSAKSLNSGQWGSNPIKVLGFQAASQLRFQDNLKHPFFIYPNEEEYTGSTRTFAALLNSCLKYNRHALALCRLRSNHVPEFCVLIPQEEKTSSNGQEYPPGFHLIILPYKDSIRPPPKKVAEFLQSPPIATDEQINAMKAVIKRTRFKAAAYRPEIYPNPSLAYHYDQLQALAFEEDWDPEDPAKQALDKTMPLYGGMHSRAGEFMEEFNKEIENDERAVEKLAAPTKRGKAEKETTVNEWDLRNIPDMWKKGTLSQLSILARLRLRRRPFTGQNQKGGYHRRRIRTSFHK 
entry created 2011-10-19 dataset Swiss-Prot modified 2023-02-22 version 43 accession Q8GT66 accession Q9SC41 name TIC40_PEA protein recommendedName fullName Protein-TIC-40,-chloroplastic alternativeName fullName Translocon-at-the-inner-envelope-membrane-of-chloroplasts-40 shortName PsTIC40 gene name type primary TIC40 organism name type scientific Pisum-sativum name type common Garden-pea dbReference id 3888 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon eudicotyledons taxon Gunneridae taxon Pentapetalae taxon rosids taxon fabids taxon Fabales taxon Fabaceae taxon Papilionoideae taxon 50-kb-inversion-clade taxon NPAAA-clade taxon Hologalegina taxon IRL-clade taxon Fabeae taxon Pisum reference key 1 citation date 1999 first 37467 last 37472 name J.-Biol.-Chem. type journal-article volume 274 title Tic40,-a-new-'old'-subunit-of-the-chloroplast-protein-import-translocon. authorList person name Stahl-T. person name Glockmann-C. person name Soll-J. person name Heins-L. dbReference id 10601321 type PubMed dbReference id 10.1074/jbc.274.52.37467 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope PROTEIN-SEQUENCE-OF-73-98 scope FUNCTION scope SUBCELLULAR-LOCATION scope INTERACTION-WITH-TIC110 source strain cv.-Golf tissue Leaf reference key 2 citation date 2003 first 2970 last 2980 name EMBO-J. type journal-article volume 22 title Tic40,-a-membrane-anchored-co-chaperone-homolog-in-the-chloroplast-protein-translocon. authorList person name Chou-M.L. person name Fitzpatrick-L.M. person name Tu-S.L. person name Budziszewski-G. person name Potter-Lewis-S. person name Akita-M. person name Levin-J.Z. person name Keegstra-K. person name Li-H.M. dbReference id 12805212 type PubMed dbReference id 10.1093/emboj/cdg281 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope SUBCELLULAR-LOCATION scope TOPOLOGY scope INTERACTION-WITH-HSP93;-TIC110-AND-TOC75 source strain cv.-Little-Marvel reference key 3 citation date 2002 first 6136 last 6145 name EMBO-J. type journal-article volume 21 title Protein-import-into-chloroplasts-involves-redox-regulated-proteins. authorList person name Kuechler-M. person name Decker-S. person name Hoermann-F. person name Soll-J. person name Heins-L. dbReference id 12426385 type PubMed dbReference id 10.1093/emboj/cdf621 type DOI scope INTERACTION-WITH-TIC62 reference key 4 citation date 2006 first 893 last 900 name J.-Cell-Biol. type journal-article volume 175 title Stimulation-of-transit-peptide-release-and-ATP-hydrolysis-by-a-cochaperone-during-protein-import-into-chloroplasts. authorList person name Chou-M.L. person name Chu-C.C. person name Chen-L.J. person name Akita-M. person name Li-H.M. dbReference id 17158958 type PubMed dbReference id 10.1083/jcb.200609172 type DOI scope FUNCTION scope INTERACTION-WITH-TIC110-AND-HSP93 reference key 5 citation date 2009 first 1050 last 1061 name Plant-Physiol. type journal-article volume 150 title Role-of-temperature-stress-on-chloroplast-biogenesis-and-protein-import-in-pea. authorList person name Dutta-S. person name Mohanty-S. person name Tripathy-B.C. dbReference id 19403728 type PubMed dbReference id 10.1104/pp.109.137265 type DOI scope INDUCTION-BY-COLD reference key 6 citation date 2010 first 740 last 747 name Biochim.-Biophys.-Acta type journal-article volume 1803 title Protein-import-into-chloroplasts:-the-Tic-complex-and-its-regulation. authorList person name Kovacs-Bogdan-E. person name Soll-J. person name Bolter-B. dbReference id 20100520 type PubMed dbReference id 10.1016/j.bbamcr.2010.01.015 type DOI scope REVIEW comment type function text evidence 3-6 Involved-in-protein-precursor-import-into-chloroplasts.-Part-of-the-motor-complex-consisting-of-a-co-chaperone-(TIC40)-and-a-chaperone-(HSP93)-associated-with-the-import-channel-(TIC110).-Causes-the-release-of-bound-transit-peptides-from-TIC110-and-stimulates-ATP-hydrolysis-by-HSP93.-Involved-in-reinsertion-of-proteins-from-the-chloroplast-stroma-into-the-inner-membrane. comment type subunit text evidence 3-4-5-6 Part-of-the-Tic-complex.-Interacts-with-HSP93,-TIC110,-TIC62-and-TOC75. comment type subcellular-location subcellularLocation location evidence 3-5 Plastid location evidence 3-5 Chloroplast-inner-membrane topology evidence 3-5 Single-pass-membrane-protein comment type induction text evidence 7 Down-regulated-by-cold-stress. comment type domain text The-STI1-2-domain-(373-412)-has-a-stimulatory-effect-on-HSP93-ATP-hydrolysis. comment type miscellaneous text Inserts-into-the-inner-envelope-membrane-from-the-stroma-after-import-from-the-cytoplasm.-The-transit-peptide-undergoes-a-two-step-processing.-The-initial-cleavage-to-generate-the-intermediate-found-in-the-stroma-is-mediated-by-the-stromal-processing-peptidase-(SPP)-while-the-final-processing-step-by-a-signal-peptidase-I-type-(SPase-I),-possibly-PLSP1,-requires-association-with-the-inner-membrane. dbReference id AJ243758 type EMBL property type protein-sequence-ID value CAB50925.1 property type molecule-type value mRNA dbReference id AY157668 type EMBL property type protein-sequence-ID value AAN75219.1 property type molecule-type value mRNA dbReference id Q8GT66 type AlphaFoldDB dbReference id Q8GT66 type SMR dbReference id Q8GT66 type IntAct property type interactions value 2 dbReference id 3.A.9.1.1 type TCDB property type family-name value the-chloroplast-envelope-protein-translocase-(cept-or-tic-toc)-family dbReference id GO:0009706 type GO property type term value C:chloroplast-inner-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0015031 type GO property type term value P:protein-transport property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 1.10.260.100 type Gene3D property type match-status value 1 dbReference id IPR041243 type InterPro property type entry-name value STI1/HOP_DP dbReference id IPR006636 type InterPro property type entry-name value STI1_HS-bd dbReference id PTHR47296 type PANTHER property type entry-name value PROTEIN-TIC-40,-CHLOROPLASTIC property type match-status value 1 dbReference id PTHR47296:SF1 type PANTHER property type entry-name value PROTEIN-TIC-40,-CHLOROPLASTIC property type match-status value 1 dbReference id PF17830 type Pfam property type entry-name value STI1 property type match-status value 1 dbReference id SM00727 type SMART property type entry-name value STI1 property type match-status value 2 proteinExistence type evidence-at-protein-level keyword id KW-0150 Chloroplast keyword id KW-0903 Direct-protein-sequencing keyword id KW-0472 Membrane