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Database: UniProt
Entry: M3HGP8_CANMX
LinkDB: M3HGP8_CANMX
Original site: M3HGP8_CANMX 
ID   M3HGP8_CANMX            Unreviewed;       545 AA.
AC   M3HGP8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   22-NOV-2017, entry version 15.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EMG46447.1};
GN   ORFNames=G210_3307 {ECO:0000313|EMBL:EMG46447.1};
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:EMG46447.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG46447.1, 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:EMG46447.1}.
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DR   EMBL; AOGT01002005; EMG46447.1; -; Genomic_DNA.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EMG46447; EMG46447; G210_3307.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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   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}.
SQ   SEQUENCE   545 AA;  60810 MW;  992024FE2F77AF19 CRC64;
     MSTTPETSDN ELESLSTPDI STIESTDIED NEYEDQDLAH GTILLDSNYV FKVPDMSQTI
     SQLPTPKESF RDYYETYSAK YIDFMTNNPT TNHTITHFKS LLENNGFTYL PDTKKIENLT
     PGFYFTSKDD QSLIAFVIGG KWEPSHGSCF IGSHCDALTV KLNPRGSLRE KIDGYELLGV
     APYSGSLNRL WLNRDLGLAG SVLVRDERTG KVSRKLINSS PDPIAFIPQL APHFGISKDE
     YNPQTEMVPI CGFSNDDEEL IPTDEEKKSK FYGRHSLALL RYISQLSNTP LSQIIDFDLD
     LVDVQPSHRG GLNNEFIYSG CLDDRLCAFT SVYGLIEYSQ RFYLNKDVES YDGLSGIYLA
     NNEEIGSGTR TGAKGGFFID ILKSIVSDKV KFHTQEAVAN LTTNTIFLST DVTHALNPNF
     KDVYLDKNFP VPNTGPSIKF DSNGHVLSDS KGNEFLTRII DELPGIKLQH FHIRNDSRSG
     GTIGPIMSDS KRGINGAKLI IDVGLPILSM HSIRSIAGYK DVGIGIRFFK QVLSKWQTTI
     NAMEQ
//
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