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Database: UniProt
Entry: A0A179G2G7_METCM
LinkDB: A0A179G2G7_METCM
Original site: A0A179G2G7_METCM 
ID   A0A179G2G7_METCM        Unreviewed;       387 AA.
AC   A0A179G2G7;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   10-APR-2019, entry version 15.
DE   SubName: Full=Subtilisin-like protease PR1I {ECO:0000313|EMBL:OAQ71927.1};
GN   ORFNames=VFPPC_00003 {ECO:0000313|EMBL:OAQ71927.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae;
OC   Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ71927.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ71927.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ71927.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B.,
RA   Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora
RT   revealed by genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|RuleBase:RU003355, ECO:0000256|SAAS:SAAS01077246}.
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:OAQ71927.1}.
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DR   EMBL; LSBJ02000001; OAQ71927.1; -; Genomic_DNA.
DR   RefSeq; XP_018148010.1; XM_018280110.1.
DR   GeneID; 28844104; -.
DR   OrthoDB; 308083at2759; -.
DR   Proteomes; UP000078397; Chromosome 1.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 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:UP000078397};
KW   Hydrolase {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS01077244};
KW   Protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS01099369, ECO:0000313|EMBL:OAQ71927.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW   Serine protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS01099373}.
FT   DOMAIN       37    103       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      136    345       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   387 AA;  40256 MW;  775281764645535A CRC64;
     MYFSLLLLLP SAAAAPASQG TKLAPLITPP GNVIANRYIV KFKESAATSS VSTTLLNLNA
     KADAVYTNIF NGFSGTLSAT ALEQLRNHVE VDYIEQDSAV TIHAFIEQPD APWGISRISH
     QQGGNSTYVY DESAGSGTCT YVIDTGVDGS HPDFEGRAFQ IKSFIEGQDG DGDGHGTHCA
     GTIGSKTYGI AKQTTIYGIK VLDNEGSGTI SGVIAGMDFA MADSQTRSCP KGIVANMSLG
     GRYSLTLNRA AARLVEAGIF LGVAAGNSNS DASYYSPASE PTVCTVGATQ IDDSFASYSN
     YGSVVDILAP GTNILSTWIG GRTNIISGTS MATPHVVGLA AYLASLEGFP GSQALCERIR
     TISTQGAITK LPPKTTNFLA FNGNPSA
//
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