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Database: UniProt
Entry: A0A150VEC2_9PEZI
LinkDB: A0A150VEC2_9PEZI
Original site: A0A150VEC2_9PEZI 
ID   A0A150VEC2_9PEZI        Unreviewed;       517 AA.
AC   A0A150VEC2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   10-APR-2019, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYG48898.1};
GN   ORFNames=M433DRAFT_150590 {ECO:0000313|EMBL:KYG48898.1};
OS   Acidomyces richmondensis BFW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales;
OC   Capnodiales incertae sedis; Acidomyces.
OX   NCBI_TaxID=766039 {ECO:0000313|EMBL:KYG48898.1, ECO:0000313|Proteomes:UP000075602};
RN   [1] {ECO:0000313|EMBL:KYG48898.1, ECO:0000313|Proteomes:UP000075602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFW {ECO:0000313|EMBL:KYG48898.1,
RC   ECO:0000313|Proteomes:UP000075602};
RX   PubMed=26973616; DOI=10.3389/fmicb.2016.00238;
RA   Mosier A.C., Miller C.S., Frischkorn K.R., Ohm R.A., Li Z.,
RA   LaButti K., Lapidus A., Lipzen A., Chen C., Johnson J.,
RA   Lindquist E.A., Pan C., Hettich R.L., Grigoriev I.V., Singer S.W.,
RA   Banfield J.F.;
RT   "Fungi Contribute Critical but Spatially Varying Roles in Nitrogen and
RT   Carbon Cycling in Acid Mine Drainage.";
RL   Front. Microbiol. 7:238-238(2016).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {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:KYG48898.1}.
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DR   EMBL; JPDO01000036; KYG48898.1; -; Genomic_DNA.
DR   EnsemblFungi; KYG48898; KYG48898; M433DRAFT_150590.
DR   Proteomes; UP000075602; Unassembled WGS sequence.
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; 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; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075602};
KW   Hydrolase {ECO:0000256|SAAS:SAAS01077244};
KW   Protease {ECO:0000256|SAAS:SAAS01099369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075602};
KW   Serine protease {ECO:0000256|SAAS:SAAS01099373};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     15       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        16    517       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5012768654.
FT   DOMAIN       42    137       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      177    428       Peptidase S8. {ECO:0000259|Pfam:PF00082}.
FT   COILED      486    510       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   517 AA;  55590 MW;  D313E22C9D56FF42 CRC64;
     MKGVLGLSLA TLAASSPVLF GEHQEAAPII SAENAKEIQD NYLIVFKKHV TDKHAADHHA
     WVQDVHLQRQ NAKTELRKRS LSSQTPLIDD IFGGLKHTYN IAGSLLGYSG HFDEDVIEQI
     RRHPDVEYIE KDQEVHTLSK SEPELERNAP WGLARISHRD ALSFGNFNKY LYSEDGGEGV
     DVYIIDTGTN INHVDFEGRA SWGKTIPQGD KDEDGNGHGT HCSGTVAGKK YGVAKKAHIK
     AVKVLRSNGS GSMSDVVKGV EYAAEQHLEQ VSIAKKGKRK GFKGSAANMS LGGGKSSILD
     QAVNAAVDAG LHFAVAAGND NADSCNYSPA AAEKAVTVGA STLADERAYF SNYGKCNDIF
     APGLSILSTW IGSNHSVNTI SGTSMASPHV AGLLAYMLSL QPSKDSAYAV ADITPKKLKA
     NLISIATEGA LTDVPSNTAN ILAWNGGGES NYSSIIDKGS YKVAKKEDQE ISLDFGKIEE
     GVTSDAKKLA QKIEQLSHKV EEEVAEELKD FFHELNI
//
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