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Database: UniProt
Entry: U2A2C2_9PSED
LinkDB: U2A2C2_9PSED
Original site: U2A2C2_9PSED 
ID   U2A2C2_9PSED            Unreviewed;       429 AA.
AC   U2A2C2;
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=N878_12965 {ECO:0000313|EMBL:ERI54050.1};
OS   Pseudomonas sp. EGD-AK9.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1386078 {ECO:0000313|EMBL:ERI54050.1, ECO:0000313|Proteomes:UP000016488};
RN   [1] {ECO:0000313|EMBL:ERI54050.1, ECO:0000313|Proteomes:UP000016488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EGD-Ak9 {ECO:0000313|Proteomes:UP000016488};
RA   Kapley A., Sagarkar S., Bhardwaj P., Qureshi A., Khardenavis A.,
RA   Purohit H.J.;
RT   "Indian agricultural soil isolates capable of pesticide degradation.";
RL   Submitted (AUG-2013) 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:ERI54050.1}.
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DR   EMBL; AVOF01000045; ERI54050.1; -; Genomic_DNA.
DR   RefSeq; WP_021442100.1; NZ_AVOF01000045.1.
DR   EnsemblBacteria; ERI54050; ERI54050; N878_12965.
DR   PATRIC; fig|1386078.3.peg.463; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000016488; 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:ERI54050.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016488};
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:UP000016488};
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       156    156       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
FT   METAL       401    401       Zinc. {ECO:0000256|HAMAP-Rule:MF_00467}.
SQ   SEQUENCE   429 AA;  46924 MW;  79F02C205A76860B CRC64;
     MREELNQGLI DFLNASPTPF HATTSLAMRL EAAGYRHLDE RAPWHTEAGG RYYVTRNDSS
     LIAFKLGKRP AVDGGIRLVG AHTDSPCLRV KPNPELQRQG FFQLGVEVYG GALLAPWFDR
     DLSLAGRVTY RRDGKVESQL IDFYQPIAVI PSLAIHLNRE ANQGWAINPQ NELPPILAQL
     ASSETADFRA LLSEQLAMEH DFNADAVLDY ELSFYDTQSA AIVGLNQDFI AGARLDNLLS
     CYAGLQALID SSDEETCVLV CTDHEEVGSC SACGADGPFL EQVLRRVLPE GDAFVRTIQR
     SLLVSADNAH GVHPNYADKH DGNHGPKLNA GPVIKINSNQ RYATNSETAG FFRHLCLENE
     VPVQSFVVRS DMACGSTIGP LTASQLGVRT VDIGLPTFAM HSIRELAGSH DLEHLVKVLS
     AFYSSPELP
//
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