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Database: UniProt/TrEMBL
Entry: C6UMR0_ECOBR
LinkDB: C6UMR0_ECOBR
Original site: C6UMR0_ECOBR 
ID   C6UMR0_ECOBR            Unreviewed;       671 AA.
AC   C6UMR0;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   11-JUN-2014, entry version 42.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.2;
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN   Name=ligA; OrderedLocusNames=ECB_02311;
OS   Escherichia coli (strain B / REL606).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=413997;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B / REL606;
RX   PubMed=19786035; DOI=10.1016/j.jmb.2009.09.052;
RA   Jeong H., Barbe V., Lee C.H., Vallenet D., Yu D.S., Choi S.H.,
RA   Couloux A., Lee S.W., Yoon S.H., Cattolico L., Hur C.G., Park H.S.,
RA   Segurens B., Kim S.C., Oh T.K., Lenski R.E., Studier F.W.,
RA   Daegelen P., Kim J.F.;
RT   "Genome sequences of Escherichia coli B strains REL606 and
RT   BL21(DE3).";
RL   J. Mol. Biol. 394:644-652(2009).
CC   -!- FUNCTION: DNA ligase that catalyzes the formation of
CC       phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl
CC       groups in double-stranded DNA using NAD as a coenzyme and as the
CC       energy source for the reaction. It is essential for DNA
CC       replication and repair of damaged DNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-
CC       ribonucleotide + (deoxyribonucleotide)(n+m).
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 BRCT domain.
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DR   EMBL; CP000819; ACT39966.1; -; Genomic_DNA.
DR   RefSeq; YP_003045502.1; NC_012967.1.
DR   ProteinModelPortal; C6UMR0; -.
DR   SMR; C6UMR0; 1-586.
DR   STRING; 413997.ECB_02311; -.
DR   EnsemblBacteria; ACT39966; ACT39966; ECB_02311.
DR   GeneID; 8176788; -.
DR   KEGG; ebr:ECB_02311; -.
DR   PATRIC; 18236806; VBIEscCol118196_2416.
DR   eggNOG; COG0272; -.
DR   HOGENOM; HOG000218459; -.
DR   KO; K01972; -.
DR   OMA; FPAQEQL; -.
DR   OrthoDB; EOG6TTVM9; -.
DR   BioCyc; ECOL413997:GCQD-2525-MONOMER; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   HAMAP; MF_01588; DNA_ligase_A; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR018239; DNA_ligase_AS.
DR   InterPro; IPR001679; DNAligase.
DR   InterPro; IPR013839; DNAligase_adenylation.
DR   InterPro; IPR013840; DNAligase_N.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004150; NAD_DNA_ligase_OB.
DR   InterPro; IPR010994; RuvA_2-like.
DR   InterPro; IPR004149; Znf_DNAligase_C4.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF01653; DNA_ligase_aden; 1.
DR   Pfam; PF03120; DNA_ligase_OB; 1.
DR   Pfam; PF03119; DNA_ligase_ZBD; 1.
DR   PIRSF; PIRSF001604; LigA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00278; HhH1; 4.
DR   SMART; SM00532; LIGANc; 1.
DR   SUPFAM; SSF47781; SSF47781; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   TIGRFAMs; TIGR00575; dnlj; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR   PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA damage; DNA repair; DNA replication; Ligase;
KW   Magnesium; Manganese; Metal-binding; NAD; Zinc.
FT   NP_BIND      32     36       NAD (By similarity){EA4}.
FT   NP_BIND      81     82       NAD (By similarity){EA4}.
FT   ACT_SITE    115    115       N6-AMP-lysine intermediate (By
FT                                similarity){EA4}.
FT   METAL       408    408       Zinc (By similarity){EA4}.
FT   METAL       411    411       Zinc (By similarity){EA4}.
FT   METAL       426    426       Zinc (By similarity){EA4}.
FT   METAL       432    432       Zinc (By similarity){EA4}.
FT   BINDING     113    113       NAD (By similarity){EA4}.
FT   BINDING     136    136       NAD (By similarity){EA4}.
FT   BINDING     173    173       NAD (By similarity){EA4}.
FT   BINDING     290    290       NAD (By similarity){EA4}.
FT   BINDING     314    314       NAD (By similarity){EA4}.
SQ   SEQUENCE   671 AA;  73579 MW;  B9068F3AB6835693 CRC64;
     MESIEQQLTE LRTTLRHHEY LYHVMDAPEI PDAEYDRLMR ELRELETKHP ELITPDSPTQ
     RVGAAPLAAF SQIRHEVPML SLDNVFDEES FLAFNKRVQD RLKSNEKVTW CCELKLDGLA
     VSILYENGVL VSAATRGDGT TGEDITSNVR TIRAIPLKLH GENIPARLEV RGEVFLPQAG
     FEKINEDARR TGGKVFANPR NAAAGSLRQL DPRITAKRPL TFFCYGVGVL EGGELPDTHL
     GRLLQFKQWG LPVSDRVTLC ESAEEVLAFY HKVEEDRPTL GFDIDGVVIK VNSLAQQEQL
     GFVARAPRWA VAFKFPAQEQ MTFVRDVEFQ VGRTGAITPV ARLEPVHVAG VLVSNATLHN
     ADEIERLGLR IGDKVVIRRA GDVIPQVVNV VLSERPEDTR EVVFPTHCPV CGSDVERVEG
     EAVARCTGGL ICGAQRKESL KHFVSRRAMD VDGMGDKIID QLVEKEYVHT PADLFKLTAG
     KLTGLERMGP KSAQNVVNAL EKAKETTFAR FLYALGIREV GEATAAGLAA YFGTLEALEA
     ASIEELQKVP DVGIVVASHV HNFFAEESNR NVISELLAEG VHWPAPIVIN AEEIDSPFAG
     KTVVLTGSLS QMSRDDAKAR LVELGAKVAG SVSKKTDLVI AGEAAGSKLA KAQELGIEVI
     DEAEMLRLLG S
//
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