entry created 2019-10-16 dataset Swiss-Prot modified 2023-02-22 version 12 accession P0DOR4 accession P12922 accession P68607 name PG078_VARV protein recommendedName fullName Protein-OPG078 alternativeName fullName Protein-I2 gene name type primary OPG078 name type ORF I2L organism name type scientific Variola-virus dbReference id 10255 type NCBI-Taxonomy lineage taxon Viruses taxon Varidnaviria taxon Bamfordvirae taxon Nucleocytoviricota taxon Pokkesviricetes taxon Chitovirales taxon Poxviridae taxon Chordopoxvirinae taxon Orthopoxvirus organismHost name type scientific Homo-sapiens name type common Human dbReference id 9606 type NCBI-Taxonomy reference key 1 citation date 1993 first 748 last 751 name Nature type journal-article volume 366 title Potential-virulence-determinants-in-terminal-regions-of-variola-smallpox-virus-genome. authorList person name Massung-R.F. person name Esposito-J.J. person name Liu-L.I. person name Qi-J. person name Utterback-T.R. person name Knight-J.C. person name Aubin-L. person name Yuran-T.E. person name Parsons-J.M. person name Loparev-V.N. person name Selivanov-N.A. person name Cavallaro-K.F. person name Kerlavage-A.R. person name Mahy-B.W.J. person name Venter-J.C. dbReference id 8264798 type PubMed dbReference id 10.1038/366748a0 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] source strain Bangladesh-1975 reference key 2 citation date 1995-12 db EMBL/GenBank/DDBJ-databases type submission authorList person name Shchelkunov-S.N. person name Chizhikov-V.E. person name Totmenin-A.V. person name Resenchuk-S.M. person name Blinov-V.M. person name Sandakhchiev-L.S. scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] source strain Garcia-1966 comment type function text evidence 1 Late-protein-which-probably-plays-a-role-in-virus-entry-into-the-host-cell. comment type subcellular-location subcellularLocation location evidence 1 Virion-membrane topology evidence 1 Single-pass-membrane-protein text evidence 1 Component-of-the-membrane-of-the-mature-virion. comment type induction text Expressed-in-the-late-phase-of-the-viral-replicative-cycle. comment type similarity text evidence 3 Belongs-to-the-orthopoxvirus-OPG078-family. dbReference id L22579 type EMBL property type protein-sequence-ID value AAA60804.1 property type molecule-type value Genomic_DNA dbReference id X76263 type EMBL property type protein-sequence-ID value CAA53830.1 property type molecule-type value Genomic_DNA dbReference id F72157 type PIR property type entry-name value F72157 dbReference id T28494 type PIR property type entry-name value T28494 dbReference id NP_042100.1 type RefSeq property type nucleotide-sequence-ID value NC_001611.1 dbReference id 1486457 type GeneID dbReference id vg:1486457 type KEGG dbReference id UP000119805 type Proteomes property type component value Genome dbReference id GO:0016020 type GO property type term value C:membrane property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0055036 type GO property type term value C:virion-membrane property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0046718 type GO property type term value P:viral-entry-into-host-cell property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id IPR009175 type InterPro property type entry-name value Poxvirus_I2 dbReference id PF12575 type Pfam property type entry-name value Pox_EPC_I2-L1 property type match-status value 1 dbReference id PIRSF003766 type PIRSF property type entry-name value VAC_I2L property type match-status value 1 proteinExistence type evidence-at-transcript-level keyword id KW-0426 Late-protein keyword id KW-0472 Membrane keyword id KW-1185 Reference-proteome keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix keyword id KW-1162 Viral-penetration-into-host-cytoplasm keyword id KW-0946 Virion keyword id KW-1160 Virus-entry-into-host-cell feature description Protein-OPG078 id PRO_0000448199 type chain location begin position 1 end position 73 feature description Helical evidence 2 type transmembrane-region location begin position 49 end position 69 evidence key 1 type ECO:0000250 source dbReference id P68606 type UniProtKB evidence key 2 type ECO:0000255 evidence key 3 type ECO:0000305 sequence checksum 9AA89F7883384C72 length 73 mass 8499 modified 2019-10-16 version 1 MDKLYAAIFGVFMGSPEDDLTDFIEIVKSVLSDEKTVTSTNNTGCWGWYWLIIIFFIVLILLLLIYLYLKVVW 
entry created 2019-12-11 dataset Swiss-Prot modified 2022-05-25 version 12 accession A0A452CSQ9 name TX21_HADIN protein recommendedName fullName evidence 3 U21-hexatoxin-Hi1a shortName evidence 2 U21-HXTX-Hi1a organism name type scientific Hadronyche-infensa name type common Fraser-island-funnel-web-spider name type synonym Atrax-infensus dbReference id 153481 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Ecdysozoa taxon Arthropoda taxon Chelicerata taxon Arachnida taxon Araneae taxon Mygalomorphae taxon Hexathelidae taxon Hadronyche reference key 1 citation date 2017-10 db PDB-data-bank type submission title Single-gene-recruitment-underlies-venom-complexity-in-the-Australian-funnel-web-spider-Hadronyche-infensa. authorList person name Pineda-S.S. person name Chin-Y.K.-Y. person name Senff-S. person name Mobli-M. person name Escoubas-P. person name Nicholson-G. person name Kass-Q. person name Fry-B.G. person name Mattick-J.S. person name King-G.F. scope STRUCTURE-BY-NMR scope DISULFIDE-BOND comment type function text evidence 2 Probable-neurotoxin-with-ion-channel-impairing-activity. comment type subcellular-location subcellularLocation location evidence 2 Secreted comment type tissue-specificity text evidence 2 Expressed-by-the-venom-gland. comment type domain text evidence 1 The-presence-of-a-'disulfide-through-disulfide-knot'-structurally-defines-this-protein-as-a-knottin. comment type similarity text evidence 2 Belongs-to-the-neurotoxin-21-family. dbReference id 6BA3 type PDB property type method value NMR property type chains value A=1-74 dbReference id 6BA3 type PDBsum dbReference id A0A452CSQ9 type AlphaFoldDB dbReference id A0A452CSQ9 type BMRB dbReference id A0A452CSQ9 type SMR dbReference id GO:0005576 type GO property type term value C:extracellular-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0099106 type GO property type term value F:ion-channel-regulator-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0090729 type GO property type term value F:toxin-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id IPR035311 type InterPro property type entry-name value Cys_Knot_tox dbReference id PF17486 type Pfam property type entry-name value Cys_Knot_tox property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-1015 Disulfide-bond keyword id KW-0872 Ion-channel-impairing-toxin keyword id KW-0960 Knottin keyword id KW-0528 Neurotoxin keyword id KW-0964 Secreted keyword id KW-0800 Toxin feature description U21-hexatoxin-Hi1a id PRO_0000448638 type