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Database: UniProt
Entry: E5XV31_9ACTN
LinkDB: E5XV31_9ACTN
Original site: E5XV31_9ACTN 
ID   E5XV31_9ACTN            Unreviewed;       452 AA.
AC   E5XV31;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 2.
DT   28-FEB-2018, entry version 35.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF9336_03353 {ECO:0000313|EMBL:EFV11867.2};
OS   Segniliparus rugosus ATCC BAA-974.
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=679197 {ECO:0000313|EMBL:EFV11867.2, ECO:0000313|Proteomes:UP000004816};
RN   [1] {ECO:0000313|EMBL:EFV11867.2, ECO:0000313|Proteomes:UP000004816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-974 {ECO:0000313|EMBL:EFV11867.2,
RC   ECO:0000313|Proteomes:UP000004816};
RX   PubMed=22675588; DOI=10.4056/sigs.2255041;
RA   Earl A.M., Desjardins C.A., Fitzgerald M.G., Arachchi H.M., Zeng Q.,
RA   Mehta T., Griggs A., Birren B.W., Toney N.C., Carr J., Posey J.,
RA   Butler W.R.;
RT   "High quality draft genome sequence of Segniliparus rugosus CDC
RT   945(T)= (ATCC BAA-974(T)).";
RL   Stand. Genomic Sci. 5:389-397(2011).
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:EFV11867.2}.
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DR   EMBL; ACZI02000001; EFV11867.2; -; Genomic_DNA.
DR   STRING; 679197.HMPREF9336_03353; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EFV11867; EFV11867; HMPREF9336_03353.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000004816; 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   Gene3D; 2.30.250.10; -; 1.
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|RuleBase:RU004386};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004816};
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   Reference proteome {ECO:0000313|Proteomes:UP000004816};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   452 AA;  47500 MW;  5034E17EC4A6948C CRC64;
     MTLETSLSAI GAPPTSFASG EAAPTPSPAD PGPNGLCAFV DASPTPFHAR QTVATILSAH
     GFAELWGTDE WPAVGGKHFV VRGASIIAWA APEDRPPAAF RIAAGHVDSP NLRVKQHADG
     SVAGWRTVAL EPYGGAWTHT WLDRDLGLAG RVVFREGASA VERLVEVPEP ILRVPQLAIH
     LAEERDAVRL NPQRHLNAVW GVGSEPRPIA AFLAERLDIA ADAILGFDLM AFDLAPSAVI
     GADRDLVSAP RLDNQASCHA GVQALLRAAE NAGPDSPVPV LALFDHEEIG SVSERGAASE
     FLTTVLERIV LASGGGRAEL LRAFAGSACA SADMAHATHP NYPDRHEPGH LIFAGKGPVL
     KVNQNLRYAT DGMGEALFAL ACQQADVPLQ RYMHRADLPC GSTVGPVLSA RTGMATVDVG
     APQLAMHSIR ELMAAADVEP YAKALAAFLG PR
//
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