keyword id KW-0934 Plastid keyword id KW-1001 Plastid-inner-membrane keyword id KW-0653 Protein-transport keyword id KW-0677 Repeat keyword id KW-0809 Transit-peptide keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix keyword id KW-0813 Transport feature description Chloroplast evidence 1 type transit-peptide location begin position 1 end position 39 feature description Chloroplast;-inner-membrane evidence 1 type transit-peptide location begin position 40 end position 72 feature description Protein-TIC-40,-chloroplastic id PRO_0000413674 type chain location begin position 73 end position 436 feature description Chloroplast-intermembrane evidence 1 type topological-domain location begin position 73 end position 98 feature description Helical evidence 1 type transmembrane-region location begin position 99 end position 119 feature description Stromal evidence 1 type topological-domain location begin position 120 end position 436 feature description STI1-1 type domain location begin position 297 end position 331 feature description STI1-2 type domain location begin position 373 end position 412 feature description Disordered evidence 2 type region-of-interest location begin position 74 end position 95 feature description Disordered evidence 2 type region-of-interest location begin position 160 end position 191 feature description Disordered evidence 2 type region-of-interest location begin position 245 end position 285 feature description Polar-residues evidence 2 type compositionally-biased-region location begin position 74 end position 88 feature description Polar-residues evidence 2 type compositionally-biased-region location begin position 170 end position 191 feature description Polar-residues evidence 2 type compositionally-biased-region location begin position 263 end position 284 feature description In-Ref.-1;-CAB50925. evidence 8 ref 1 type sequence-conflict original G variation R location position position 28 feature description In-Ref.-1;-CAB50925. evidence 8 ref 1 type sequence-conflict original D variation S location position position 70 feature description In-Ref.-1;-CAB50925. evidence 8 ref 1 type sequence-conflict original S variation G location position position 277 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 3 type ECO:0000269 source dbReference id 10601321 type PubMed evidence key 4 type ECO:0000269 source dbReference id 12426385 type PubMed evidence key 5 type ECO:0000269 source dbReference id 12805212 type PubMed evidence key 6 type ECO:0000269 source dbReference id 17158958 type PubMed evidence key 7 type ECO:0000269 source dbReference id 19403728 type PubMed evidence key 8 type ECO:0000305 sequence checksum B9C18DE99BC93EC7 length 436 mass 47172 modified 2003-03-01 precursor true version 1 MENLNLALVSSPKPLLLGHSSSKNVFSGRKSFTFGTFRVSANSSSSHVTRAASKSHQNLKSVQGKVNAHDFASISSSNGQETTSVGVSPQLSPPPPSTVGSPLFWIGIGVGFSALFSVVASRVKKYAMQQAFKSMMGQMNTQNNPFDSGAFSSGPPFPFPMPSASGPATPAGFAGNQSQATSTRSASQSTVTVDIPATKVEAAAPAPDINVKEEVEVKNEPKKSAFVDVSPEETVQKNAFERFKDVDESSSFKEARAPAEASQNGTPFKQGFGDSPSSPSERKSALSVDALEKMMEDPTVQQMVYPYLPEEMRNPSTFKWMMQNPEYRQQLEAMLNNMGGGTEWDSRMMDTLKNFDLNSPDVKQQFDQIGLSPQEVISKIMANPDVAMAFQNPRVQAAIMDCSQNPMSIVKYQNDKEVMDVFNKISELFPGVSGPP 
entry created 2012-03-21 dataset Swiss-Prot modified 2023-02-22 version 105 accession O29808 name QUEE_ARCFU protein recommendedName fullName evidence 1 7-carboxy-7-deazaguanine-synthase shortName evidence 1 CDG-synthase ecNumber evidence 1 4.3.99.3 alternativeName fullName evidence 1 Archaeosine-biosynthesis-protein-QueE gene name evidence 1 type primary queE name type ordered-locus AF_0441 organism name type scientific Archaeoglobus-fulgidus-(strain-ATCC-49558-/-DSM-4304-/-JCM-9628-/-NBRC-100126-/-VC-16) dbReference id 224325 type NCBI-Taxonomy lineage taxon Archaea taxon Euryarchaeota taxon Archaeoglobi taxon Archaeoglobales taxon Archaeoglobaceae taxon Archaeoglobus reference key 1 citation date 1997 first 364 last 370 name Nature type journal-article volume 390 title The-complete-genome-sequence-of-the-hyperthermophilic,-sulphate-reducing-archaeon-Archaeoglobus-fulgidus. authorList person name Klenk-H.-P. person name Clayton-R.A. person name Tomb-J.-F. person name White-O. person name Nelson-K.E. person name Ketchum-K.A. person name Dodson-R.J. person name Gwinn-M.L. person name Hickey-E.K. person name Peterson-J.D. person name Richardson-D.L. person name Kerlavage-A.R. person name Graham-D.E. person name Kyrpides-N.C. person name Fleischmann-R.D. person name Quackenbush-J. person name Lee-N.H. person name Sutton-G.G. person name Gill-S.R. person name Kirkness-E.F. person name Dougherty-B.A. person name McKenney-K. person name Adams-M.D. person name Loftus-B.J. person name Peterson-S.N. person name Reich-C.I. person name McNeil-L.K. person name Badger-J.H. person name Glodek-A. person name Zhou-L. person name Overbeek-R. person name Gocayne-J.D. person name Weidman-J.F. person name McDonald-L.A. person name Utterback-T.R. person name Cotton-M.D. person name Spriggs-T. person name Artiach-P. person name Kaine-B.P. person name Sykes-S.M. person name Sadow-P.W. person name D'Andrea-K.P. person name Bowman-C. person name Fujii-C. person name Garland-S.A. person name Mason-T.M. person name Olsen-G.J. person name Fraser-C.M. person name Smith-H.O. person name Woese-C.R. person name Venter-J.C. dbReference id 9389475 type PubMed dbReference id 10.1038/37052 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-49558-/-DSM-4304-/-JCM-9628-/-NBRC-100126-/-VC-16 comment type function text evidence 1 Catalyzes-the-complex-heterocyclic-radical-mediated-conversion-of-6-carboxy-5,6,7,8-tetrahydropterin-(CPH4)-to-7-carboxy-7-deazaguanine-(CDG),-a-step-common-to-the-biosynthetic-pathways-of-all-7-deazapurine-containing-compounds. comment type catalytic-activity reaction evidence 1 text 6-carboxy-5,6,7,8-tetrahydropterin-+-H(+)-=-7-carboxy-7-deazaguanine-+-NH4(+) dbReference id RHEA:27974 type Rhea dbReference id CHEBI:15378 type ChEBI dbReference id CHEBI:28938 type ChEBI dbReference id CHEBI:61032 type ChEBI dbReference id CHEBI:61036 type ChEBI dbReference id 4.3.99.3 type EC comment type cofactor cofactor evidence 1 name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI text evidence 1 Binds-1-[4Fe-4S]-cluster.-The-cluster-is-coordinated-with-3-cysteines-and-an-exchangeable-S-adenosyl-L-methionine. comment type cofactor cofactor evidence 1 name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI text evidence 1 Binds-1-S-adenosyl-L-methionine-per-subunit. comment type cofactor cofactor evidence 1 name Mg(2+) dbReference id CHEBI:18420 type ChEBI comment type pathway text evidence 1 Purine-metabolism;-7-cyano-7-deazaguanine-biosynthesis. comment type subunit text evidence 1 Homodimer. comment type similarity text evidence 1 Belongs-to-the-radical-SAM-superfamily.