chain location begin position 1 end position 74 feature evidence 1-4 type disulfide-bond location begin position 23 end position 37 feature evidence 1-4 type disulfide-bond location begin position 30 end position 49 feature evidence 1-4 type disulfide-bond location begin position 36 end position 64 feature evidence 1-4 type disulfide-bond location begin position 67 end position 74 feature evidence 5 type helix location begin position 3 end position 6 feature evidence 5 type strand location begin position 20 end position 22 feature evidence 5 type helix location begin position 33 end position 35 feature evidence 5 type turn location begin position 40 end position 44 feature evidence 5 type strand location begin position 45 end position 52 feature evidence 5 type turn location begin position 55 end position 58 feature evidence 5 type strand location begin position 61 end position 70 evidence key 1 type ECO:0000269 source ref 1 evidence key 2 type ECO:0000305 evidence key 3 type ECO:0000312 source dbReference id 6BA3 type PDB evidence key 4 type ECO:0007744 source dbReference id 6BA3 type PDB evidence key 5 type ECO:0007829 source dbReference id 6BA3 type PDB sequence checksum D25866A3C371EBBD length 74 mass 8187 modified 2019-05-08 version 1 SNRWNLGYGIPHKQVKLPNGQLCKEPGDSCSKRDECCKADDQKTYSSGCAQTWSAMEGGFVRECYICAVESSMC 
entry created 2021-04-07 dataset Swiss-Prot modified 2022-05-25 version 3 accession P0DUJ5 name MORO_PTEVL protein recommendedName fullName evidence 3 Pteroicidin-alpha shortName evidence 3 Alpha-Pte-CONH2 shortName evidence 3 Alpha-Pte-COOH alternativeName fullName evidence 3 Piscidin-like-peptide organism name type scientific Pterois-volitans name type common Red-lionfish name type synonym Gasterosteus-volitans dbReference id 185886 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Chordata taxon Craniata taxon Vertebrata taxon Euteleostomi taxon Actinopterygii taxon Neopterygii taxon Teleostei taxon Neoteleostei taxon Acanthomorphata taxon Eupercaria taxon Perciformes taxon Scorpaenoidei taxon Scorpaenidae taxon Pteroinae taxon Pterois reference key 1 citation date 2018 first 318 last 324 name Fish-Shellfish-Immunol. type journal-article volume 72 title Identification-of-a-moronecidin-like-antimicrobial-peptide-in-the-venomous-fish-Pterois-volitans:-Functional-and-structural-study-of-pteroicidin-alpha. authorList person name Houyvet-B. person name Bouchon-Navaro-Y. person name Bouchon-C. person name Goux-D. person name Bernay-B. person name Corre-E. person name Zatylny-Gaudin-C. dbReference id 29108968 type PubMed dbReference id 10.1016/j.fsi.2017.11.003 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope PROTEIN-SEQUENCE-OF-23-66 scope SUBCELLULAR-LOCATION scope AMIDATION-AT-ARG-43 scope MASS-SPECTROMETRY scope SYNTHESIS-OF-23-66 source tissue Venom comment type function text evidence 1-2 The-amidated-peptide-is-bactericidal-on-human-pathogens-like-S.aureus-or-E.coli,-as-well-as-on-the-fish-pathogen-A.salmonicida-(PubMed:29108968).-May-also-be-active-against-a-variety-of-fungi-(By-similarity).-It-can-kill-bacteria-in-less-than-30-minutes-(S.aureus)-and-120-minutes-(V.vulnificus)-(PubMed:29108968).-It-induces-hemolysis-of-erythrocytes-from-human-and-fishes-(sea-bass-and-lesser-spotted-dogfish)-(PubMed:29108968). comment type function text evidence 2 The-non-amidated-peptide-only-inhibits-growth-of-human-pathogens-like-S.aureus-or-E.coli,-and-the-fish-pathogen-A.salmonicida.-Induces-hemolysis-of-erythrocytes-from-human-and-fishes-(sea-bass-and-lesser-spotted-dogfish). comment type subcellular-location subcellularLocation location evidence 2 Secreted comment type tissue-specificity text evidence 5 Expressed-in-gill,-skin,-intestine,-spleen,-anterior-kidney,-and-blood-cells. comment type PTM text evidence 2 This-peptide-exists-in-N-terminally-amidated-and-non-amidated-forms.-The-amidated-form-is-more-active-and-has-a-greater-alpha-helix-content-than-the-non-amidated-form. comment evidence 2 mass 2408.22 method MALDI type mass-spectrometry text Amidated-form. comment evidence 2 mass 2409.09 method MALDI type mass-spectrometry text Non-amidated-form. comment type similarity text evidence 4 Belongs-to-the-pleurocidin-family. dbReference id P0DUJ5 type AlphaFoldDB dbReference id GO:0005576 type GO property type term value C:extracellular-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0042742 type GO property type term value P:defense-response-to-bacterium property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0050832 type GO property type term value P:defense-response-to-fungus property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0045087 type GO property type term value P:innate-immune-response property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0031640 type GO property type term value P:killing-of-cells-of-another-organism property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id IPR012515 type InterPro property type entry-name value Antimicrobial12 dbReference id PF08107 type Pfam property type entry-name value Antimicrobial12 property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0027 Amidation keyword id KW-0044 Antibiotic keyword id KW-0929 Antimicrobial keyword id KW-0903 Direct-protein-sequencing keyword id KW-0295 Fungicide keyword id KW-0391 Immunity keyword id KW-0399 Innate-immunity keyword id KW-0964 Secreted keyword id KW-0732 Signal feature evidence 2 type signal-peptide location begin position 1 end position 22 feature description Pteroicidin-alpha evidence 2 id PRO_0000452481 type peptide location begin position 23 end position 43 feature evidence 2 id PRO_0000452482 type propeptide location begin position 44 end position 66 feature description Arginine-amide;-partial evidence 3 type modified-residue location position position 43 evidence key 1 type ECO:0000250 source dbReference id Q8UUG2 type UniProtKB evidence key 2 type ECO:0000269 source dbReference id 29108968 type PubMed evidence key 3 type ECO:0000303 source dbReference id 29108968 type PubMed evidence key 4 type ECO:0000305 evidence key 5 type ECO:0000305 source dbReference id 29108968 type PubMed sequence checksum DC59E1D2936BFEA2 length 66 mass 7508 modified 2021-04-07 precursor true version 1 MKCIALFLVLSMVVLMAEPGEAFIHHIIGGLFHVGKSIHDLIRGKNRDMAEQQELERAFDRERAFA 
