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Database: UniProt
Entry: A0A093YJ82_9PEZI
LinkDB: A0A093YJ82_9PEZI
Original site: A0A093YJ82_9PEZI 
ID   A0A093YJ82_9PEZI        Unreviewed;       412 AA.
AC   A0A093YJ82;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   31-JUL-2019, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY05111.1};
GN   ORFNames=O988_00266 {ECO:0000313|EMBL:KFY05111.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFY05111.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFY05111.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFY05111.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A.,
RA   Gerasimov E.S., Kochkina G.A., Ivanushkina N.E., Vasilenko O.V.,
RA   Kondrashov A.S., Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence
RT   of horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY05111.1}.
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DR   EMBL; JPJR01000044; KFY05111.1; -; Genomic_DNA.
DR   EnsemblFungi; KFY05111; KFY05111; O988_00266.
DR   Proteomes; UP000029329; 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:UP000029329};
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:UP000029329};
KW   Serine protease {ECO:0000256|RuleBase:RU003355,
KW   ECO:0000256|SAAS:SAAS01201831}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     20       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        21    412       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5001894405.
FT   DOMAIN       42    117       Inhibitor I9. {ECO:0000259|Pfam:PF05922}.
FT   DOMAIN      164    388       Peptidase_S8. {ECO:0000259|Pfam:PF00082}.
SQ   SEQUENCE   412 AA;  42604 MW;  5E18CF14C906DA87 CRC64;
     MKFTQNLIAL AACFLPLIAG IPTAQPHMKI QNPAAKNVIP NSYIVVFNKD IDSAAIKSEY
     ASVNSMLSKR GSAHKGIGSK YDLEHFKGYQ IEADTATIDQ IASSPQVAWI EKDAKVHANA
     LTTRSGAPWG LNSISHKASN GTTRGIFYRQ TNSTSDYTYD DSAGSGATVY IVDTGIFIEH
     KEFEGRATWG KNFIEGSKDT DENGHGTHCA GTIGGATYGV SNKAKLVAVK VLDGEGSGSN
     SGVIAGIEWV GKNAGPKSVL SMSLGGEFSE ALNAAAASTI KAGVTVVVAA GNDGADASKY
     SPASAPDAIT VGAIDKTNTR ADFSNFGPVL DVFAPGVDVL SAWIGSPDAQ NTISGTSMAT
     PHVAGLAAYL IGLENLATPA AVVARIQDLA SKGAIPNPEN SKNYLAYNGN GA
//
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