-7-carboxy-7-deazaguanine-synthase-family. dbReference evidence 1 id 4.3.99.3 type EC dbReference id AE000782 type EMBL property type protein-sequence-ID value AAB90793.1 property type molecule-type value Genomic_DNA dbReference id A69305 type PIR property type entry-name value A69305 dbReference id WP_010877948.1 type RefSeq property type nucleotide-sequence-ID value NC_000917.1 dbReference id O29808 type AlphaFoldDB dbReference id O29808 type SMR dbReference id 224325.AF_0441 type STRING dbReference id 1483657 type DNASU dbReference id AAB90793 type EnsemblBacteria property type protein-sequence-ID value AAB90793 property type gene-ID value AF_0441 dbReference id 24793978 type GeneID dbReference id afu:AF_0441 type KEGG dbReference id arCOG02173 type eggNOG property type taxonomic-scope value Archaea dbReference id CLU_066739_1_0_2 type HOGENOM dbReference id IPQTHKM type OMA dbReference id 7980at2157 type OrthoDB dbReference id O29808 type PhylomeDB dbReference id UPA00391 type UniPathway dbReference id UP000002199 type Proteomes property type component value Chromosome dbReference id GO:0051539 type GO property type term value F:4-iron,-4-sulfur-cluster-binding property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0016840 type GO property type term value F:carbon-nitrogen-lyase-activity property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0000287 type GO property type term value F:magnesium-ion-binding property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:1904047 type GO property type term value F:S-adenosyl-L-methionine-binding property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id cd01335 type CDD property type entry-name value Radical_SAM property type match-status value 1 dbReference id 3.20.20.70 type Gene3D property type entry-name value Aldolase-class-I property type match-status value 1 dbReference id MF_00917 type HAMAP property type entry-name value QueE property type match-status value 1 dbReference id IPR024924 type InterPro property type entry-name value 7-CO-7-deazaguanine_synth-like dbReference id IPR013785 type InterPro property type entry-name value Aldolase_TIM dbReference id IPR007197 type InterPro property type entry-name value rSAM dbReference id PTHR42836 type PANTHER property type entry-name value 7-CARBOXY-7-DEAZAGUANINE-SYNTHASE property type match-status value 1 dbReference id PTHR42836:SF1 type PANTHER property type entry-name value 7-CARBOXY-7-DEAZAGUANINE-SYNTHASE property type match-status value 1 dbReference id PF13353 type Pfam property type entry-name value Fer4_12 property type match-status value 1 dbReference id PF04055 type Pfam property type entry-name value Radical_SAM property type match-status value 1 dbReference id PIRSF000370 type PIRSF property type entry-name value QueE property type match-status value 1 dbReference id SFLDS00029 type SFLD property type entry-name value Radical_SAM property type match-status value 1 dbReference id SSF102114 type SUPFAM property type entry-name value Radical-SAM-enzymes property type match-status value 1 dbReference id PS51918 type PROSITE property type entry-name value RADICAL_SAM property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0004 4Fe-4S keyword id KW-0408 Iron keyword id KW-0411 Iron-sulfur keyword id KW-0456 Lyase keyword id KW-0460 Magnesium keyword id KW-0479 Metal-binding keyword id KW-1185 Reference-proteome keyword id KW-0949 S-adenosyl-L-methionine feature description 7-carboxy-7-deazaguanine-synthase id PRO_0000416215 type chain location begin position 1 end position 225 feature description Radical-SAM-core evidence 2 type domain location begin position 18 end position 225 feature evidence 1 type binding-site location begin position 12 end position 14 ligand name substrate feature evidence 1 type binding-site location position position 27 ligand name substrate feature evidence 1 type binding-site location position position 31 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI note 4Fe-4S-S-AdoMet feature evidence 1 type binding-site location position position 35 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI note 4Fe-4S-S-AdoMet feature evidence 1 type binding-site location position position 38 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI note 4Fe-4S-S-AdoMet feature evidence 1 type binding-site location position position 40 ligand name Mg(2+) dbReference id CHEBI:18420 type ChEBI feature evidence 1 type binding-site location position position 80 ligand name substrate feature evidence 1 type binding-site location position position 82 ligand name S-adenosyl-L-methionine dbReference id CHEBI:59789 type ChEBI evidence key 1 type ECO:0000255 source dbReference id MF_00917 type HAMAP-Rule evidence key 2 type ECO:0000255 source dbReference id PRU01266 type PROSITE-ProRule sequence checksum 27A28FB3CCE2188A length 225 mass 25873 modified 1998-01-01 version 1 MRANLIEIFESIQGEGFYIGVRQLFVRFAGCNLNCYYCDTPKTSENCLDLTANRTLKNPVSAEYVQGRIDSSKVHSVCFTGGEPMLQAEFIASLSKTHPFYLESNMTLPEKAKKLKFCDYVAGDLKVREAGLKNYDEVFQKTVKCFKVLRNTRRRKTFCKIVLPDKFDADEVLNSAYEIKNYVFGFVLQPVFGSRVEKILKLQKRMIDFADTRVIPQVHKYLGVR 
entry created 2012-03-21 dataset Swiss-Prot modified 2023-02-22 version 58 accession E4RUV9 name QUEG_LEAB4 protein recommendedName fullName evidence 1 Epoxyqueuosine-reductase ecNumber evidence 1 1.17.99.6 alternativeName fullName evidence 1 Queuosine-biosynthesis-protein-QueG gene name evidence 1 type primary queG name type ordered-locus Lbys_1262 organism name type scientific Leadbetterella-byssophila-(strain-DSM-17132-/-JCM-16389-/-KACC-11308-/-NBRC-106382-/-4M15) dbReference id 649349 type NCBI-Taxonomy lineage taxon Bacteria taxon Bacteroidota taxon Cytophagia taxon Cytophagales taxon Spirosomaceae taxon Leadbetterella reference key 1 citation date 2011 first 2 last 12 name Stand.