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Database: UniProt
Entry: Q0ATX3_SYNWW
LinkDB: Q0ATX3_SYNWW
Original site: Q0ATX3_SYNWW 
ID   Q0ATX3_SYNWW            Unreviewed;       463 AA.
AC   Q0ATX3;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   22-NOV-2017, entry version 70.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Swol_2543 {ECO:0000313|EMBL:ABI69831.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI69831.1, ECO:0000313|Proteomes:UP000001968};
RN   [1] {ECO:0000313|Proteomes:UP000001968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI69831.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0ATX3; -.
DR   STRING; 335541.Swol_2543; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; ABI69831; ABI69831; Swol_2543.
DR   KEGG; swo:Swol_2543; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000056589; -.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; SWOL335541:GHL1-2540-MONOMER; -.
DR   Proteomes; UP000001968; 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:ABI69831.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001968};
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:UP000001968};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   463 AA;  51311 MW;  49E789606FC65555 CRC64;
     MSEQKENLKK NAWLRIKPAD LPMVHDFNQG YRDFLNQVKT EREAVAYIKQ AAQGHGFIDL
     DRVASLEPGQ KLFFQQKGKI CALVVIGQEA MENGVNMVVS HIDSPRLDLK ANPLYEADGL
     ALFKTHYYGG IKKYQWLAIP LALHGVVIKK DGQVVSVVIG EENDDFVLSI ADLLPHLAKE
     QMEKKMSEAI PAENLNILVG SQPLGDTADN PIKKQVLQIL QEKYAIEEED FSSAELQAVP
     AFQARDIGFD RSMIGAYGQD DRVCAYTSLR AALELEAPKR TAICLFVDKE EIGSNGNTGL
     QSLIIENLMA ELMSKAGYNN YLALRKSLAN SCALSADVNA AVDPNYPEVF EKMNCSFLSR
     GVVLTKYTGS RGKSNSNDAN PEFLARIRRL FDDNEVFWQV GELGKVDIGG GGTVAHYMAR
     YGMEVVDLGV ALLGMHSPFE VSSKVDVFLA YKAYRVFMQS FTN
//
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