entry created 2021-06-02 dataset Swiss-Prot modified 2023-02-22 version 12 accession A0A345BJP8 name CLZ18_COCLU protein recommendedName fullName evidence 4 Acyltransferase-clz18 shortName evidence 4 AT-clz18 ecNumber evidence 6 2.3.1.- alternativeName fullName evidence 4 Squalestatin-S1-biosynthesis-cluster-protein-clz18 alternativeName fullName evidence 4 Zaragozic-acid-A-biosynthesis-cluster-protein-18 gene name evidence 4 type primary clz18 organism name type scientific Cochliobolus-lunatus name type common Filamentous-fungus name type synonym Curvularia-lunata dbReference id 5503 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Pezizomycotina taxon Dothideomycetes taxon Pleosporomycetidae taxon Pleosporales taxon Pleosporineae taxon Pleosporaceae taxon Curvularia reference key 1 citation date 2017 first 3560 last 3563 name Org.-Lett. type journal-article volume 19 title Identification-and-heterologous-production-of-a-benzoyl-primed-tricarboxylic-acid-polyketide-intermediate-from-the-zaragozic-acid-A-biosynthetic-pathway. authorList person name Liu-N. person name Hung-Y.S. person name Gao-S.S. person name Hang-L. person name Zou-Y. person name Chooi-Y.H. person name Tang-Y. dbReference id 28605916 type PubMed dbReference id 10.1021/acs.orglett.7b01534 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope FUNCTION scope PATHWAY source strain ATCC-74067 comment type function text evidence 1-3-6 Acyltransferase;-part-of-the-gene-cluster-that-mediates-the-biosynthesis-of-squalestatin-S1-(SQS1,-also-known-as-zaragozic-acid-A),-a-heavily-oxidized-fungal-polyketide-that-offers-potent-cholesterol-lowering-activity-by-targeting-squalene-synthase-(SS)-(PubMed:28605916).-SQS1-is-composed-of-a-2,8-dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic-acid-core-that-is-connected-to-two-lipophilic-polyketide-arms-(PubMed:28605916).-These-initial-steps-feature-the-priming-of-an-unusual-benzoic-acid-starter-unit-onto-the-highly-reducing-polyketide-synthase-clz14,-followed-by-oxaloacetate-extension-and-product-release-to-generate-a-tricarboxylic-acid-containing-product-(PubMed:28605916).-The-phenylalanine-ammonia-lyase-(PAL)-clz10-and-the-acyl-CoA-ligase-clz12-are-involved-in-transforming-phenylalanine-into-benzoyl-CoA-(PubMed:28605916).-The-citrate-synthase-like-protein-clz17-is-involved-in-connecting-the-C-alpha-carbons-of-the-hexaketide-chain-and-oxaloacetate-to-afford-the-tricarboxylic-acid-unit-(PubMed:28605916).-The-potential-hydrolytic-enzymes,-clz11-and-clz13,-are-in-close-proximity-to-pks2-and-may-participate-in-product-release-(PubMed:28605916).-On-the-other-side,-the-tetraketide-arm-is-synthesized-by-a-the-squalestatin-tetraketide-synthase-clz2-and-enzymatically-esterified-to-the-core-in-the-last-biosynthetic-step,-by-the-acetyltransferase-clz6-(By-similarity).-The-biosynthesis-of-the-tetraketide-must-involve-3-rounds-of-chain-extension-(By-similarity).-After-the-first-and-second-rounds-methyl-transfer-occurs,-and-in-all-rounds-of-extension-the-ketoreductase-and-dehydratase-are-active-(By-similarity).-The-enoyl-reductase-and-C-MeT-of-clz2-are-not-active-in-the-final-round-of-extension-(By-similarity).-The-acetyltransferase-clz6-appears-to-have-a-broad-substrate-selectivity-for-its-acyl-CoA-substrate,-allowing-the-in-vitro-synthesis-of-novel-squalestatins-(By-similarity).-The-biosynthesis-of-SQS1-requires-several-oxidative-steps-likely-performed-by-oxidoreductases-clz3,-clz15-and-clz16-(Probable).-Finally,-in-support-of-the-identification-of-the-cluster-as-being-responsible-for-SQS1-production,-the-cluster-contains-a-gene-encoding-a-putative-squalene-synthase-(SS)-clz20,-suggesting-a-likely-mechanism-for-self-resistance-(Probable). comment type pathway text evidence 6 Secondary-metabolite-biosynthesis. comment type subcellular-location subcellularLocation location evidence 2 Membrane topology evidence 2 Multi-pass-membrane-protein comment type similarity text evidence 5 Belongs-to-the-acyltransferase-3-family. dbReference evidence 6 id 2.3.1.- type EC dbReference id MF806533 type EMBL property type protein-sequence-ID value AXF50661.1 property type molecule-type value Genomic_DNA dbReference id A0A345BJP8 type AlphaFoldDB 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:0016747 type GO property type term value F:acyltransferase-activity,-transferring-groups-other-than-amino-acyl-groups property type evidence value ECO:0007669 property type project value InterPro dbReference id IPR002656 type InterPro property type entry-name value Acyl_transf_3_dom dbReference id PTHR23028 type PANTHER property type entry-name value ACETYLTRANSFERASE property type match-status value 1 dbReference id PTHR23028:SF53 type PANTHER property type entry-name value ACYL_TRANSF_3-DOMAIN-CONTAINING-PROTEIN property type match-status value 1 dbReference id PF01757 type Pfam property type entry-name value Acyl_transf_3 property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0012 Acyltransferase keyword id KW-0472 Membrane keyword id KW-0808 Transferase keyword id KW-0812 Transmembrane keyword id KW-1133 Transmembrane-helix feature description Acyltransferase-clz18 id PRO_0000452639 type chain location begin position 1 end position 469 feature description Helical evidence 2 type transmembrane-region location begin position 21 end position 41 feature description Helical evidence 2 type transmembrane-region location begin position 70 end position 90 feature description Helical evidence 2 type transmembrane-region location begin position 134 end position 154 feature description Helical evidence 2 type transmembrane-region location begin position 253 end position 273 feature description Helical evidence 2 type transmembrane-region location begin position 346 end position 366 feature description Helical evidence 2 type transmembrane-region location begin position 391 end position 411 feature description Helical evidence 2 type transmembrane-region location begin position 424 end position 444 evidence key 1 type ECO:0000250 source dbReference id A0A3G1DJH6 type UniProtKB evidence key 2 type ECO:0000255 evidence key 3 type ECO:0000269 source dbReference id 28605916 type PubMed evidence key 4 type ECO:0000303 source dbReference id 28605916 type PubMed evidence key 5 type ECO:0000305 evidence key 6 type ECO:0000305 source dbReference id 28605916 type PubMed sequence checksum 697BDCDFDC180DF3 length 469 mass 52739 modified 2018-11-07 version 1 MIHKPIPNSKPLTAYIDGLRGLLSIIIFNAHLTPVIILGYDKVSRSQVSTSPRNVLDIPLVASCVNNWVLFTIPILKLVYSASPAVCLFFAISGYVMSLKWVRYMNHRSQTSEINSARIFTDFGSSIFRRTLRLSLLAMASMIVPFALMKTGFFDRTVVQQHGLTKLERGMRFWLEQWEQFPARHESWWEQTCDLVQNCARIFTVFMQRRDEAFSPRYNPVLWTIKADLRASLALTVTHLALLGTKRSSRLQILAALAVLGVAVGSLECPLFWAGWIIAEIHHAAEQTPLAQGKGTGQPRQKTNTAGMDTFGKTVVLALGCYVASYPTWKPEKAPMFNTFHMMTPGLIVPPRTWHSLGAVLVLYSLRDVPLARRICESSVAQFLGTHSFAIYLIHFCLVISFGPDLFSWVWSRTGHENLQSLAVGFGITYSILFMAVLLTAAIFRRFIESPVNKCVDSLYRSASVRKEA 
