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Database: UniProt
Entry: C0QL03_DESAH
LinkDB: C0QL03_DESAH
Original site: C0QL03_DESAH 
ID   C0QL03_DESAH            Unreviewed;       454 AA.
AC   C0QL03;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   28-FEB-2018, entry version 56.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=HRM2_31620 {ECO:0000313|EMBL:ACN16243.1};
OS   Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfobacterium.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN16243.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN16243.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J.,
RA   Andres S., Henne A., Fricke W.F., Martinez-Arias R., Bartels D.,
RA   Goesmann A., Krause L., Puehler A., Klenk H.P., Richter M.,
RA   Schuler M., Gloeckner F.O., Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine
RT   sulfate reducer oxidizing organic carbon completely to carbon
RT   dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN16243.1; -; Genomic_DNA.
DR   RefSeq; WP_015905005.1; NC_012108.1.
DR   ProteinModelPortal; C0QL03; -.
DR   STRING; 177437.HRM2_31620; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ACN16243; ACN16243; HRM2_31620.
DR   KEGG; dat:HRM2_31620; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; DAUT177437:G1GC3-3135-MONOMER; -.
DR   Proteomes; UP000000442; 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   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACN16243.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000442};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ACN16243.1};
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:UP000000442};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   454 AA;  50309 MW;  57ADE88A7EFDAF91 CRC64;
     MPPEKQPPDK FNQAKFNQEL FTFIDNSPTP FHAVRSMEKA LNKQGFIHLD EGDAWHLETN
     GCYYVTRNNS SLIAFKMGGT PPWETGIKII GAHTDSPCLR VKPSPLQRQD SMTRLGCEVY
     GGTLLNTWFD RGLNLAGRVT CRTVEKGKER IQSFLINYNR PVAIIPSLAI HLDREANTNR
     TVNPEVHISP LFSLDDQMNN PEQNDSFKAI LLKRVNEEHP SHELVEVMAH ELSFSHAEPC
     FYTGLDREII SAPRLDNLLS CHSALKSLWS AAPCTTAMVV FADNEEVGSE TRTGARGSFL
     QSILSRMTQT PEQLARTTAR SFMISCDNAH GVHPAFREKH EPNHRPLLNT GPVLKINASQ
     RYATNSESGA VFKEICAGAK LVVQDFVMRS DLACGSTIGP AIAARAGIRT VDVGAATLAM
     HSVREVTGAK DPMMMFKALN HYLSLDELPL LSLT
//
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