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Database: UniProt
Entry: U2PSX7_9CLOT
LinkDB: U2PSX7_9CLOT
Original site: U2PSX7_9CLOT 
ID   U2PSX7_9CLOT            Unreviewed;       431 AA.
AC   U2PSX7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   22-NOV-2017, entry version 22.
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   ORFNames=CINTURNW_3201 {ECO:0000313|EMBL:ERK29530.1};
OS   Clostridium intestinale URNW.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1294142 {ECO:0000313|EMBL:ERK29530.1, ECO:0000313|Proteomes:UP000016721};
RN   [1] {ECO:0000313|EMBL:ERK29530.1, ECO:0000313|Proteomes:UP000016721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=URNW {ECO:0000313|EMBL:ERK29530.1,
RC   ECO:0000313|Proteomes:UP000016721};
RX   PubMed=24136853;
RA   Lal S., Ramachandran U., Zhang X., Sparling R., Levin D.B.;
RT   "Draft Genome Sequence of the Hydrogen- and Ethanol-Producing
RT   Bacterium Clostridium intestinale Strain URNW.";
RL   Genome Announc. 1:e00871-13(2013).
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:ERK29530.1}.
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DR   EMBL; APJA01000016; ERK29530.1; -; Genomic_DNA.
DR   RefSeq; WP_021803171.1; NZ_KI273145.1.
DR   EnsemblBacteria; ERK29530; ERK29530; CINTURNW_3201.
DR   PATRIC; fig|1294142.3.peg.3348; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000016721; 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   HAMAP; MF_00467; Aminopeptidase_M18_2; 1.
DR   InterPro; IPR022984; M18_aminopeptidase_2.
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|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ERK29530.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016721};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00467,
KW   ECO:0000256|RuleBase:RU004386};
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:UP000016721};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00467, ECO:0000256|RuleBase:RU004386}.
FT   METAL        82     82       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       159    159       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       407    407       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   431 AA;  48156 MW;  A3D00B86CFB57F31 CRC64;
     MEKVIAKELL DFLYDSPTAF HAVENISEIL MKQGFKELKE EDKWKLKKEG KYFVKKNDSA
     LIAFVVGEDT PQEKGFKIIG AHTDSPGFRI KPRPEMIAEN VYLKLNTEVY GGPILATWFD
     RPLALAGRVT LKSDNPLYPK MEFLNINRPI LIIPSLAIHM NRNVNQGVEI NRQKDVLPLM
     TMINDSLEKD NLLLQVISEE LNVSKEEIID FDLFPYEFEK GSLIGLKEEF ISSARLDDLS
     MVHAGLKALT AVKSSKGTNI LACFDNEEVG SSTKQGADSE LLASVLERIV IALKGDREDY
     LRSLAKSFII SADLAHAVHP NYGEKHDPQL RPVINGGPVI KIAASQSYTT DAESSAVYEM
     ICKKAGVPYQ KFANRSDSRG GSTIGPINST HLNIRSVDMG NPVLGMHSIR ELGGVKDHYY
     CIKSFEEFYK L
//
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