entry created 2021-06-02 dataset Swiss-Prot modified 2023-02-22 version 14 accession A0A345BJN4 name CLZ17_COCLU protein recommendedName fullName evidence 3 Citrate-synthase-like-protein-clz17 ecNumber evidence 5 2.3.3.- alternativeName fullName evidence 3 Squalestatin-S1-biosynthesis-cluster-protein-clz17 alternativeName fullName evidence 3 Zaragozic-acid-A-biosynthesis-cluster-protein-17 gene name evidence 3 type primary clz17 organism name type scientific Cochliobolus-lunatus name type common Filamentous-fungus name type synonym Curvularia-lunata dbReference id 5503 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Pezizomycotina taxon Dothideomycetes taxon Pleosporomycetidae taxon Pleosporales taxon Pleosporineae taxon Pleosporaceae taxon Curvularia reference key 1 citation date 2017 first 3560 last 3563 name Org.-Lett. type journal-article volume 19 title Identification-and-heterologous-production-of-a-benzoyl-primed-tricarboxylic-acid-polyketide-intermediate-from-the-zaragozic-acid-A-biosynthetic-pathway. authorList person name Liu-N. person name Hung-Y.S. person name Gao-S.S. person name Hang-L. person name Zou-Y. person name Chooi-Y.H. person name Tang-Y. dbReference id 28605916 type PubMed dbReference id 10.1021/acs.orglett.7b01534 type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope FUNCTION scope CATALYTIC-ACTIVITY scope PATHWAY source strain ATCC-74067 comment type function text evidence 1-2-5 Citrate-synthase-like-protein;-part-of-the-gene-cluster-that-mediates-the-biosynthesis-of-squalestatin-S1-(SQS1,-also-known-as-zaragozic-acid-A),-a-heavily-oxidized-fungal-polyketide-that-offers-potent-cholesterol-lowering-activity-by-targeting-squalene-synthase-(SS)-(PubMed:28605916).-SQS1-is-composed-of-a-2,8-dioxobicyclic[3.2.1]octane-3,4,5-tricarboxyclic-acid-core-that-is-connected-to-two-lipophilic-polyketide-arms-(PubMed:28605916).-These-initial-steps-feature-the-priming-of-an-unusual-benzoic-acid-starter-unit-onto-the-highly-reducing-polyketide-synthase-clz14,-followed-by-oxaloacetate-extension-and-product-release-to-generate-a-tricarboxylic-acid-containing-product-(PubMed:28605916).-The-phenylalanine-ammonia-lyase-(PAL)-clz10-and-the-acyl-CoA-ligase-clz12-are-involved-in-transforming-phenylalanine-into-benzoyl-CoA-(PubMed:28605916).-The-citrate-synthase-like-protein-clz17-is-involved-in-connecting-the-C-alpha-carbons-of-the-hexaketide-chain-and-oxaloacetate-to-afford-the-tricarboxylic-acid-unit-(PubMed:28605916).-The-potential-hydrolytic-enzymes,-clz11-and-clz13,-are-in-close-proximity-to-pks2-and-may-participate-in-product-release-(PubMed:28605916).-On-the-other-side,-the-tetraketide-arm-is-synthesized-by-a-the-squalestatin-tetraketide-synthase-clz2-and-enzymatically-esterified-to-the-core-in-the-last-biosynthetic-step,-by-the-acetyltransferase-clz6-(By-similarity).-The-biosynthesis-of-the-tetraketide-must-involve-3-rounds-of-chain-extension-(By-similarity).-After-the-first-and-second-rounds-methyl-transfer-occurs,-and-in-all-rounds-of-extension-the-ketoreductase-and-dehydratase-are-active-(By-similarity).-The-enoyl-reductase-and-C-MeT-of-clz2-are-not-active-in-the-final-round-of-extension-(By-similarity).-The-acetyltransferase-clz6-appears-to-have-a-broad-substrate-selectivity-for-its-acyl-CoA-substrate,-allowing-the-in-vitro-synthesis-of-novel-squalestatins-(By-similarity).-The-biosynthesis-of-SQS1-requires-several-oxidative-steps-likely-performed-by-oxidoreductases-clz3,-clz15-and-clz16-(Probable).-Finally,-in-support-of-the-identification-of-the-cluster-as-being-responsible-for-SQS1-production,-the-cluster-contains-a-gene-encoding-a-putative-squalene-synthase-(SS)-clz20,-suggesting-a-likely-mechanism-for-self-resistance-(Probable). comment type pathway text evidence 2 Secondary-metabolite-biosynthesis. comment type similarity text evidence 4 Belongs-to-the-citrate-synthase-family. dbReference evidence 5 id 2.3.3.- type EC dbReference id MF806532 type EMBL property type protein-sequence-ID value AXF50647.1 property type molecule-type value Genomic_DNA dbReference id A0A345BJN4 type AlphaFoldDB dbReference id A0A345BJN4 type SMR dbReference id GO:0046912 type GO property type term value F:acyltransferase-activity,-acyl-groups-converted-into-alkyl-on-transfer property type evidence value ECO:0007669 property type project value InterPro dbReference id GO:0006099 type GO property type term value P:tricarboxylic-acid-cycle property type evidence value ECO:0007669 property type project value InterPro dbReference id 1.10.580.10 type Gene3D property type entry-name value Citrate-Synthase,-domain-1 property type match-status value 1 dbReference id 1.10.230.10 type Gene3D property type entry-name value Cytochrome-P450-Terp,-domain-2 property type match-status value 1 dbReference id IPR016142 type InterPro property type entry-name value Citrate_synth-like_lrg_a-sub dbReference id IPR016143 type InterPro property type entry-name value Citrate_synth-like_sm_a-sub dbReference id IPR002020 type InterPro property type entry-name value Citrate_synthase dbReference id IPR019810 type InterPro property type entry-name value Citrate_synthase_AS dbReference id IPR036969 type InterPro property type entry-name value Citrate_synthase_sf dbReference id PTHR11739 type PANTHER property type entry-name value CITRATE-SYNTHASE property type match-status value 1 dbReference id PTHR11739:SF4 type PANTHER property type entry-name value CITRATE-SYNTHASE,-PEROXISOMAL property type match-status value 1 dbReference id PF00285 type Pfam property type entry-name value Citrate_synt property type match-status value 1 dbReference id PR00143 type PRINTS property type entry-name value CITRTSNTHASE dbReference id SSF48256 type SUPFAM property type entry-name value Citrate-synthase property type match-status value 1 dbReference id PS00480 type PROSITE property type entry-name value CITRATE_SYNTHASE property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0808 Transferase feature description Citrate-synthase-like-protein-clz17 id PRO_0000452638 type chain location begin position 1 end position 423 feature evidence 1 type active-site location position position 357 feature evidence 1 type active-site location position position 413 evidence key 1 type ECO:0000250 source dbReference id A0A3G1DJJ8 type UniProtKB evidence key 2 type ECO:0000269 source dbReference id 28605916 type PubMed evidence key 3 type ECO:0000303 source dbReference id 28605916 type PubMed evidence key 4 type ECO:0000305 evidence key 5 type ECO:0000305 source dbReference id 28605916 type PubMed sequence checksum 4521924F2D9F1DAD length 423 mass 46850 modified 2018-11-07 version 1 MATVNGAVGKPQHISKMIESTKMNGNQAQDAAGRADTPVSSDTPDYLHVFDSRTCNIHHIPVSDGFVRGSDLSTIAAPVKGNSGRMQKLAVLDPGFQHTACKESGITFIDGEKGELRYRGVRIEDLFHDHDFDSTLHLLLWGRLPTNDEKIAFERRIFEAATPPQEVCDVIRKLPKNTDFISMFLTGLSTYMGADEEMTRSRHQAVMTYHKNMKATDDAIIRCFAYVSATLATVYCHVKGVELHPPKEGLTLVENFLHMIGMEDPDKKVSRTIDRLSINMADHELSCSTAAFLHVASSLTDPMTCLLTAISAASGPLHGGALEVCYQGLELIGSVENVPAYIAAVKAKKFRLFGYGHRVYKTQDPRAALTKELMEEHREAIAANPLLQIAVEIDRQANTDPYFVERKLKLNADFYGCFVYIAL 
