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Database: UniProt
Entry: C4Y2A4_CLAL4
LinkDB: C4Y2A4_CLAL4
Original site: C4Y2A4_CLAL4 
ID   C4Y2A4_CLAL4            Unreviewed;       502 AA.
AC   C4Y2A4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   22-NOV-2017, entry version 39.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEQ38541.1};
GN   ORFNames=CLUG_02667 {ECO:0000313|EMBL:EEQ38541.1};
OS   Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida
OS   lusitaniae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Metschnikowiaceae; Clavispora.
OX   NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ38541.1, ECO:0000313|Proteomes:UP000007703};
RN   [1] {ECO:0000313|EMBL:EEQ38541.1, ECO:0000313|Proteomes:UP000007703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ38541.1,
RC   ECO:0000313|Proteomes:UP000007703};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L.,
RA   Agrafioti I., Arnaud M.B., Bates S., Brown A.J., Brunke S.,
RA   Costanzo M.C., Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L.,
RA   Hube B., Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R.,
RA   Neiman A.M., Nikolaou E., Quail M.A., Quinn J., Santos M.C.,
RA   Schmitzberger F.F., Sherlock G., Shah P., Silverstein K.A.,
RA   Skrzypek M.S., Soll D., Staggs R., Stansfield I., Stumpf M.P.,
RA   Sudbery P.E., Srikantha T., Zeng Q., Berman J., Berriman M.,
RA   Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CH408078; EEQ38541.1; -; Genomic_DNA.
DR   RefSeq; XP_002617223.1; XM_002617177.1.
DR   ProteinModelPortal; C4Y2A4; -.
DR   STRING; 306902.XP_002617223.1; -.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EEQ38541; EEQ38541; CLUG_02667.
DR   GeneID; 8497812; -.
DR   KEGG; clu:CLUG_02667; -.
DR   eggNOG; KOG2596; Eukaryota.
DR   eggNOG; COG1362; LUCA.
DR   InParanoid; C4Y2A4; -.
DR   KO; K01268; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000007703; 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   PANTHER; PTHR28570; PTHR28570; 1.
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:UP000007703};
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:UP000007703};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   502 AA;  54426 MW;  939D5BA0CE9D7B9D CRC64;
     MSLPQIEQQL RELLKDRNVA ELEALLKTSA SQNQTHHYDQ GYFDAHASAY IDFTYENPTI
     YHVVQHFAAQ LRDAGFVYLA EKDSWSSIKP GKYYTIRNGA ALVAFVVGSE WTPSKGVGAI
     GAHIDALTVS LKPNSTKPPV EGYELLGVAP YAGTLGAPWW DRDLGVGGRV WVRKDSKVSS
     RLVDSTPHPV AKIPTLAPHF GAPAVGPFNL ETQAVPVVGY VGDEPEPEPT SAEKASPLYG
     KHPLRLLRYV AKLAGVEVAD IVQWDLQLYD VQKGVRGGLQ SEFVFAPRVD DRVCSYAAIN
     ALLEADARGK LADDSFAAVA LFDSEEIGSG TRTGVRGQLL EAVVARVVAS DLYGGGAEQT
     RQTWANSVVL SADVNHLVNP NFAEVYLEKH KPVPNTGLAL ALDPNGHMAT DSVGVALMED
     LARQNDDKLQ YFQIRNDSRS GGTIGPYSAT QTGARTIDVG IPQLSMHSIR ATLGAKDIGL
     GTKFFAGFFA NWRSTYDKFT EL
//
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