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Database: UniProt
Entry: M3JDX5_CANMX
LinkDB: M3JDX5_CANMX
Original site: M3JDX5_CANMX 
ID   M3JDX5_CANMX            Unreviewed;       522 AA.
AC   M3JDX5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   22-NOV-2017, entry version 18.
DE   SubName: Full=Vacuolar aminopeptidase I {ECO:0000313|EMBL:EMG50408.1};
GN   ORFNames=G210_4545 {ECO:0000313|EMBL:EMG50408.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG50408.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG50408.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial
RT   strain for xylitol and ethanol production.";
RL   Submitted (FEB-2013) 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:EMG50408.1}.
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DR   EMBL; AOGT01000279; EMG50408.1; -; Genomic_DNA.
DR   EnsemblFungi; EMG50408; EMG50408; G210_4545.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000011777; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EMG50408.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011777};
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:UP000011777};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
FT   COILED        8     35       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   522 AA;  56902 MW;  7D4F016DC9D9AE5A CRC64;
     MSNIDDILAG LTESLKRLQQ ASEQKLADEQ NAKVESQKPS QSPLTKGTKF TNEYYSKIAD
     DYIEFTYKNP TIYHVVQTFK KQLEDNGFTY LPESSSWSDL KAGKYFTVRN GSSLAAFVVG
     DKWTPSNGVG AIGSHIDSLT TVLKPNSTKA KVDGYELLGV APYAGTLGDV WWDRDLGVGG
     RLLVKGKSGK VSQQLVDSTP HPIAHIPTLA PHFGAPANGP FNTETQAVPV IGFTGEGDED
     EEEPATEAEK NAPLYGKHPL KLLRYIAGLA DVEVADILQW DLQLYDIQKG TKGGLKKEFV
     FAPRVDDRVC SFAALNALID STVDGTLAKD SFSIVGLYDN EEIGSLTRQG AKGGLIELVV
     NRVLSSEFVN PEGVDIQESL RLTYANSIIL SADVNHLLNP NFAQVYLDHH KPLPNVGVTL
     SLDPNGHMAT DSIGLALAEE LARKNGDKVQ YFQIRNDSRS GGTIGPSISV QTGARTIDLG
     IPQLSMHSIR ATLGSKDIGL GIKFFYGFFK NWRETYNDFV DL
//
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