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Database: UniProt
Entry: A0A0L0NQV8_9ASCO
LinkDB: A0A0L0NQV8_9ASCO
Original site: A0A0L0NQV8_9ASCO 
ID   A0A0L0NQV8_9ASCO        Unreviewed;       495 AA.
AC   A0A0L0NQV8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-SEP-2017, entry version 13.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KND96458.1};
GN   ORFNames=QG37_07195 {ECO:0000313|EMBL:KND96458.1};
OS   [Candida] auris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora;
OC   Clavispora/Candida clade.
OX   NCBI_TaxID=498019 {ECO:0000313|EMBL:KND96458.1, ECO:0000313|Proteomes:UP000037122};
RN   [1] {ECO:0000313|EMBL:KND96458.1, ECO:0000313|Proteomes:UP000037122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6684 {ECO:0000313|EMBL:KND96458.1,
RC   ECO:0000313|Proteomes:UP000037122};
RA   Alampalli S.V., Chatterjee S., Nageshan R.K., Joshi S.,
RA   Thiruganasambandam S.C., Tatu U.S.;
RT   "Draft Genome of a commonly misdiagnosed multidrug resistant pathogen
RT   Candida auris.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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:KND96458.1}.
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DR   EMBL; LGST01000055; KND96458.1; -; Genomic_DNA.
DR   RefSeq; XP_018166182.1; XM_018316006.1.
DR   EnsemblFungi; KND96458; KND96458; QG37_07195.
DR   GeneID; 28880866; -.
DR   KEGG; caur:QG37_07195; -.
DR   KO; K01268; -.
DR   Proteomes; UP000037122; 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:UP000037122};
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:UP000037122};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   495 AA;  54493 MW;  9A7A88DF447D7019 CRC64;
     MTLRTRDAFA LLSVTEESLG TRSKVVTKNA KENCEMYARN YVDFTYLNPT VWHVTRHFGE
     ALKKAGFQYL PEKELWAGIE PGKYYTTRSG SSLVAFAIGE DWVPEIGIGA IGSHIDALAT
     SVKPISLKDN KDGYNLLGVA PYAGALSSQW WDRDLGIGGR VLVKIDGKVK YVYVDSTPQP
     VARISTLAPH FGTPANGPFN KETQTVPIIG YGGSEEEPTE NEKKSPLYGK HSLKLLRYVA
     HRIGYRVEDM LQWDLQLYDV QRGAVGGLDN EFLFAPRIDD RVCSYAAIHA LIEAAAAKKI
     SNDSFAIVGL FDNEEVGSGT RQGAQGRLFL SVVERVIASS YYNPGDLDAT DQVKVAFANS
     IILSADVTHL FNPNFPDVYL EHHKPVPNKG MTVALDPNGH MATDSKGLAL IEQIAKKNGD
     ELQYFQIRND SRSGGTIGPY LSVQTGSRTI DLGIPQLSMH SIRAAIGSKD IGLAVNFFKG
     FFKHWRSTYD AFVQD
//
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