-Genomic-Sci. type journal-article volume 4 title Complete-genome-sequence-of-Leadbetterella-byssophila-type-strain-(4M15). authorList person name Abt-B. person name Teshima-H. person name Lucas-S. person name Lapidus-A. person name Del-Rio-T.G. person name Nolan-M. person name Tice-H. person name Cheng-J.F. person name Pitluck-S. person name Liolios-K. person name Pagani-I. person name Ivanova-N. person name Mavromatis-K. person name Pati-A. person name Tapia-R. person name Han-C. person name Goodwin-L. person name Chen-A. person name Palaniappan-K. person name Land-M. person name Hauser-L. person name Chang-Y.J. person name Jeffries-C.D. person name Rohde-M. person name Goker-M. person name Tindall-B.J. person name Detter-J.C. person name Woyke-T. person name Bristow-J. person name Eisen-J.A. person name Markowitz-V. person name Hugenholtz-P. person name Klenk-H.P. person name Kyrpides-N.C. dbReference id 21475582 type PubMed dbReference id 10.4056/sigs.1413518 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain DSM-17132-/-JCM-16389-/-KACC-11308-/-NBRC-106382-/-4M15 comment type function text evidence 1 Catalyzes-the-conversion-of-epoxyqueuosine-(oQ)-to-queuosine-(Q),-which-is-a-hypermodified-base-found-in-the-wobble-positions-of-tRNA(Asp),-tRNA(Asn),-tRNA(His)-and-tRNA(Tyr). comment type catalytic-activity reaction evidence 1 text AH2-+-epoxyqueuosine(34)-in-tRNA-=-A-+-H2O-+-queuosine(34)-in-tRNA dbReference id RHEA:32159 type Rhea dbReference id RHEA-COMP:10345 type Rhea dbReference id RHEA-COMP:10346 type Rhea dbReference id CHEBI:13193 type ChEBI dbReference id CHEBI:15377 type ChEBI dbReference id CHEBI:17499 type ChEBI dbReference id CHEBI:82831 type ChEBI dbReference id CHEBI:82834 type ChEBI dbReference id 1.17.99.6 type EC comment type cofactor cofactor evidence 1 name cob(II)alamin dbReference id CHEBI:16304 type ChEBI comment type cofactor cofactor evidence 1 name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI text evidence 1 Binds-2-[4Fe-4S]-clusters-per-monomer. comment type pathway text evidence 1 tRNA-modification;-tRNA-queuosine-biosynthesis. comment type subunit text evidence 1 Monomer. comment type subcellular-location subcellularLocation location evidence 1 Cytoplasm comment type similarity text evidence 1 Belongs-to-the-QueG-family. dbReference evidence 1 id 1.17.99.6 type EC dbReference id CP002305 type EMBL property type protein-sequence-ID value ADQ16982.1 property type molecule-type value Genomic_DNA dbReference id WP_013408032.1 type RefSeq property type nucleotide-sequence-ID value NC_014655.1 dbReference id E4RUV9 type AlphaFoldDB dbReference id E4RUV9 type SMR dbReference id 649349.Lbys_1262 type STRING dbReference id ADQ16982 type EnsemblBacteria property type protein-sequence-ID value ADQ16982 property type gene-ID value Lbys_1262 dbReference id lby:Lbys_1262 type KEGG dbReference id COG1600 type eggNOG property type taxonomic-scope value Bacteria dbReference id CLU_030790_0_0_10 type HOGENOM dbReference id ICDTDLS type OMA dbReference id 9784571at2 type OrthoDB dbReference id UPA00392 type UniPathway dbReference id UP000007435 type Proteomes property type component value Chromosome dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0051539 type GO property type term value F:4-iron,-4-sulfur-cluster-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0052693 type GO property type term value F:epoxyqueuosine-reductase-activity property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0046872 type GO property type term value F:metal-ion-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0008616 type GO property type term value P:queuosine-biosynthetic-process property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id GO:0008033 type GO property type term value P:tRNA-processing property type evidence value ECO:0007669 property type project value UniProtKB-UniRule dbReference id 3.30.70.20 type Gene3D property type match-status value 1 dbReference id MF_00916 type HAMAP property type entry-name value QueG property type match-status value 1 dbReference id IPR017896 type InterPro property type entry-name value 4Fe4S_Fe-S-bd dbReference id IPR017900 type InterPro property type entry-name value 4Fe4S_Fe_S_CS dbReference id IPR004453 type InterPro property type entry-name value QueG dbReference id IPR013542 type InterPro property type entry-name value QueG_DUF1730 dbReference id PTHR30002 type PANTHER property type entry-name value EPOXYQUEUOSINE-REDUCTASE property type match-status value 1 dbReference id PTHR30002:SF4 type PANTHER property type entry-name value EPOXYQUEUOSINE-REDUCTASE property type match-status value 1 dbReference id PF13484 type Pfam property type entry-name value Fer4_16 property type match-status value 1 dbReference id PF08331 type Pfam property type entry-name value QueG_DUF1730 property type match-status value 1 dbReference id SSF46548 type SUPFAM property type entry-name value alpha-helical-ferredoxin property type match-status value 1 dbReference id TIGR00276 type TIGRFAMs property type entry-name value epoxyqueuosine-reductase property type match-status value 1 dbReference id PS00198 type PROSITE property type entry-name value 4FE4S_FER_1 property type match-status value 1 dbReference id PS51379 type PROSITE property type entry-name value 4FE4S_FER_2 property type match-status value 2 proteinExistence type inferred-from-homology keyword id KW-0004 4Fe-4S keyword id KW-0963 Cytoplasm keyword id KW-0408 Iron keyword id KW-0411 Iron-sulfur keyword id KW-0479 Metal-binding keyword id KW-0560 Oxidoreductase keyword id KW-0671 Queuosine-biosynthesis keyword id KW-1185 Reference-proteome keyword id KW-0677 Repeat keyword id KW-0819 tRNA-processing feature description Epoxyqueuosine-reductase id PRO_0000416074 type chain location begin position 1 end position 302 feature description 4Fe-4S-ferredoxin-type-1 evidence 1 type domain location begin position 170 end position 202 feature description 4Fe-4S-ferredoxin-type-2 evidence 1 type domain location begin position 221 end position 251 feature description Proton-donor evidence 1 type active-site location position position 128 feature evidence 1 type binding-site location position position 182 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI label 1 feature evidence 1 type binding-site location position position 185 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI label 1 feature evidence 1 type binding-site location position position 188 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI label 1 feature evidence 1 type binding-site location position position 192 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI label 2 feature evidence 1 type binding-site location position position 207 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI label 2 feature evidence 1 type binding-site location position position 234 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI label 2 feature evidence 1 type binding-site location position position 237 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI label 2 feature evidence 1 type binding-site location position position 241 ligand name [4Fe-4S]-cluster dbReference id CHEBI:49883 type ChEBI label 1 evidence key 1 type ECO:0000255 source dbReference id MF_00916 type HAMAP-Rule sequence checksum 2F7B67A4CE33D186 length 302 mass 34760 modified 2011-02-08 version 1 MRDYSKEIKSWAAELGFDFCGISAADFLEEEAPRLERWLNRNYHGKMAYMANHFDKRLDPRKLVDGAKSVVSLLLNYYPEEPLDASPYKISKYAYGKDYHYVIKDKLKLLFERIQKEIGEVGGRIFVDSAPVMDKIWAKKAGLGWVGKNSNLINRKMGSFFFIAELILDLPLQADGPIRDYCGTCTACIDACPTDAITPYEVDGSKCISYLTIELKDQIPNEFKGKMENWIFGCDICQDVCPWNSFARPHSTEEFYPNENLKTFQDWDEITSEIFSHLFKKSAVERTKLEGLKRNIAFVKEV 
