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Database: UniProt
Entry: E4RP25_HALHG
LinkDB: E4RP25_HALHG
Original site: E4RP25_HALHG 
ID   E4RP25_HALHG            Unreviewed;       468 AA.
AC   E4RP25;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   22-NOV-2017, entry version 39.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Halsa_0375 {ECO:0000313|EMBL:ADQ13850.1};
OS   Halanaerobium hydrogeniformans (Halanaerobium sp. (strain
OS   sapolanicus)).
OC   Bacteria; Firmicutes; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=656519 {ECO:0000313|EMBL:ADQ13850.1, ECO:0000313|Proteomes:UP000007434};
RN   [1] {ECO:0000313|EMBL:ADQ13850.1, ECO:0000313|Proteomes:UP000007434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=sapolanicus {ECO:0000313|Proteomes:UP000007434};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Begemann M.B., Mormile M.R., Wall J.D., Elias D.A., Woyke T.;
RT   "Complete sequence of Halanaerobium sp. sapolanicus.";
RL   Submitted (NOV-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}.
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DR   EMBL; CP002304; ADQ13850.1; -; Genomic_DNA.
DR   RefSeq; WP_013404956.1; NC_014654.1.
DR   STRING; 656519.Halsa_0375; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ADQ13850; ADQ13850; Halsa_0375.
DR   KEGG; has:Halsa_0375; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000007434; Chromosome.
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:ADQ13850.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007434};
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:UP000007434};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  52213 MW;  EE7614D0EEF81C0E CRC64;
     MSEEKKQKDK FSYEAKNAWL EMGEDEREEV FSFNKEYADF LTANKTEREF VKAAVKKLEA
     AGFKNIKQYE ELKKGDKIYV LNRSRALMAA VIGEKELTDG LKIVGSHIDS PRLDLKPNPL
     YEAGELGLFK THYYGGVKKY QWVTMPLALH GIVVKDDGTE VEINIGEKES DPIFFISDLL
     PHLGKSQMKK SMKEGITGEK LNLVVGSIPV ADEDAKEKIK TAILEHLNKE YGIKEEDFMS
     ADLQAVPAFK TRDAGFDRGL LAGYGHDDRV CSFTALEAIL DLGQPKYTSM ILLMDREEVG
     SMGSTGMQSH FFEDQLANLV DLYYDSYSEL LLRRVMQNSK VISADVNAAY DPDFAELYAK
     YNSAYLGKGI VISKYTGARG KAGASEASAE FMAEIRGLFN NKGVIWQTAE LGRIDEGGGG
     TIAKFLANYN MDVVDSGPPV LSMHSPYEVV SKVDVYNSYL AYNVFLEN
//
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