entry created 2021-09-29 dataset Swiss-Prot modified 2023-02-22 version 12 accession A0A4P8DJW5 name DMXR8_CRYX8 protein recommendedName fullName evidence 4 Short-chain-dehydrogenase/reductase-dmxR8 shortName evidence 4 SDR-dmxR8 ecNumber evidence 6 1.1.1.- alternativeName fullName evidence 4 Dimeric-xanthone-biosynthesis-cluster-protein-R8 gene name evidence 4 type primary dmxR8 organism name type scientific Cryptosporiopsis-sp.-(strain-8999) dbReference id 2572248 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Pezizomycotina taxon Leotiomycetes taxon Helotiales taxon Dermateaceae taxon Cryptosporiopsis reference key 1 citation date 2019 first 2930 last 2939 name Chem.-Sci. type journal-article volume 10 title Structure-revision-of-cryptosporioptides-and-determination-of-the-genetic-basis-for-dimeric-xanthone-biosynthesis-in-fungi. authorList person name Greco-C. person name de-Mattos-Shipley-K. person name Bailey-A.M. person name Mulholland-N.P. person name Vincent-J.L. person name Willis-C.L. person name Cox-R.J. person name Simpson-T.J. dbReference id 30996871 type PubMed dbReference id 10.1039/c8sc05126g type DOI scope NUCLEOTIDE-SEQUENCE-[GENOMIC-DNA] scope FUNCTION scope PATHWAY source strain 8999 comment type function text evidence 3-6 Short-chain-dehydrogenase;-part-of-the-gene-cluster-that-mediates-the-biosynthesis-of-the-dimeric-xanthones-cryptosporioptides-(PubMed:30996871).-The-pathway-begins-with-the-synthesis-of-atrochrysone-thioester-by-the-polyketide-synthase-dmx-nrPKS-(Probable).-The-atrochrysone-carboxyl-ACP-thioesterase-dmxR1-then-breaks-the-thioester-bond-and-releases-the-atrochrysone-carboxylic-acid-from-dmx-nrPKS-(Probable).-Atrochrysone-carboxylic-acid-is-decarboxylated-by-the-decarboxylase-dmxR15,-and-oxidized-by-the-anthrone-oxygenase-dmxR16-to-yield-emodin-(Probable).-Emodin-is-then-reduced-to-emodin-hydroquinone-by-the-oxidoreductase-dmxR7-(Probable).-A-ring-reduction-by-the-short-chain-dehydrogenase-dmxR18,-dehydration-by-the-scytalone-dehydratase-like-protein-dmxR17-and-probable-spontaneous-re-oxidation,-results-in-overall-deoxygenation-to-chrysophanol-(PubMed:30996871).-Baeyer-Villiger-oxidation-by-the-Baeyer-Villiger-monooxygenase-(BVMO)-dmxR6-then-yields-monodictylactone-in-equilibrium-with-monodictyphenone-(PubMed:30996871).-In-the-case-of-the-cryptosporioptides-biosynthesis,-monodictylactone-is-reduced-at-C-12-to-an-alcohol-(by-the-short-chain-dehydrogenases-dmxR12-or-dmxR8)-and-hydroxylated-at-C-5-by-dmxR9,-yielding-the-electron-rich-aromatic-which-could-eliminate-H(2)O-to-form-the-ortho-quinonemethide,-followed-by-tautomerisation-to-paraquinone-and-complete-the-formal-reduction-to-produce-the-10-methylgroup-(Probable).-Conjugate-addition-of-C-4a-OH-to-the-resulting-paraquinone-by-the-monooxygenase-dmxR10-then-gives-cyclohexadienone,-which-is-then-reduced-at-C-5-by-the-short-chain-dehydrogenase-dmxR3-to-give-the-dihydroxanthone-(Probable).-The-6,7-epoxide-in-the-cryptosporioptides-could-be-introduced-by-the-cytochrome-P450-monooxygenase-dmxL3-(Probable).-The-highly-reducing-PKS-dmxL2-manufactures-butyrate,-which-is-further-carboxylated-by-dmxL1-to-form-ethylmalonate-(PubMed:30996871).-It-is-not-yet-clear-whether-the-carboxylation-occurs-while-the-butyrate-is-attached-to-the-ACP-of-dmxL2,-but-this-unusual-fungal-metabolite-could-then-be-esterified-to-O-5-by-the-O-acetyltransferase-dmxR13-(PubMed:30996871).-Finally,-dimerization-performed-by-dmxR5-gives-the-observed-dimers-cryptosporioptides-A,-B-and-C-as-the-final-products-of-the-pathway-(PubMed:30996871). comment type pathway text evidence 6 Secondary-metabolite-biosynthesis. comment type similarity text evidence 5 Belongs-to-the-short-chain-dehydrogenases/reductases-(SDR)-family. dbReference evidence 6 id 1.1.1.- type EC dbReference id MK182094 type EMBL property type protein-sequence-ID value QCL09099.1 property type molecule-type value Genomic_DNA dbReference id A0A4P8DJW5 type AlphaFoldDB dbReference id A0A4P8DJW5 type SMR dbReference id GO:0016491 type GO property type term value F:oxidoreductase-activity 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 IPR002347 type InterPro property type entry-name value SDR_fam dbReference id PTHR43157:SF31 type PANTHER property type entry-name value DEHYDROGENASES,-SHORT-CHAIN property type match-status value 1 dbReference id PTHR43157 type PANTHER property type entry-name value PHOSPHATIDYLINOSITOL-GLYCAN-BIOSYNTHESIS-CLASS-F-PROTEIN-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 SSF51735 type SUPFAM property type entry-name value NAD(P)-binding-Rossmann-fold-domains property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-0520 NAD keyword id KW-0521 NADP keyword id KW-0560 Oxidoreductase feature description Short-chain-dehydrogenase/reductase-dmxR8 id PRO_0000453447 type chain location begin position 1 end position 324 feature description Proton-acceptor evidence 2 type active-site location position position 200 feature evidence 1 type binding-site location begin position 25 end position 33 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI feature evidence 1 type binding-site location begin position 52 end position 53 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI feature evidence 1 type binding-site location begin position 82 end position 84 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI feature evidence 1 type binding-site location begin position 229 end position 231 ligand name NAD(+) dbReference id CHEBI:57540 type ChEBI evidence key 1 type ECO:0000250 source dbReference id Q92506 type UniProtKB evidence key 2 type ECO:0000255 source dbReference id PRU10001 type PROSITE-ProRule evidence key 3 type ECO:0000269 source dbReference id 30996871 type PubMed evidence key 4 type ECO:0000303 source dbReference id 30996871 type PubMed evidence key 5 type ECO:0000305 evidence key 6 type ECO:0000305 source dbReference id 30996871 type PubMed sequence checksum E4D8BC7D9FFFB670 length 324 mass 35296 modified 2019-07-31 version 1 MGFLYSQLFKSLPYPTGNYSGKTIVITGSNVGLGKEAARHYVRLGASKMILAVRSLDKGHDAKHDIEGTTKCADNVIEVWKLDMASYDSVQKFAARVVTELPRVDIFIANAGIAPGSYRTAEDNESSITVNVVSTFLLAALVMPKMKSTAATFKTRPTFTITSSDVHGHTTFPQKSAPDGQIIATVNDKATAEKIWDDMYPISKLLEVLGVRSIAEQNPASKFPVTINCVNPGLCHSELGRDFPTIGFWLIKFFLARTTEVGSRTLVHAGSQGEDSHGQYMSDCEIGTPAPFVTSVEGKETQDRVWNELVKKLDAIKPGVTSNF 