entry created 2012-07-11 dataset Swiss-Prot modified 2023-02-22 version 72 accession Q97WX5 name CMR7A_SACS2 protein recommendedName fullName CRISPR-system-CMR-subunit-Cmr7-1 gene name type primary cmr7A name type ordered-locus SSO1986 organism name type scientific Saccharolobus-solfataricus-(strain-ATCC-35092-/-DSM-1617-/-JCM-11322-/-P2) name type common Sulfolobus-solfataricus dbReference id 273057 type NCBI-Taxonomy lineage taxon Archaea taxon Crenarchaeota taxon Thermoprotei taxon Sulfolobales taxon Sulfolobaceae taxon Saccharolobus reference key 1 citation date 2001 first 7835 last 7840 name Proc.-Natl.-Acad.-Sci.-U.S.A. type journal-article volume 98 title The-complete-genome-of-the-crenarchaeon-Sulfolobus-solfataricus-P2. authorList person name She-Q. person name Singh-R.K. person name Confalonieri-F. person name Zivanovic-Y. person name Allard-G. person name Awayez-M.J. person name Chan-Weiher-C.C.-Y. person name Clausen-I.G. person name Curtis-B.A. person name De-Moors-A. person name Erauso-G. person name Fletcher-C. person name Gordon-P.M.K. person name Heikamp-de-Jong-I. person name Jeffries-A.C. person name Kozera-C.J. person name Medina-N. person name Peng-X. person name Thi-Ngoc-H.P. person name Redder-P. person name Schenk-M.E. person name Theriault-C. person name Tolstrup-N. person name Charlebois-R.L. person name Doolittle-W.F. person name Duguet-M. person name Gaasterland-T. person name Garrett-R.A. person name Ragan-M.A. person name Sensen-C.W. person name Van-der-Oost-J. dbReference id 11427726 type PubMed dbReference id 10.1073/pnas.141222098 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-35092-/-DSM-1617-/-JCM-11322-/-P2 reference key 2 citation date 2012 first 303 last 313 name Mol.-Cell type journal-article volume 45 title Structure-and-mechanism-of-the-CMR-complex-for-CRISPR-mediated-antiviral-immunity. authorList person name Zhang-J. person name Rouillon-C. person name Kerou-M. person name Reeks-J. person name Brugger-K. person name Graham-S. person name Reimann-J. person name Cannone-G. person name Liu-H. person name Albers-S.V. person name Naismith-J.H. person name Spagnolo-L. person name White-M.F. dbReference id 22227115 type PubMed dbReference id 10.1016/j.molcel.2011.12.013 type DOI scope IDENTIFICATION-BY-MASS-SPECTROMETRY scope FUNCTION-IN-CMR-COMPLEX scope SUBUNIT scope SUBCELLULAR-LOCATION source strain ATCC-35092-/-DSM-1617-/-JCM-11322-/-P2 reference key 3 citation date 2010 first 167 last 180 name J.-Struct.-Funct.-Genomics type journal-article volume 11 title The-Scottish-Structural-Proteomics-Facility:-targets,-methods-and-outputs. authorList person name Oke-M. person name Carter-L.G. person name Johnson-K.A. person name Liu-H. person name McMahon-S.A. person name Yan-X. person name Kerou-M. person name Weikart-N.D. person name Kadi-N. person name Sheikh-M.A. person name Schmelz-S. person name Dorward-M. person name Zawadzki-M. person name Cozens-C. person name Falconer-H. person name Powers-H. person name Overton-I.M. person name van-Niekerk-C.A. person name Peng-X. person name Patel-P. person name Garrett-R.A. person name Prangishvili-D. person name Botting-C.H. person name Coote-P.J. person name Dryden-D.T. person name Barton-G.J. person name Schwarz-Linek-U. person name Challis-G.L. person name Taylor-G.L. person name White-M.F. person name Naismith-J.H. dbReference id 20419351 type PubMed dbReference id 10.1007/s10969-010-9090-y type DOI scope X-RAY-CRYSTALLOGRAPHY-(2.05-ANGSTROMS) comment type function text evidence 1-2 CRISPR-(clustered-regularly-interspaced-short-palindromic-repeat)-is-an-adaptive-immune-system-that-provides-protection-against-mobile-genetic-elements-(viruses,-transposable-elements-and-conjugative-plasmids).-CRISPR-clusters-contain-spacers,-sequences-complementary-to-antecedent-mobile-elements,-and-target-invading-nucleic-acids.-CRISPR-clusters-are-transcribed-and-processed-into-CRISPR-RNA-(crRNA)-(By-similarity).-The-CMR-complex-degrades-RNA-complementary-to-the-crRNA-(target-RNA)-within-UA-dinucleotides,-generating-3'-OH-and-5'-phosphate-ends.-Activity-is-dependent-on-the-8-nt-long-5'-tag-in-the-crRNA,-an-unpaired-3'-flag-on-the-target-RNA,-and-is-stimulated-by-ATP.-Some-cleavage-of-the-guide-crRNA-can-also-be-observed. comment type subunit text evidence 2 Possible-homodimer.-Part-of-the-CMR-ribonucleoprotein-complex,-consisting-of-crRNA-plus-Cmr1/Cmr2/Cmr3/Cmr4/Cmr5/Cmr6-at-1:1-and-possibly-3-Cmr7-dimers.-A-Cmr2/Cmr3/Cmr7-subcomplex-without-crRNA-can-also-be-isolated.-It-does-not-cleave-target-RNA. comment type subcellular-location subcellularLocation location evidence 2 Cytoplasm comment type similarity text evidence 3 Belongs-to-the-CRISPR-system-Cmr7-family. dbReference id AE006641 type EMBL property type protein-sequence-ID value AAK42176.1 property type molecule-type value Genomic_DNA dbReference id A90365 type PIR property type entry-name value A90365 dbReference id WP_009993002.1 type RefSeq property type nucleotide-sequence-ID value NC_002754.1 dbReference id 2X5Q type PDB property type method value X-ray property type resolution value 2.05-A property type chains value A/B=1-197 dbReference id 2X5Q type PDBsum dbReference id Q97WX5 type AlphaFoldDB dbReference id Q97WX5 type SMR dbReference id 273057.SSO1986 type STRING dbReference id AAK42176 type EnsemblBacteria property type protein-sequence-ID value AAK42176 property type gene-ID value SSO1986 dbReference id 27428312 type GeneID dbReference id 72910464 type GeneID dbReference id sso:SSO1986 type KEGG dbReference id fig|273057.12.peg.2062 type PATRIC dbReference id arCOG08552 type eggNOG property type taxonomic-scope value Archaea dbReference id CLU_1472150_0_0_2 type HOGENOM dbReference id Q97WX5 type EvolutionaryTrace dbReference id UP000001974 type Proteomes property type component value Chromosome dbReference id GO:0005737 type GO property type term value C:cytoplasm property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0099048 type GO property type term value P:CRISPR-cas-system property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0051607 type GO property type term value P:defense-response-to-virus property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 2.60.120.1670 type Gene3D property type match-status value 1 dbReference id IPR043959 type InterPro property type entry-name value Cmr7A dbReference id PF19021 type Pfam property type entry-name value Cmr7A property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-0051 Antiviral-defense keyword id KW-0963 Cytoplasm keyword id KW-1185 Reference-proteome feature description CRISPR-system-CMR-subunit-Cmr7-1 id PRO_0000418083 type chain location begin position 1 end position 197 feature evidence 4 type strand location begin position 10 end position 14 feature evidence 4 type strand location begin position 20 end position 22 feature evidence 4 type turn