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Database: UniProt
Entry: A0A151ANF2_9CLOT
LinkDB: A0A151ANF2_9CLOT
Original site: A0A151ANF2_9CLOT 
ID   A0A151ANF2_9CLOT        Unreviewed;       434 AA.
AC   A0A151ANF2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-MAR-2018, entry version 13.
DE   RecName: Full=Probable M18 family aminopeptidase 2 {ECO:0000256|HAMAP-Rule:MF_00467};
DE            EC=3.4.11.- {ECO:0000256|HAMAP-Rule:MF_00467};
GN   Name=apeB {ECO:0000256|HAMAP-Rule:MF_00467,
GN   ECO:0000313|EMBL:KYH29153.1};
GN   ORFNames=CLCOL_12900 {ECO:0000313|EMBL:KYH29153.1};
OS   Clostridium colicanis DSM 13634.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121305 {ECO:0000313|EMBL:KYH29153.1, ECO:0000313|Proteomes:UP000075374};
RN   [1] {ECO:0000313|EMBL:KYH29153.1, ECO:0000313|Proteomes:UP000075374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13634 {ECO:0000313|EMBL:KYH29153.1,
RC   ECO:0000313|Proteomes:UP000075374};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium colicanis DSM 13634.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00467, ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00467, 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:KYH29153.1}.
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DR   EMBL; LTBB01000005; KYH29153.1; -; Genomic_DNA.
DR   RefSeq; WP_061858157.1; NZ_LTBB01000005.1.
DR   EnsemblBacteria; KYH29153; KYH29153; CLCOL_12900.
DR   PATRIC; fig|1121305.3.peg.1292; -.
DR   Proteomes; UP000075374; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.250.10; -; 1.
DR   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
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|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KYH29153.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000075374};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KYH29153.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075374};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        84     84       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       161    161       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       409    409       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   434 AA;  48675 MW;  3C74AF3466889136 CRC64;
     MTKELEFAKE LIDFIYESPT AFHAVENVKN TLEQNGFKQL KEEEKWKLEK GKKYFMIKNH
     SALIAFTVGN EKIEENGFRI IGAHTDSPSF RVKPNPEMTS ENSYIKLNTE VYGGPILNTW
     FDRPLSLAGR VIIKGKNILN PKVKLLNIKK PVMIIPNLAI HMNRKVNEGI ELNKQVDTLP
     ILGLINEKFE KDNYLAKVIA DELKVDYKDI LDFDLFLYEY EKGSIIGINN EFISSSRLDD
     LEAVHGGVHA LINAENPVST NVLVCFDNEE VGSATKQGAD SEMLSNVLER IVLSLDGNRD
     DFFRVLAKSF MISADAAHAV HPNKGQKSDP TNRPFINKGP AVKIAASQSY TSDSYSTSIF
     VSLCEKAGVP VQKFVNRSDE RGGSTIGPIS STHINIPSVD IGTPMLAMHS IRELCGVMDH
     YYVARVFKKF YELH
//
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