entry created 2021-09-29 dataset Swiss-Prot modified 2023-02-22 version 17 accession A0A0U5GMR5 name AUSJ_ASPCI protein recommendedName fullName evidence 5 Austinoid-biosynthesis-cluster-protein-J gene name evidence 5 type primary ausJ name type ORF ASPCAL14366 organism name type scientific Aspergillus-calidoustus dbReference id 454130 type NCBI-Taxonomy lineage taxon Eukaryota taxon Fungi taxon Dikarya taxon Ascomycota taxon Pezizomycotina taxon Eurotiomycetes taxon Eurotiomycetidae taxon Eurotiales taxon Aspergillaceae taxon Aspergillus taxon Aspergillus-subgen.-Nidulantes reference key 1 citation date 2016 first 0 last 0 name Genome-Announc. type journal-article volume 4 title Draft-genome-sequences-of-fungus-Aspergillus-calidoustus. authorList person name Horn-F. person name Linde-J. person name Mattern-D.J. person name Walther-G. person name Guthke-R. person name Scherlach-K. person name Martin-K. person name Brakhage-A.A. person name Petzke-L. person name Valiante-V. dbReference id 26966204 type PubMed dbReference id 10.1128/genomea.00102-16 type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain SF006504 reference key 2 citation date 2017 first 1227 last 1234 name ACS-Chem.-Biol. type journal-article volume 12 title Discovery-of-an-Extended-Austinoid-Biosynthetic-Pathway-in-Aspergillus-calidoustus. authorList person name Valiante-V. person name Mattern-D.J. person name Schueffler-A. person name Horn-F. person name Walther-G. person name Scherlach-K. person name Petzke-L. person name Dickhaut-J. person name Guthke-R. person name Hertweck-C. person name Nett-M. person name Thines-E. person name Brakhage-A.A. dbReference id 28233494 type PubMed dbReference id 10.1021/acschembio.7b00003 type DOI scope FUNCTION scope PATHWAY reference key 3 citation date 2017 first 2927 last 2933 name ACS-Chem.-Biol. type journal-article volume 12 title Rewiring-of-the-austinoid-biosynthetic-pathway-in-filamentous-fungi. authorList person name Mattern-D.J. person name Valiante-V. person name Horn-F. person name Petzke-L. person name Brakhage-A.A. dbReference id 29076725 type PubMed dbReference id 10.1021/acschembio.7b00814 type DOI scope FUNCTION comment type function text evidence 1-3-4 Part-of-the-gene-cluster-that-mediates-the-biosynthesis-of-calidodehydroaustin,-a-fungal-meroterpenoid-(PubMed:28233494,-PubMed:29076725).-The-first-step-of-the-pathway-is-the-synthesis-of-3,5-dimethylorsellinic-acid-by-the-polyketide-synthase-ausA-(PubMed:28233494).-3,5-dimethylorsellinic-acid-is-then-prenylated-by-the-polyprenyl-transferase-ausN-(PubMed:28233494).-Further-epoxidation-by-the-FAD-dependent-monooxygenase-ausM-and-cyclization-by-the-probable-terpene-cyclase-ausL-lead-to-the-formation-of-protoaustinoid-A-(By-similarity).-Protoaustinoid-A-is-then-oxidized-to-spiro-lactone-preaustinoid-A3-by-the-combined-action-of-the-FAD-binding-monooxygenases-ausB-and-ausC,-and-the-dioxygenase-ausE-(By-similarity).-Acid-catalyzed-keto-rearrangement-and-ring-contraction-of-the-tetraketide-portion-of-preaustinoid-A3-by-ausJ-lead-to-the-formation-of-preaustinoid-A4-(By-similarity).-The-aldo-keto-reductase-ausK,-with-the-help-of-ausH,-is-involved-in-the-next-step-by-transforming-preaustinoid-A4-into-isoaustinone-which-is-in-turn-hydroxylated-by-the-P450-monooxygenase-ausI-to-form-austinolide-(By-similarity).-The-cytochrome-P450-monooxygenase-ausG-modifies-austinolide-to-austinol-(By-similarity).-Austinol-is-further-acetylated-to-austin-by-the-O-acetyltransferase-ausP,-which-spontaneously-changes-to-dehydroaustin-(PubMed:28233494).-The-cytochrome-P450-monooxygenase-ausR-then-converts-dehydroaustin-is-into-7-dehydrodehydroaustin-(PubMed:28233494).-The-hydroxylation-catalyzed-by-ausR-permits-the-O-acetyltransferase-ausQ-to-add-an-additional-acetyl-group-to-the-molecule,-leading-to-the-formation-of-acetoxydehydroaustin-(PubMed:28233494).-The-short-chain-dehydrogenase-ausT-catalyzes-the-reduction-of-the-double-bond-present-between-carbon-atoms-1-and-2-to-convert-7-dehydrodehydroaustin-into-1,2-dihydro-7-hydroxydehydroaustin-(PubMed:28233494).-AusQ-catalyzes-not-only-an-acetylation-reaction-but-also-the-addition-of-the-PKS-ausV-diketide-product-to-1,2-dihydro-7-hydroxydehydroaustin,-forming-precalidodehydroaustin-(PubMed:28233494).-Finally,-the-iron/alpha-ketoglutarate-dependent-dioxygenase-converts-precalidodehydroaustin-into-calidodehydroaustin-(PubMed:28233494). comment type pathway text evidence 7 Secondary-metabolite-biosynthesis;-terpenoid-biosynthesis. comment type subunit text evidence 2 Homodimer. comment type miscellaneous text evidence 8 In-A.calidoustus,-the-austinoid-gene-cluster-lies-on-a-contiguous-DNA-region,-while-clusters-from-E.nidulans-and-P.brasilianum-are-split-in-their-respective-genomes.-Genetic-rearrangements-provoked-variability-among-the-clusters-and-E.nidulans-produces-the-least-number-of-austionoid-derivatives-with-the-end-products-austinol-and-dehydroaustinol,-while-P.brasilianum-can-produce-until-acetoxydehydroaustin,-and-A.calidoustus-produces-the-highest-number-of-identified-derivatives. comment type similarity text evidence 6 Belongs-to-the-trt14-isomerase-family. dbReference id CDMC01000024 type EMBL property type protein-sequence-ID value CEL11263.1 property type molecule-type value Genomic_DNA dbReference id A0A0U5GMR5 type AlphaFoldDB dbReference id A0A0U5GMR5 type SMR dbReference id 2343142at2759 type OrthoDB dbReference id UPA00213 type UniPathway dbReference id UP000054771 type Proteomes property type component value Unassembled-WGS-sequence 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 3.10.450.50 type Gene3D property type match-status value 1 dbReference id PTHR39598 type PANTHER property type entry-name value AUSTINOL-SYNTHESIS-PROTEIN-F-RELATED property type match-status value 1 dbReference id PTHR39598:SF1 type PANTHER property type entry-name value AUSTINOL-SYNTHESIS-PROTEIN-F-RELATED property type match-status value 1 proteinExistence type inferred-from-homology keyword id KW-1185 Reference-proteome feature description Austinoid-biosynthesis-cluster-protein-J id PRO_0000453832 type chain location begin position 1 end position 165 evidence key 1 type ECO:0000250 source dbReference id C8VQ92 type UniProtKB evidence key 2 type ECO:0000250 source dbReference id Q5AR31 type UniProtKB evidence key 3 type ECO:0000269 source dbReference id 28233494 type PubMed evidence key 4 type ECO:0000269 source dbReference id 29076725 type PubMed evidence key 5 type ECO:0000303 source dbReference id 28233494 type PubMed evidence key 6 type ECO:0000305 evidence key 7 type ECO:0000305 source dbReference id 28233494 type PubMed evidence key 8 type ECO:0000305 source dbReference id 29076725 type PubMed sequence checksum 75EA4F37B45F8EC5 length 165 mass 18832 modified 2016-03-16 version 1 MTTTRHRLLATASRFVTTLESLDVDAMLAVRSPTCLHHMCLPSFRNYSITNDQTREAFPQWKATITKYQFGILDDSQTLVDEQARKVMIRAKTAAETTVGDYNNEYVFILRMTEDCDTVDEIWEFYDSLRLRDLHHRLEGGHVPIGVDAPAPFTTTGSNSLDRSK 
