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Database: UniProt
Entry: A0A0M2CYK3_9MICC
LinkDB: A0A0M2CYK3_9MICC
Original site: A0A0M2CYK3_9MICC 
ID   A0A0M2CYK3_9MICC        Unreviewed;       439 AA.
AC   A0A0M2CYK3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   22-NOV-2017, entry version 9.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=H488_0101955 {ECO:0000313|EMBL:EYT55422.1};
OS   Kocuria sp. UCD-OTCP.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX   NCBI_TaxID=1292021 {ECO:0000313|EMBL:EYT55422.1, ECO:0000313|Proteomes:UP000033173};
RN   [1] {ECO:0000313|EMBL:EYT55422.1, ECO:0000313|Proteomes:UP000033173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-OTCP {ECO:0000313|EMBL:EYT55422.1,
RC   ECO:0000313|Proteomes:UP000033173};
RX   PubMed=23661474;
RA   Coil D.A., Doctor J.I., Lang J.M., Darling A.E., Eisen J.A.;
RT   "Draft Genome Sequence of Kocuria sp. Strain UCD-OTCP (Phylum
RT   Actinobacteria).";
RL   Genome Announc. 1:E00172-13(2013).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
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:EYT55422.1}.
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DR   EMBL; AOSQ01000002; EYT55422.1; -; Genomic_DNA.
DR   RefSeq; WP_017832094.1; NZ_AOSQ01000002.1.
DR   EnsemblBacteria; EYT55422; EYT55422; H488_0101955.
DR   Proteomes; UP000033173; 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   ECO:0000313|EMBL:EYT55422.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033173};
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   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   439 AA;  46247 MW;  7D8A2EE22B3411A9 CRC64;
     MEPRTAVDPR SAVEDLGRYV MESPSSFHAA HAAAARLEEA GFVRLDETED WARTGVRGRR
     YVLRDGAVIA WATPAEVPPA AGFRILGAHT DSPGFKLKPR PTTTAHTWHQ AGVETYGGAL
     LNSWLDRELR LAGRLVVRGT DGAPVEHLTA TGPVARIPQL AIHLDREANK GLQLDRQQHV
     QPIWGVGQPE DADVLALLAE HADGGPVDPA RIVGYDVVLA DAQPPAVFGQ GGTLFASGRL
     DNLSSVHAGL SALAREAEAV EQGRHIAVLA AFDHEEIGSR TRSGAAGPFL EDVLVRIGEG
     LGRSAAEHRR SLAGSVCLSA DAGHLVHPNY QGHHDPVNRP VPGAGPLLKI NADQHYATDA
     VGAGIWAEAC ARAGVGYQEF VSNNRVPCGS TIGPITAARL GVRTIDVGIG LLSMHSAREL
     CHVDDVAALG AVAGAFYTA
//
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