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Database: UniProt
Entry: D2MLQ1_9FIRM
LinkDB: D2MLQ1_9FIRM
Original site: D2MLQ1_9FIRM 
ID   D2MLQ1_9FIRM            Unreviewed;       433 AA.
AC   D2MLQ1;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-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=HMPREF9013_1405 {ECO:0000313|EMBL:EFC06460.1};
OS   Bulleidia extructa W1219.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Bulleidia.
OX   NCBI_TaxID=679192 {ECO:0000313|EMBL:EFC06460.1, ECO:0000313|Proteomes:UP000005017};
RN   [1] {ECO:0000313|Proteomes:UP000005017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W1219 {ECO:0000313|Proteomes:UP000005017};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RT   "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL   Submitted (DEC-2009) 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:EFC06460.1}.
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DR   EMBL; ADFR01000001; EFC06460.1; -; Genomic_DNA.
DR   ProteinModelPortal; D2MLQ1; -.
DR   STRING; 679192.HMPREF9013_1405; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EFC06460; EFC06460; HMPREF9013_1405.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000005017; 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:EFC06460.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005017};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EFC06460.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EFC06460.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005017};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   433 AA;  48228 MW;  7070ECAC27D919EF CRC64;
     MQNVNEQLMK LIDASPTAYH AIDQVKKKLI RGGYTELLES EAWHLEEDGR YFVCRNGSSL
     LAFRVPVKDY HGFMIGAAHS DSPSFKLKEN GEIEKEGYLQ LNVEGYGGML MAPWFDRPLG
     IAGRVVVKEG KTFSSHLVDS KEAIAMIPNL AIHMDRQANE NHSYNIQNDL LPIIAQGKKD
     EQVLHYFAKK LEVEKEAILS HDLFLYPRNE AYIWGMNQEF LTAPRLDDLQ CAFANLYGFL
     AAKDSNSIPI MVIFDNEEVG SLTKQGADST FLSDCLNRIH QALGHDGKTY AQAIANSMMV
     SADNAHGVHP NYIGKHDPVN HPKLNEGIVI KFNANQHYTT DGISAALFKD ICQSQEIPFQ
     VFTNRSDVRG GSTLGNISNA HVSLVTVDVG LAQLAMHSPV ETAGVKDTTY MVEALAEFFS
     RSLIQTKSGY EWK
//
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