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Database: UniProt
Entry: D4M2Q5_9FIRM
LinkDB: D4M2Q5_9FIRM
Original site: D4M2Q5_9FIRM 
ID   D4M2Q5_9FIRM            Unreviewed;       466 AA.
AC   D4M2Q5;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   22-NOV-2017, entry version 38.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=RTO_08080 {ECO:0000313|EMBL:CBL25517.1};
OS   Ruminococcus torques L2-14.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Blautia.
OX   NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25517.1, ECO:0000313|Proteomes:UP000008956};
RN   [1] {ECO:0000313|EMBL:CBL25517.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL25517.1,
RC   ECO:0000313|Proteomes:UP000008956};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus torques L2-14.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL25517.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL25517.1,
RC   ECO:0000313|Proteomes:UP000008956};
RA   Pajon A.;
RL   Submitted (MAR-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; FP929055; CBL25517.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4M2Q5; -.
DR   STRING; 657313.RTO_08080; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; CBL25517; CBL25517; RTO_08080.
DR   KEGG; rto:RTO_08080; -.
DR   PATRIC; fig|657313.3.peg.487; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   BioCyc; RTOR657313:G13EB-704-MONOMER; -.
DR   Proteomes; UP000008956; 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:CBL25517.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008956};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CBL25517.1};
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:UP000008956};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   466 AA;  51797 MW;  650AA4FDB498A64B CRC64;
     MDRKNAWTTY SKEELDRLEQ VNTEYKNCLD AGKTERECVT LAVEKAKAEG YKDIRDIIKN
     GEKVKAGDKL YAVCMNKTIA LFHMGTKPLT EGMNILGAHI DSPRIDVKQN PLYENEEFAY
     LDTHYYGGIK KYQWVTLPLA LHGVIAKKDG TTVQVSIGEK EDDPVFVITD LLIHLASKQM
     EKKAATVVEG EKLDLLIGSR PIEQDETLEE KEKEAVKANV INLLKQYYDM EEEDFLSAEL
     EIVPAGKARD CGLDRSMVLA YGQDDRVCAF TSLFAMLDVE EVEHTACCIL VDKEEIGSVG
     ATGMHSRFFE NTVAELVALT EGESDLKVRR ALMNSRMLSS DVSAAYDPMY AEVFEKRSSA
     FFGKGLVFNK FTGARGKSGS NDANAEYLAK IRNAMDAQSV AYQFAELGKV DAGGGGTIAY
     IMANYGMEVI DSGVAVLSMH APWEVTSKAD VYEAYKGYKA FIEEMR
//
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