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Database: UniProt
Entry: Q6CCD1_YARLI
LinkDB: Q6CCD1_YARLI
Original site: Q6CCD1_YARLI 
ID   Q6CCD1_YARLI            Unreviewed;       493 AA.
AC   Q6CCD1;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   05-JUL-2017, entry version 72.
DE   SubName: Full=YALI0C10494p {ECO:0000313|EMBL:CAG81988.1};
GN   ORFNames=YALI0_C10494g {ECO:0000313|EMBL:CAG81988.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG81988.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG81988.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; CR382129; CAG81988.1; -; Genomic_DNA.
DR   RefSeq; XP_501681.1; XM_501681.1.
DR   ProteinModelPortal; Q6CCD1; -.
DR   STRING; 4952.XP_501681.1; -.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; CAG81988; CAG81988; YALI0_C10494g.
DR   GeneID; 2909472; -.
DR   KEGG; yli:YALI0C10494g; -.
DR   HOGENOM; HOG000253244; -.
DR   InParanoid; Q6CCD1; -.
DR   KO; K01268; -.
DR   OMA; SIVNWEL; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
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:UP000001300};
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:UP000001300};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   493 AA;  54451 MW;  067E0B82C6A184F6 CRC64;
     MRTRQTPRTP VRETASLPDM DSLSLKDDCA RAKRFCDFMD TSPTTYHAVH YLSKDLENAG
     FRPLNERDSW EDEFHTHDKF YVTRNGSSII AFVVGKDWTP GNGAGVVGTH IDALCAKVKP
     ISKKTPVDGY TLLGAAPYSG AFSDTWWDRD LGIAGRIICR DGNNKVTSKL VHVPYPIARI
     PTLAPHFGAP ANPPFNKETQ MTPVIGLTSS KEISEPTEDE KLSPLVGKHS IDLLRTLSKH
     SGVAVKDMLQ MDMELFDTQK AALGGLNQDF IFCPRIDDKV CTYTAVQGFI ESVPDMDPRA
     LNIVVCFDNE EVGSNTRQGA QGGLLESVVE RVISHGMDAS VANLAEEYKR KTYANSFFCS
     ADVNHAVNPN FSNIYLEHHK PQLNYGMTLA VDPNAHMTTD AVSLGFIEEV ARRGKNKTQY
     FQIRNDSRSG GTIGPYISSS TGMRSIDLGI AQLSMHSIRA TIGSKDVALG TKFFKNFYEL
     WFGVDEEFNK GGI
//
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