ID C4Y2A4_CLAL4 Unreviewed; 502 AA.
AC C4Y2A4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 28-FEB-2018, entry version 41.
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 EuPathDB; FungiDB: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 Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
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 Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT COILED 3 23 {ECO:0000256|SAM:Coils}.
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
//