location begin position 23 end position 25 feature evidence 4 type strand location begin position 26 end position 28 feature evidence 4 type strand location begin position 30 end position 32 feature evidence 4 type strand location begin position 34 end position 37 feature evidence 4 type strand location begin position 44 end position 48 feature evidence 4 type strand location begin position 51 end position 53 feature evidence 4 type strand location begin position 55 end position 59 feature evidence 4 type strand location begin position 61 end position 64 feature evidence 4 type turn location begin position 65 end position 68 feature evidence 4 type strand location begin position 69 end position 72 feature evidence 4 type strand location begin position 79 end position 92 feature evidence 4 type strand location begin position 94 end position 101 feature evidence 4 type helix location begin position 102 end position 104 feature evidence 4 type strand location begin position 107 end position 109 feature evidence 4 type strand location begin position 115 end position 123 feature evidence 4 type strand location begin position 138 end position 143 feature evidence 4 type helix location begin position 147 end position 156 feature evidence 4 type helix location begin position 158 end position 161 feature evidence 4 type helix location begin position 163 end position 168 feature evidence 4 type helix location begin position 171 end position 184 feature evidence 4 type strand location begin position 187 end position 194 evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000269 source dbReference id 22227115 type PubMed evidence key 3 type ECO:0000305 evidence key 4 type ECO:0007829 source dbReference id 2X5Q type PDB sequence checksum C8AC8DACA9BA65D6 length 197 mass 22151 modified 2001-10-01 version 1 MTSGAGWEEQVFLPITNSISSEDNNQIKIGSSVSIEYNQNGQHVSQIDDKGLHNILVLTGYAIDESTGELVPTFDPCDYVKGILISGKILKGNHFKIIGIPSNKLYIIRKKDVHGNITFSLPIKNFNTGTYQVDLRDKVTSFVSLDRDVAKTIVDNVLAKIYAKIYNSLNKEQKDKLYRDVEEIFNYYSIKSLKSNP 
entry created 2012-09-05 dataset Swiss-Prot modified 2023-02-22 version 58 accession B5GW45 name TMUUS_STRCL protein recommendedName fullName evidence 5 (+)-T-muurolol-synthase-((2E,6E)-farnesyl-diphosphate-cyclizing) ecNumber evidence 4 4.2.3.98 alternativeName fullName evidence 5 Terpene-cyclase alternativeName fullName evidence 5 Type-I-terpene-synthase gene name type ORF SCLAV_p0068 name type ORF SSCG_03688 organism name type scientific Streptomyces-clavuligerus dbReference id 1901 type NCBI-Taxonomy lineage taxon Bacteria taxon Actinobacteria taxon Streptomycetales taxon Streptomycetaceae taxon Streptomyces geneLocation type plasmid name pSCL4 reference key 1 citation date 2010 first 212 last 224 name Genome-Biol.-Evol. type journal-article volume 2 title The-sequence-of-a-1.8-mb-bacterial-linear-plasmid-reveals-a-rich-evolutionary-reservoir-of-secondary-metabolic-pathways. authorList person name Medema-M.H. person name Trefzer-A. person name Kovalchuk-A. person name van-den-Berg-M. person name Mueller-U. person name Heijne-W. person name Wu-L. person name Alam-M.T. person name Ronning-C.M. person name Nierman-W.C. person name Bovenberg-R.A.L. person name Breitling-R. person name Takano-E. dbReference id 20624727 type PubMed dbReference id 10.1093/gbe/evq013 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-27064-/-DSM-738-/-JCM-4710-/-NBRC-13307-/-NCIMB-12785-/-NRRL-3585-/-VKM-Ac-602 plasmid pSCL4 reference key 2 citation date 2008-02 db EMBL/GenBank/DDBJ-databases type submission title Annotation-of-Streptomyces-clavuligerus-ATCC-27064. authorList person name Fischbach-M. person name Ward-D. person name Young-S. person name Jaffe-D. person name Gnerre-S. person name Berlin-A. person name Heiman-D. person name Hepburn-T. person name Sykes-S. person name Alvarado-L. person name Kodira-C.D. person name Straight-P. person name Clardy-J. person name Hung-D. person name Kolter-R. person name Mekalanos-J. person name Walker-S. person name Walsh-C.T. person name Lander-E. person name Galagan-J. person name Nusbaum-C. person name Birren-B. scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain ATCC-27064-/-DSM-738-/-JCM-4710-/-NBRC-13307-/-NCIMB-12785-/-NRRL-3585-/-VKM-Ac-602 reference key 3 citation date 2011 first 32 last 37 name Chem.-Biol. type journal-article volume 18 title Genome-mining-in-Streptomyces-clavuligerus:-expression-and-biochemical-characterization-of-two-new-cryptic-sesquiterpene-synthases. authorList person name Hu-Y. person name Chou-W.K. person name Hopson-R. person name Cane-D.E. dbReference id 21276937 type PubMed dbReference id 10.1016/j.chembiol.2010.11.008 type DOI scope FUNCTION scope CATALYTIC-ACTIVITY scope BIOPHYSICOCHEMICAL-PROPERTIES scope REACTION-MECHANISM source strain ATCC-27064-/-DSM-738-/-JCM-4710-/-NBRC-13307-/-NCIMB-12785-/-NRRL-3585-/-VKM-Ac-602 comment type function text evidence 4 Catalyzes-the-conversion-of-(2E,6E)-farnesyl-diphosphate-(FPP)-into-(+)-T-muurolol-via-a-1,10-cyclization,-which-requires-isomerization-of-FPP-to-nerolidyl-diphosphate-(NPP)-and-then-abstraction-of-the-pyrophosphate-from-intermediate-NPP-leading-to-a-(E,Z)-germacradienyl-(helminthogermacradienyl)-cation. comment type catalytic-activity reaction evidence 4 text (2E,6E)-farnesyl-diphosphate-+-H2O-=-(+)-T-muurolol-+-diphosphate dbReference id RHEA:32011 type Rhea dbReference id CHEBI:15377 type ChEBI dbReference id CHEBI:33019 type ChEBI dbReference id CHEBI:63704 type ChEBI dbReference id CHEBI:175763 type ChEBI dbReference id 4.2.3.98 type EC comment type cofactor cofactor evidence 2 name Mg(2+) dbReference id CHEBI:18420 type ChEBI text evidence 2 Binds-3-Mg(2+)-ions-per-subunit. comment type biophysicochemical-properties kinetics KM evidence 4 2.7-uM-for-(2E,6E)-farnesyl-diphosphate text evidence 4 kcat-is-0.00163-sec(-1). comment type pathway text evidence 1 Secondary-metabolite-biosynthesis;-terpenoid-biosynthesis. comment type domain text evidence 1 The-Asp-Asp-Xaa-Xaa-Xaa-Asp-(DDXXXD)-motif-is-important-for-the-catalytic-activity,-presumably-through-binding-to-Mg(2+). comment type similarity text evidence 6 Belongs-to-the-terpene-synthase-family. dbReference evidence 4 id 4.2.3.98 type EC dbReference id CM000914 type EMBL property type protein-sequence-ID value EFG03561.2 property type molecule-type value Genomic_DNA dbReference id DS570654 type EMBL property type protein-sequence-ID value EDY50541.1 property type molecule-type value Genomic_DNA dbReference id WP_003956090.1 type RefSeq property type nucleotide-sequence-ID value NZ_CP027859.1 dbReference id B5GW45 type AlphaFoldDB dbReference id B5GW45 type SMR dbReference id 443255.SCLAV_p0068 type STRING dbReference id EDY50541 type EnsemblBacteria property type protein-sequence-ID value EDY50541 property type