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Database: UniProt
Entry: D4LP99_9FIRM
LinkDB: D4LP99_9FIRM
Original site: D4LP99_9FIRM 
ID   D4LP99_9FIRM            Unreviewed;       464 AA.
AC   D4LP99;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   25-OCT-2017, entry version 41.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CK1_40050 {ECO:0000313|EMBL:CBL21660.1};
OS   Ruminococcus sp. SR1/5.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=657323 {ECO:0000313|EMBL:CBL21660.1, ECO:0000313|Proteomes:UP000007055};
RN   [1] {ECO:0000313|EMBL:CBL21660.1, ECO:0000313|Proteomes:UP000007055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SR1/5 {ECO:0000313|EMBL:CBL21660.1,
RC   ECO:0000313|Proteomes:UP000007055};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus sp. SR1/5.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL21660.1, ECO:0000313|Proteomes:UP000007055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SR1/5 {ECO:0000313|EMBL:CBL21660.1,
RC   ECO:0000313|Proteomes:UP000007055};
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; FP929053; CBL21660.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4LP99; -.
DR   STRING; 657323.CK1_40050; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; CBL21660; CBL21660; CK1_40050.
DR   KEGG; rum:CK1_40050; -.
DR   PATRIC; fig|657323.3.peg.3710; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   BioCyc; RSP657323:G13D6-3284-MONOMER; -.
DR   Proteomes; UP000007055; 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   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:CBL21660.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007055};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CBL21660.1};
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:UP000007055};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   464 AA;  50978 MW;  E90C121CE6005839 CRC64;
     MERRNAWLSY KEAEETEMEK LAKAYREFLD KGKTERECVA EIVKEAEAAG YESLESKLEK
     GEKIKAGDKV YAVGMKKIVA LFHVGTEELS GGMSILCAHI DSPRLDIKQN PLYEDTDLAY
     LDTHYYGGVK KYQWVTLPLA MHGVVAKKDG SIVEISIGED VEDPVLYITD LLIHLSGKQL
     QKKAAEVIEG EMLDILIGSR PLAELPDDSK KDAVKQNVLK ILNEKYGIEE EDFLSAELEI
     VPAGKARDCG LDRSMIAAYG QDDRVCAYTS LAAMLEMEET PKRTGCCLLV DKEEIGSVGA
     TGMQSRFFEN SVAELLDGMG CYSELALRRA LRNSSMLSSD VSAGYDPAYG EAFEKKNAAY
     LGRGIVLNKF TGARGKSGSN DANAEYVARV RRIFDDHNVA FQTAELGKVD FGGGGTIAYI
     AALYGMEVID SGVAVLSMHA PWEVTSKADV YEAYKAYKAF LLDA
//
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