entry created 2021-09-29 dataset Swiss-Prot modified 2023-02-22 version 9 accession A0A6M3VZT9 name CAPS1_PFV2 protein recommendedName fullName evidence 4 Major-capsid-protein-1 alternativeName fullName evidence 4 MCP1 alternativeName fullName evidence 1 Major-capsid-protein-VP1 gene name evidence 6 type ORF PFV2_gp20 organism name type scientific Pyrobaculum-filamentous-virus-2 name type common PFV2 dbReference id 2730621 type NCBI-Taxonomy lineage taxon Viruses taxon Adnaviria taxon Zilligvirae taxon Taleaviricota taxon Tokiviricetes taxon Primavirales taxon Tristromaviridae taxon Alphatristromavirus taxon Alphatristromavirus-PFV2 organismHost name type scientific Pyrobaculum-arsenaticum dbReference id 121277 type NCBI-Taxonomy organismHost name type scientific Pyrobaculum-oguniense dbReference id 99007 type NCBI-Taxonomy reference key 1 citation date 2020 first 1821 last 1833 name ISME-J. type journal-article volume 14 title New-virus-isolates-from-Italian-hydrothermal-environments-underscore-the-biogeographic-pattern-in-archaeal-virus-communities. authorList person name Baquero-D.P. person name Contursi-P. person name Piochi-M. person name Bartolucci-S. person name Liu-Y. person name Cvirkaite-Krupovic-V. person name Prangishvili-D. person name Krupovic-M. dbReference id 32322010 type PubMed dbReference id 10.1038/s41396-020-0653-z type DOI scope NUCLEOTIDE-SEQUENCE-[LARGE-SCALE-GENOMIC-DNA] source strain 4 reference key 2 citation date 2020 first 19643 last 19652 name Proc.-Natl.-Acad.-Sci.-U.S.A. type journal-article volume 117 title Structures-of-filamentous-viruses-infecting-hyperthermophilic-archaea-explain-DNA-stabilization-in-extreme-environments. authorList person name Wang-F. person name Baquero-D.P. person name Beltran-L.C. person name Su-Z. person name Osinski-T. person name Zheng-W. person name Prangishvili-D. person name Krupovic-M. person name Egelman-E.H. dbReference id 32759221 type PubMed dbReference id 10.1073/pnas.2011125117 type DOI scope SUBUNIT scope FUNCTION reference evidence 7 key 3 citation date 2020 first veaa023 last veaa023 name Virus-Evol. type journal-article volume 6 title Structure-of-a-filamentous-virus-uncovers-familial-ties-within-the-archaeal-virosphere. authorList person name Wang-F. person name Baquero-D.P. person name Su-Z. person name Osinski-T. person name Prangishvili-D. person name Egelman-E.H. person name Krupovic-M. dbReference id 32368353 type PubMed dbReference id 10.1093/ve/veaa023 type DOI scope STRUCTURE-BY-ELECTRON-MICROSCOPY-(3.40-ANGSTROMS) scope SUBCELLULAR-LOCATION scope FUNCTION comment type function text evidence 2-5 Self-assembles-to-form-a-helical,-filamentous-nucleocapsid-mesuring-400-nm-in-length-and-20-nm-in-width-(Probable)-(PubMed:32368353).-Together-with-capsid-protein-2,-wraps-arounds-the-DNA-and-maintains-it-in-an-A-form-(Probable).-Capsid-proteins-probably-maintain-the-DNA-in-A-form-by-non-specific-desolvation-and-specific-coordination-of-the-DNA-phosphate-groups-by-positively-charged-residues-(Probable).-This-certainly-protects-the-viral-DNA-under-conditions-such-as-the-extreme-desiccation-of-its-host-(Probable). comment type subunit text evidence 3 Heterodimer-composed-of-major-capsid-protein-1-and-major-capsid-protein-2. comment type subcellular-location subcellularLocation location evidence 2 Virion dbReference id MN876844 type EMBL property type protein-sequence-ID value QJF12393.1 property type molecule-type value Genomic_DNA dbReference id 6V7B type PDB property type method value EM property type resolution value 3.40-A property type chains value A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W=1-129 dbReference id 6V7B type PDBsum dbReference id A0A6M3VZT9 type SMR dbReference id UP000502572 type Proteomes property type component value Genome dbReference id GO:0019029 type GO property type term value C:helical-viral-capsid property type evidence value ECO:0000314 property type project value UniProtKB dbReference id GO:0003677 type GO property type term value F:DNA-binding property type evidence value ECO:0000314 property type project value UniProtKB proteinExistence type evidence-at-protein-level keyword id KW-0002 3D-structure keyword id KW-1185 Reference-proteome keyword id KW-0946 Virion feature description Major-capsid-protein-1 id PRO_0000453882 type chain location begin position 1 end position 129 evidence key 1 type ECO:0000250 source dbReference id A0A140F3K6 type UniProtKB evidence key 2 type ECO:0000269 source dbReference id 32368353 type PubMed evidence key 3 type ECO:0000269 source dbReference id 32759221 type PubMed evidence key 4 type ECO:0000303 source dbReference id 32368353 type PubMed evidence key 5 type ECO:0000305 source dbReference id 32759221 type PubMed evidence key 6 type ECO:0000312 source dbReference id QJF12393.1 type EMBL evidence key 7 type ECO:0007744 source dbReference id 6V7B type PDB sequence checksum 7250F8D0C5F890BB length 129 mass 14964 modified 2020-10-07 version 1 MSVVTTRARIAETLTEKHTLGIEKVVATDSWRVGITSREKKLERINISAEISRRIQDEAIAYARNKGIPYLPGINGIAWKLLRLKWLGYTDQINVVMRTVPAEWRDFLTQIMENTQMESMYSELRKVRV 
entry created 2022-02-23 dataset Swiss-Prot modified 2023-02-22 version 6 accession A0A6B9L1F0 name PR13A_PLARH protein recommendedName fullName evidence 4 Kazal-peptide-Pr13a alternativeName fullName evidence 7 Venom-Kazal-domain-peptide-Pr13a organism name type scientific Platymeris-rhadamanthus name type common Red-spot-assassin-bug dbReference id 1134088 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Ecdysozoa taxon Arthropoda taxon Hexapoda taxon Insecta taxon Pterygota taxon Neoptera taxon Paraneoptera taxon Hemiptera taxon Heteroptera taxon Panheteroptera taxon Cimicomorpha taxon Reduviidae taxon Platymeris reference key 1 citation date 2019 first E673 last E673 name Toxins type journal-article volume 11 title Missiles-of-mass-disruption:-composition-and-glandular-origin-of-venom-used-as-a-projectile-defensive-weapon-by-the-assassin-bug-Platymeris-rhadamanthus. authorList person name Walker-A.A. person name Robinson-S.D. person name Undheim-E.A.B. person name Jin-J. person name Han-X. person name Fry-B.G. person name Vetter-I. person name King-G.F. dbReference id 31752210 type PubMed dbReference id 10.3390/toxins11110673 type DOI scope NUCLEOTIDE-SEQUENCE-[MRNA] scope TISSUE-SPECIFICITY source tissue Venom-gland comment type function text evidence 5 May-act-as-a-serine-protease-inhibitor,-since-it-possess-the-kazal-serine-protease-inhibitor-signature. comment type subcellular-location subcellularLocation location evidence 6 Secreted comment type tissue-specificity text evidence 3 Expressed-by-the-venom-gland-(anterior-main-gland)-(at-protein-level). dbReference id MN208328 type EMBL property type protein-sequence-ID value QHB21517.1 property type molecule-type value mRNA dbReference id A0A6B9L1F0 type AlphaFoldDB dbReference id GO:0005576 type GO property type term value C:extracellular-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0004867 type GO property type term value F:serine-type-endopeptidase-inhibitor-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0010466 type GO property type term value P:negative-regulation-of-peptidase-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id 3.30.60.30 type Gene3D property type match-status value 1 dbReference id IPR002350 type InterPro property type entry-name value Kazal_dom dbReference id IPR036058 type InterPro property type entry-name value Kazal_dom_sf dbReference id PF07648 type Pfam property type entry-name value Kazal_2 property type match-status value 1 dbReference id SSF100895 type SUPFAM property type entry-name value Kazal-type-serine-protease-inhibitors property type match-status value 1 dbReference