gene-ID value SSCG_03688 dbReference id ag:EFG03561 type KEGG dbReference id COG3170 type eggNOG property type taxonomic-scope value Bacteria dbReference id AMETWVI type OMA dbReference id 2989600at2 type OrthoDB dbReference id 4.2.3.98 type BRENDA property type organism-ID value 5988 dbReference id UPA00213 type UniPathway dbReference id UP000002357 type Proteomes property type component value Plasmid-pSCL4 dbReference id UP000006569 type Proteomes property type component value Unassembled-WGS-sequence dbReference id GO:0016829 type GO property type term value F:lyase-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0046872 type GO property type term value F:metal-ion-binding property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0016114 type GO property type term value P:terpenoid-biosynthetic-process property type evidence value ECO:0007669 property type project value UniProtKB-UniPathway dbReference id 1.10.600.10 type Gene3D property type entry-name value Farnesyl-Diphosphate-Synthase property type match-status value 1 dbReference id IPR008949 type InterPro property type entry-name value Isoprenoid_synthase_dom_sf dbReference id IPR034686 type InterPro property type entry-name value Terpene_cyclase-like_2 dbReference id PF19086 type Pfam property type entry-name value Terpene_syn_C_2 property type match-status value 1 dbReference id SFLDS00005 type SFLD property type entry-name value Isoprenoid_Synthase_Type_I property type match-status value 1 dbReference id SFLDG01020 type SFLD property type entry-name value Terpene_Cyclase_Like_2 property type match-status value 1 dbReference id SSF48576 type SUPFAM property type entry-name value Terpenoid-synthases property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0456 Lyase keyword id KW-0460 Magnesium keyword id KW-0479 Metal-binding keyword id KW-0614 Plasmid keyword id KW-1185 Reference-proteome feature description (+)-T-muurolol-synthase-((2E,6E)-farnesyl-diphosphate-cyclizing) id PRO_0000418478 type chain location begin position 1 end position 418 feature description Disordered evidence 3 type region-of-interest location begin position 354 end position 418 feature description DDXXXD-motif evidence 1 type short-sequence-motif location begin position 83 end position 88 feature evidence 2 type binding-site location position position 83 ligand name Mg(2+) dbReference id CHEBI:18420 type ChEBI label 1 feature evidence 2 type binding-site location position position 88 ligand name Mg(2+) dbReference id CHEBI:18420 type ChEBI label 1 feature evidence 2 type binding-site location position position 88 ligand name Mg(2+) dbReference id CHEBI:18420 type ChEBI label 2 feature evidence 2 type binding-site location position position 179 ligand name substrate feature evidence 2 type binding-site location position position 225 ligand name Mg(2+) dbReference id CHEBI:18420 type ChEBI label 3 feature evidence 2 type binding-site location position position 229 ligand name Mg(2+) dbReference id CHEBI:18420 type ChEBI label 3 feature evidence 2 type binding-site location position position 232 ligand name substrate feature evidence 2 type binding-site location position position 233 ligand name Mg(2+) dbReference id CHEBI:18420 type ChEBI label 3 feature evidence 2 type binding-site location begin position 312 end position 313 ligand name substrate feature description Plays-a-critical-role-in-the-stabilization-of-intermediate-cation evidence 2 type site location position position 80 feature description Plays-a-critical-role-for-substrate-recognition evidence 2 type site location position position 84 feature description Plays-a-critical-role-for-substrate-recognition evidence 2 type site location position position 159 feature description Plays-a-critical-role-for-abstraction-of-the-pyrophosphate-group evidence 2 type site location position position 183 evidence key 1 type ECO:0000250 source dbReference id A7NH01 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id B5HDJ6 type UniProtKB evidence key 3 type ECO:0000256 source dbReference id MobiDB-lite type SAM evidence key 4 type ECO:0000269 source dbReference id 21276937 type PubMed evidence key 5 type ECO:0000303 source dbReference id 21276937 type PubMed evidence key 6 type ECO:0000305 sequence checksum C0F63991CF0F4C1E length 418 mass 46002 modified 2008-10-14 version 1 MSLNHSDLMFYCPVDDLPHPAASGVNDRTLDWASGQGIPTADRDAGRLRAMAPGLLAARIAPDARGPVLDAFADHHTWLFAFDDEYCDRADGSGITEWASFLARLHRVVETGESALLPGNPYGLALRDIACRLSTYTTPAQLAEWLEALRSYFAALVWERSRRRDDDRLQSLDDYLLLRLRNGAMHTSITLLDTVNGYVLPRELRETPGVRALVEMTALLVSVDNDILSHHKESTSGTREANLLDVLGRTGHTTPGEAVAQAVALRNEIMRQFVRVAERVRTPAAVPELYRFTTGLARWIRANLDFSLTTTRYTGPVTERAALSPHEVPPLSGQGPAPARSDVIGWWWRIPEPLPEPGSDGADTPVRKRRAGDRPPTAGRGGAPHHQRTGPPPPVLPGGITASRSSGLQQSTWRREHR 
entry created 2013-05-01 dataset Swiss-Prot modified 2023-02-22 version 132 accession Q9LUE4 name HSD6_ARATH protein recommendedName fullName 11-beta-hydroxysteroid-dehydrogenase-like-6 ecNumber 1.1.1.- alternativeName fullName 17-beta-hydroxysteroid-dehydrogenase-like-6 ecNumber 1.1.1.- alternativeName fullName Hydroxysteroid-dehydrogenase-6 shortName AtHSD6 gene name type primary HSD6 name type ordered-locus At5g50770 name type ORF MFB16.17 organism name type scientific Arabidopsis-thaliana name type common Mouse-ear-cress dbReference id 3702 type NCBI-Taxonomy lineage taxon Eukaryota taxon Viridiplantae taxon Streptophyta taxon Embryophyta taxon Tracheophyta taxon Spermatophyta taxon Magnoliopsida taxon eudicotyledons taxon Gunneridae taxon Pentapetalae taxon rosids taxon malvids taxon Brassicales taxon Brassicaceae taxon Camelineae taxon Arabidopsis reference key 1 citation date 2000 first 31 last 63 name DNA-Res. type journal-article volume 7 title Structural-analysis-of-Arabidopsis-thaliana-chromosome-5.-X.-Sequence-features-of-the-regions-of-3,076,755-bp-covered-by-sixty-P1-and-TAC-clones. authorList person name Sato-S. person name Nakamura-Y. person name Kaneko-T. person name Katoh-T. person name Asamizu-E. person name Kotani-H. person name Tabata-S. dbReference id 10718197 type PubMed dbReference id 10.1093/dnares/7.1.31 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain cv.-Columbia reference key 2 citation date 2017 first 789 last 804 name Plant-J. type journal-article volume 89 title Araport11:-a-complete-reannotation-of-the-Arabidopsis-thaliana-reference-genome. authorList person name Cheng-C.Y. person name Krishnakumar-V. person name Chan-A.P. person name Thibaud-Nissen-F. person name Schobel-S. person name Town-C.D. dbReference id 27862469 type PubMed dbReference id 10.1111/tpj.13415 type DOI scope GENOME-REANNOTATION source strain cv.