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Database: UniProt/TrEMBL
Entry: A0A194XPV3_9HELO
LinkDB: A0A194XPV3_9HELO
Original site: A0A194XPV3_9HELO 
ID   A0A194XPV3_9HELO        Unreviewed;       230 AA.
AC   A0A194XPV3;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-SEP-2017, entry version 7.
DE   SubName: Full=Putative trypsin {ECO:0000313|EMBL:KUJ22191.1};
DE   Flags: Fragment;
GN   ORFNames=LY89DRAFT_552876 {ECO:0000313|EMBL:KUJ22191.1};
OS   Phialocephala scopiformis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Phialocephala.
OX   NCBI_TaxID=149040 {ECO:0000313|EMBL:KUJ22191.1, ECO:0000313|Proteomes:UP000070700};
RN   [1] {ECO:0000313|EMBL:KUJ22191.1, ECO:0000313|Proteomes:UP000070700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 120377 {ECO:0000313|EMBL:KUJ22191.1,
RC   ECO:0000313|Proteomes:UP000070700};
RG   DOE Joint Genome Institute;
RA   Walker A.K., Frasz S.L., Seifert K.A., Miller J.D., Mondo S.J.,
RA   Labutti K., Lipzen A., Dockter R., Kennedy M., Grigoriev I.V.,
RA   Spatafora J.W.;
RT   "Full genome of DAOMC 229536 Phialocephala scopiformis, a fungal
RT   endophyte of spruce producing the potent anti-insectan compound
RT   rugulosin.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
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DR   EMBL; KQ947407; KUJ22191.1; -; Genomic_DNA.
DR   RefSeq; XP_018076546.1; XM_018208325.1.
DR   EnsemblFungi; KUJ22191; KUJ22191; LY89DRAFT_552876.
DR   GeneID; 28818051; -.
DR   KEGG; psco:LY89DRAFT_552876; -.
DR   KO; K01312; -.
DR   Proteomes; UP000070700; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000070700};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00037407};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070700};
KW   Serine protease {ECO:0000256|RuleBase:RU363034}.
FT   DOMAIN        7    230       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KUJ22191.1}.
FT   NON_TER     230    230       {ECO:0000313|EMBL:KUJ22191.1}.
SQ   SEQUENCE   230 AA;  23181 MW;  71DF43B4F613D432 CRC64;
     VPGGVDIVGG SAATAGQFPY QVALLHSGSL FCGGVLINAN TVLTAAHCSV DYSASSVQVR
     AGSLKYASGG TLVSVSKIVV HPDYDEDTID NDIALWKLAT AIPTSSTIGY ATLPAQGSDP
     AAGVSTTVSG WGLTSESGST LPTSLRYVSV PVVSRTTCRS DYGTSAITNN MFCAAASGKD
     SCSGDSGGPI TITSTGVLAG TVSWGQGCAE AGYPGVYERI GNYVDYINAN
//
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