id PS51465 type PROSITE property type entry-name value KAZAL_2 property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-1015 Disulfide-bond keyword id KW-0646 Protease-inhibitor keyword id KW-0964 Secreted keyword id KW-0722 Serine-protease-inhibitor keyword id KW-0732 Signal feature evidence 1 type signal-peptide location begin position 1 end position 20 feature description Kazal-peptide-Pr13a evidence 5 id PRO_5025470253 type chain location begin position 21 end position 73 feature description Kazal-like evidence 2 type domain location begin position 21 end position 73 feature description Reactive-bond evidence 2 type site location begin position 29 end position 30 feature evidence 2 type disulfide-bond location begin position 23 end position 59 feature evidence 2 type disulfide-bond location begin position 27 end position 52 feature evidence 2 type disulfide-bond location begin position 36 end position 73 evidence key 1 type ECO:0000255 evidence key 2 type ECO:0000255 source dbReference id PRU00798 type PROSITE-ProRule evidence key 3 type ECO:0000269 source dbReference id 31752210 type PubMed evidence key 4 type ECO:0000303 source dbReference id 31752210 type PubMed evidence key 5 type ECO:0000305 evidence key 6 type ECO:0000305 source dbReference id 31752210 type PubMed evidence key 7 type ECO:0000312 source dbReference id QHB21517.1 type EMBL sequence checksum 46E5FC90C358773E length 73 mass 8200 modified 2020-06-17 precursor true version 1 MKYIILFLVLIGLQANLALGSKCKCDCTKYPYSPVCAKELKTGDTETFNNVCQLQCYNCTHMKNYVVIYSGSC 
entry created 2022-08-03 dataset Swiss-Prot modified 2023-02-22 version 4 accession C0HM09 name 3L27_NAJNA protein recommendedName fullName evidence 3 Alpha-elapitoxin-Nn3a alternativeName fullName evidence 4 Long-neurotoxin-7 alternativeName fullName evidence 3 Long-chain-alpha-neurotoxin-Nn3a organism name type scientific Naja-naja name type common Indian-cobra dbReference id 35670 type NCBI-Taxonomy lineage taxon Eukaryota taxon Metazoa taxon Chordata taxon Craniata taxon Vertebrata taxon Euteleostomi taxon Lepidosauria taxon Squamata taxon Bifurcata taxon Unidentata taxon Episquamata taxon Toxicofera taxon Serpentes taxon Colubroidea taxon Elapidae taxon Elapinae taxon Naja reference key 1 citation date 2022 first 815079 last 815079 name Front.-Pharmacol. type journal-article volume 13 title Isolation-and-Characterization-of-Two-Postsynaptic-Neurotoxins-From-Indian-Cobra-(Naja-Naja)-Venom. authorList person name Huynh-T.M. person name Silva-A. person name Isbister-G.K. person name Hodgson-W.C. dbReference id 35418867 type PubMed dbReference id 10.3389/fphar.2022.815079 type DOI scope PROTEIN-SEQUENCE scope FUNCTION scope SUBCELLULAR-LOCATION scope MASS-SPECTROMETRY comment type function text evidence 2 Nicotinic-acetylcholine-receptor-antagonist-(PubMed:35418867).-Binds-to-muscle-nicotinic-acetylcholine-receptor-(nAChR)-and-inhibits-acetylcholine-from-binding-to-the-receptor,-thereby-impairing-neuromuscular-transmission-(PubMed:35418867).-Produces-peripheral-paralysis-by-blocking-neuromuscular-transmission-at-the-postsynaptic-site-(PubMed:35418867).-Induces-concentration-dependent-inhibition-of-indirect-twitches-and-abolishes-contractile-responses-of-tissues-to-exogenous-acetylcholine-and-carbachol,-in-the-chick-biventer-cervicis-nerve-muscle-preparation-at-100-300-nM-(in-vitro)-(PubMed:35418867).-Prior-incubation-of-tissues-with-Indian-polyvalent-antivenom-(1-ml/0.6-mg)-prevents-the-neurotoxic-effects-at-100-nM-(in-vitro)-(PubMed:35418867).-Addition-of-Indian-polyvalent-antivenom-(1-ml/0.6-mg)-at-the-t90-time-point-partially-restores-the-neurotoxic-effects-(in-vitro)-(PubMed:35418867).-Displays-a-reversible-antagonism-of-concentration-response-curves-to-carbachol,-with-a-pA2-of-8.17-(in-vitro)-(PubMed:35418867). comment type subcellular-location subcellularLocation location evidence 2 Secreted comment type tissue-specificity text evidence 4 Expressed-by-the-venom-gland. comment evidence 2 mass 7807.5 method MALDI type mass-spectrometry comment type miscellaneous text evidence 2 Constitutes-approximately-3%-of-the-whole-venom-protein-content. comment type similarity text evidence 4 Belongs-to-the-snake-three-finger-toxin-family.-Long-chain-subfamily.-Type-II-alpha-neurotoxin-sub-subfamily. dbReference id UP000694559 type Proteomes property type component value Unplaced dbReference id GO:0005576 type GO property type term value C:extracellular-region property type evidence value ECO:0007669 property type project value UniProtKB-SubCell dbReference id GO:0030550 type GO property type term value F:acetylcholine-receptor-inhibitor-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0099106 type GO property type term value F:ion-channel-regulator-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id GO:0090729 type GO property type term value F:toxin-activity property type evidence value ECO:0007669 property type project value UniProtKB-KW dbReference id cd00206 type CDD property type entry-name value snake_toxin property type match-status value 1 dbReference id 2.10.60.10 type Gene3D property type entry-name value CD59 property type match-status value 1 dbReference id IPR003571 type InterPro property type entry-name value Snake_3FTx dbReference id IPR045860 type InterPro property type entry-name value Snake_toxin-like_sf dbReference id IPR018354 type InterPro property type entry-name value Snake_toxin_con_site dbReference id SSF57302 type SUPFAM property type entry-name value Snake-toxin-like property type match-status value 1 proteinExistence type evidence-at-protein-level keyword id KW-0008 Acetylcholine-receptor-inhibiting-toxin keyword id KW-0903 Direct-protein-sequencing keyword id KW-1015 Disulfide-bond keyword id KW-0872 Ion-channel-impairing-toxin keyword id KW-0528 Neurotoxin keyword id KW-0629 Postsynaptic-neurotoxin keyword id KW-1185 Reference-proteome keyword id KW-0964 Secreted keyword id KW-0800 Toxin feature description Alpha-elapitoxin-Nn3a id PRO_0000456214 type chain location begin position 1 end position 71 feature evidence 1 type disulfide-bond location begin position 3 end position 20 feature evidence 1 type disulfide-bond location begin position 14 end position 42 feature evidence 1 type disulfide-bond location begin position 26 end position 30 feature evidence 1 type disulfide-bond location begin position 46 end position 56 feature evidence 1 type disulfide-bond location begin position 57 end position 62 evidence key 1 type ECO:0000250 source dbReference id P25671 type UniProtKB evidence key 2 type ECO:0000269 source dbReference id 35418867 type PubMed evidence key 3 type ECO:0000303 source dbReference id 35418867 type PubMed evidence key 4 type ECO:0000305 sequence checksum F1981E995C9269AB length 71 mass 7805 modified 2022-08-03 version 1 IRCFITPDITSKDCPNGHVCYTKTWCDGFCSIRGERVDLDGCAATCPTVTGVDIQCCSTDNCNPFPTRKRP 
