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Database: UniProt
Entry: E4KPH7_9LACT
LinkDB: E4KPH7_9LACT
Original site: E4KPH7_9LACT 
ID   E4KPH7_9LACT            Unreviewed;       439 AA.
AC   E4KPH7;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   22-NOV-2017, entry version 34.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF9257_1465 {ECO:0000313|EMBL:EFR30967.1};
OS   Eremococcus coleocola ACS-139-V-Col8.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Aerococcaceae;
OC   Eremococcus.
OX   NCBI_TaxID=908337 {ECO:0000313|EMBL:EFR30967.1, ECO:0000313|Proteomes:UP000005990};
RN   [1] {ECO:0000313|EMBL:EFR30967.1, ECO:0000313|Proteomes:UP000005990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACS-139-V-Col8 {ECO:0000313|EMBL:EFR30967.1,
RC   ECO:0000313|Proteomes:UP000005990};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:EFR30967.1}.
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DR   EMBL; AENN01000015; EFR30967.1; -; Genomic_DNA.
DR   RefSeq; WP_006418170.1; NZ_AENN01000015.1.
DR   STRING; 908337.HMPREF9257_1465; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EFR30967; EFR30967; HMPREF9257_1465.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; ECOL908337-HMP:GMFB-302-MONOMER; -.
DR   Proteomes; UP000005990; 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:EFR30967.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005990};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EFR30967.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EFR30967.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005990};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   439 AA;  48976 MW;  14102B69162668E0 CRC64;
     MNHIEVSKDL VQFIQESPSM FHSNQSIAKR LEEAGYTYLS ESSTWQLEKD GHYYTKRNDS
     SIIAFQIGSD LSDYHFQMSA AHGDSPTFKI KSVPELEGPA EYLRLNVEAY GGMIDSTWFD
     RPLSIAGRVL VEEGNKAVSK LLYIDKDLLI IPNVAIHFNR KINSGYDYNR QVDLLPLFSA
     GELKKGDFDK MIAEELGVDP DQILARDLFL VNRQAPSIWG YKDEFVSSPK LDNLQCSYST
     LMGFLAGDNP KAVNVYCNFD NEEVGSNTKQ GAMSTFLADT LKRINAALGF DLDQYHQAVA
     KSFLISADNA HAAHPNHIEK TDDQNRTFMN QGIVIKEAAN QKYTTDAFSQ AVFKRICKKA
     QVPVQNFANR SDTPGGSTLG NLSNTQVSVH ALDIGLPQLA MHSTYETAGS KDTLYMIEAL
     TTYFNSNIEI EAADYAQMD
//
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