-Columbia reference key 3 citation date 2005-01 db EMBL/GenBank/DDBJ-databases type submission title Arabidopsis-cDNA-clones. authorList person name Shinn-P. person name Chen-H. person name Cheuk-R. person name Kim-C.J. person name Ecker-J.R. scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-MRNA] source strain cv.-Columbia reference key 4 citation date 2007 first 87 last 97 name Plant-Physiol. type journal-article volume 145 title A-putative-hydroxysteroid-dehydrogenase-involved-in-regulating-plant-growth-and-development. authorList person name Li-F. person name Asami-T. person name Wu-X. person name Tsang-E.W. person name Cutler-A.J. dbReference id 17616511 type PubMed dbReference id 10.1104/pp.107.100560 type DOI scope GENE-FAMILY reference key 5 citation date 2009 first 1463 last 1478 name Plant-Cell-Physiol. type journal-article volume 50 title Regulation-of-HSD1-in-seeds-of-Arabidopsis-thaliana. authorList person name Baud-S. person name Dichow-N.R. person name Kelemen-Z. person name d'Andrea-S. person name To-A. person name Berger-N. person name Canonge-M. person name Kronenberger-J. person name Viterbo-D. person name Dubreucq-B. person name Lepiniec-L. person name Chardot-T. person name Miquel-M. dbReference id 19542545 type PubMed dbReference id 10.1093/pcp/pcp092 type DOI scope GENE-FAMILY comment type subcellular-location subcellularLocation location evidence 4 Membrane topology evidence 4 Single-pass-type-II-membrane-protein comment type similarity text evidence 4 Belongs-to-the-short-chain-dehydrogenases/reductases-(SDR)-family. dbReference id 1.1.1.- type EC dbReference id AB023037 type EMBL property type protein-sequence-ID value BAA96990.1 property type molecule-type value Genomic_DNA dbReference id CP002688 type EMBL property type protein-sequence-ID value AED95990.1 property type molecule-type value Genomic_DNA dbReference id BT020525 type EMBL property type protein-sequence-ID value AAW49294.1 property type molecule-type value mRNA dbReference id NP_199890.1 type RefSeq property type nucleotide-sequence-ID value NM_124455.2 dbReference id Q9LUE4 type AlphaFoldDB dbReference id Q9LUE4 type SMR dbReference id 3702.AT5G50770.1 type STRING dbReference id Q9LUE4 type PaxDb dbReference id 232109 type ProteomicsDB dbReference id AT5G50770.1 type EnsemblPlants property type protein-sequence-ID value AT5G50770.1 property type gene-ID value AT5G50770 dbReference id 835149 type GeneID dbReference id AT5G50770.1 type Gramene property type protein-sequence-ID value AT5G50770.1 property type gene-ID value AT5G50770 dbReference id ath:AT5G50770 type KEGG dbReference id AT5G50770 type Araport dbReference id locus:2163315 type TAIR property type gene-designation value AT5G50770 dbReference id KOG1205 type eggNOG property type taxonomic-scope value Eukaryota dbReference id CLU_010194_2_1_1 type HOGENOM dbReference id Q9LUE4 type InParanoid dbReference id ASGCGYI type OMA dbReference id 7015at2759 type OrthoDB dbReference id Q9LUE4 type PhylomeDB dbReference id PR:Q9LUE4 type PRO dbReference id UP000006548 type Proteomes property type component value Chromosome-5 dbReference id Q9LUE4 type ExpressionAtlas property type expression-patterns value baseline-and-differential dbReference id Q9LUE4 type Genevisible property type organism-ID value AT dbReference id GO:0005829 type GO property type term value C:cytosol property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0016020 type GO property type term value C:membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0016491 type GO property type term value F:oxidoreductase-activity property type evidence value ECO:0000318 property type project value GO_Central dbReference id GO:0006694 type GO property type term value P:steroid-biosynthetic-process property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.40.50.720 type Gene3D property type entry-name value NAD(P)-binding-Rossmann-like-Domain property type match-status value 1 dbReference id IPR036291 type InterPro property type entry-name value NAD(P)-bd_dom_sf dbReference id IPR020904 type InterPro property type entry-name value Sc_DH/Rdtase_CS dbReference id IPR002347 type InterPro property type entry-name value SDR_fam dbReference id PTHR43391:SF76 type PANTHER property type entry-name value 11-BETA-HYDROXYSTEROID-DEHYDROGENASE-LIKE-6 property type match-status value 1 dbReference id PTHR43391 type PANTHER property type entry-name value RETINOL-DEHYDROGENASE-RELATED property type match-status value 1 dbReference id PF00106 type Pfam property type entry-name value adh_short property type match-status value 1 dbReference id PR00081 type PRINTS property type entry-name value GDHRDH dbReference id PR00080 type PRINTS property type entry-name value SDRFAMILY dbReference id SSF51735 type SUPFAM property type entry-name value NAD(P)-binding-Rossmann-fold-domains property type match-status value 1 dbReference id PS00061 type PROSITE property type entry-name value ADH_SHORT property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0444 Lipid-biosynthesis keyword id KW-0443 Lipid-metabolism keyword id KW-0472 Membrane keyword id KW-0521 NADP keyword id KW-0560 Oxidoreductase keyword id KW-1185 Reference-proteome keyword id KW-0735 Signal-anchor keyword id KW-0752 Steroid-biosynthesis keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix feature description 11-beta-hydroxysteroid-dehydrogenase-like-6 id PRO_0000422285 type chain location begin position 1 end position 342 feature description Helical;-Signal-anchor-for-type-II-membrane-protein evidence 2 type transmembrane-region location begin position 10 end position 30 feature description Proton-acceptor evidence 3 type active-site location position position 197 feature evidence 1 type binding-site location begin position 54 end position 80 ligand name NADP(+) dbReference id CHEBI:58349 type ChEBI feature evidence 1 type binding-site location position position 105 ligand name NADP(+) dbReference id CHEBI:58349 type ChEBI feature evidence 1 type binding-site location position position 184 ligand name substrate feature evidence 1 type binding-site location begin position 197 end position 201 ligand name NADP(+) dbReference id CHEBI:58349 type ChEBI feature evidence 1 type binding-site location position position 201 ligand name NADP(+) dbReference id CHEBI:58349 type ChEBI evidence key 1 type ECO:0000250 evidence key 2 type ECO:0000255 evidence key 3 type ECO:0000255 source dbReference id PRU10001 type PROSITE-ProRule evidence key 4 type ECO:0000305 sequence checksum 45ADF1559AAD97FC length 342 mass 37993 modified 2000-10-01 version 1 MDSINKIINFLFPLLTLYALLVFYPTYQRLKSAVSICRNLFSENVAGKVVVITGAASGIGEALAYEYGKRGAYLALVDIRGEPLFHVAALAELYGSPEVLPLVADVSKLQDCERFIRATVLHFGRLDHLVTNAGVAPLYFFADIEDVSKASPAMDINFWGSVYCTFFASPYLKKFRGRIVVIASGCGYIASPRLSFYCASKAAVIAFYETLRTEFGSDIGVTIVAPGIVDSEMSRGKFMTKDGKLVVDKELRDVQMSVLPVESAERCAKAIMRSVCRGDRYLLEPDWIGCVILLKVFCSEATEWVARWLLIARPKFPMMEALSNKILDVAHAFNSFFSFPHY 
