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Database: UniProt
Entry: G3AQC0_SPAPN
LinkDB: G3AQC0_SPAPN
Original site: G3AQC0_SPAPN 
ID   G3AQC0_SPAPN            Unreviewed;       518 AA.
AC   G3AQC0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   30-AUG-2017, entry version 30.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGW31467.1};
GN   ORFNames=SPAPADRAFT_62038 {ECO:0000313|EMBL:EGW31467.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW31467.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A.,
RA   LaButti K.M., Sun H., Clum A., Pangilinan J.L., Lindquist E.A.,
RA   Lucas S., Lapidus A., Jin M., Gunawan C., Balan V., Dale B.E.,
RA   Jeffries T.W., Zinkel R., Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GL996503; EGW31467.1; -; Genomic_DNA.
DR   RefSeq; XP_007376245.1; XM_007376183.1.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EGW31467; EGW31467; SPAPADRAFT_62038.
DR   GeneID; 18874161; -.
DR   KEGG; spaa:SPAPADRAFT_62038; -.
DR   InParanoid; G3AQC0; -.
DR   KO; K01268; -.
DR   OMA; SIVNWEL; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000709};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   518 AA;  57558 MW;  31EFC0E975E53ED7 CRC64;
     MSNSNTFNPE AFLELEQKIR DMMLVAEEAK RRYQETGETE TTSAVAKYSK EYYEKKADDY
     INFTYKNPTI YHVVSYFHEQ LNDAGFKYVS EKDSWEDLTP GRYFTTRNGS SLVAFVVGQH
     WKPKRGVGII GSHIDALTTV LKPNSTKDNV DGYELLGVAP YAGTLGEIWW DRDLGVGGRL
     LVKNSSGKIV QKLVDSTPHP IAHIPTLAPH FGTPANGPFN KETQAVPVIG FAGESDEEAE
     PTSEEKEAPL YGKHPLKLLR YIAGLADVKV SDILQWDLQL YDVQKGVKGG LRKEFVFAPR
     VDDRVCSFAA LHALIEADAS DYLKSDAFSL VALVDNEEIG SATRQGIKGG LIEQAVSRIL
     ATKFFNPESF DIQEQLRATY ANTIILSSDV NHLLNPNFKE VYLEHHKPVP NKGITVALDP
     NGHMATDSTG LALIEELARK NDDKLQYFQI RNDSRSGGTI GPSISLQTGA RTIDLGIPQL
     SMHSIRAALG TKDIGLGIKF FTGFFKNWRE TYDNFVDL
//
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