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Database: UniProt
Entry: A0A167VW35_9HYPO
LinkDB: A0A167VW35_9HYPO
Original site: A0A167VW35_9HYPO 
ID   A0A167VW35_9HYPO        Unreviewed;       398 AA.
AC   A0A167VW35;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   31-JUL-2019, entry version 20.
DE   SubName: Full=Oryzin {ECO:0000313|EMBL:OAA63041.1};
GN   ORFNames=ISF_04917 {ECO:0000313|EMBL:OAA63041.1};
OS   Cordyceps fumosorosea ARSEF 2679.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Cordycipitaceae;
OC   Cordyceps.
OX   NCBI_TaxID=1081104 {ECO:0000313|EMBL:OAA63041.1, ECO:0000313|Proteomes:UP000076744};
RN   [1] {ECO:0000313|EMBL:OAA63041.1, ECO:0000313|Proteomes:UP000076744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2679 {ECO:0000313|EMBL:OAA63041.1,
RC   ECO:0000313|Proteomes:UP000076744};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS01201832}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OAA63041.1}.
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DR   EMBL; AZHB01000011; OAA63041.1; -; Genomic_DNA.
DR   RefSeq; XP_018704248.1; XM_018848522.1.
DR   EnsemblFungi; OAA63041; OAA63041; ISF_04917.
DR   GeneID; 30021209; -.
DR   OrthoDB; 308083at2759; -.
DR   Proteomes; UP000076744; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   Gene3D; 3.30.70.80; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076744};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS01077244};
KW   Protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS01201830};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076744};
KW   Serine protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS01201831}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     15       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        16    398       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5011955369.
FT   DOMAIN       42    104       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      148    359       Peptidase_S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   398 AA;  42398 MW;  8047E5491B60F92E CRC64;
     MRLSTFVSLL PLVAGAPATR KRAEPAPILE HRGEPKELVA DKYIVKFRQG SAMKEVKRTV
     KLLREDPSQV FSDGIFTGFA GQIHSDGLEA IRQHPDVEYI EPVSVMSTNN VVSQTRRVPW
     GLERISHRDN EADSYDYDQT AGAGTCAYVI DSGVDINHPE FEGRATSLGS YIGNSDRDDC
     GHGTHVAGTI GSRSFGVAKK THIFALKALG WSRQVGNCVG NNDITIAALH YVARHAAENR
     SRCPKGAVVN MSLGGPASRS VNEAVDNLAA RGVFVAVASG NSNQDAENFS PASANGACCV
     GATDYYDRRY AMSNFGAYVD VAAPGVDVYS TLPNGQAGPM TGTSMASPHI AGLAAYLAAR
     DGVSGPKLCT KIRNMATRGA IVNQYDDTRN LIAFNGGR
//
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