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Database: UniProt
Entry: G3B676_CANTC
LinkDB: G3B676_CANTC
Original site: G3B676_CANTC 
ID   G3B676_CANTC            Unreviewed;       284 AA.
AC   G3B676;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   07-JUN-2017, entry version 19.
DE   SubName: Full=Peptidase M18, aminopeptidase I {ECO:0000313|EMBL:EGV63401.1};
GN   ORFNames=CANTEDRAFT_114712 {ECO:0000313|EMBL:EGV63401.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 /
OS   NBRC 10315 / NRRL Y-1498 / VKM Y-70) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Yamadazyma;
OC   Yamadazyma/Candida clade.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV63401.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A.,
RA   LaButti K.M., Sun H., Clum A., Pangilinan J.L., Lindquist E.A.,
RA   Lucas S., Lapidus A., Jin M., Gunawan C., Balan V., Dale B.E.,
RA   Jeffries T.W., Zinkel R., Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; GL996524; EGV63401.1; -; Genomic_DNA.
DR   RefSeq; XP_006687194.1; XM_006687131.1.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EGV63401; EGV63401; CANTEDRAFT_114712.
DR   GeneID; 18247546; -.
DR   KEGG; cten:CANTEDRAFT_114712; -.
DR   KO; K01268; -.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000000707; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EGV63401.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000707};
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:UP000000707};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   284 AA;  31252 MW;  F09A6F1FBA129250 CRC64;
     MVPVIGFDTE PEVPIDHPLA DRHSAKLLRY VSSISDVPVD DIVELELELY DTQKAVIGGL
     KGEFVFAPRL DDRLCSWAAI YGLIEYANLY DSDSLAAHDG LSMVLLVDSE EIGSGTRTGV
     KGKFLNATID KILVIKKQPP VQSVVFANSI LLSADVTHLM NPNFKSAYLD KHYPLPNTGM
     TIKIDANGHV ASEYVGYNLL KTLTSQNQLK LQQFHIRNDA SSGGTIGPYL ATATGARVID
     IGLPILSMHS VRAMCGSEDV QNGVDFFKAF FEGWRQEYNK YRGL
//
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