ID C6UMR0_ECOBR Unreviewed; 671 AA.
AC C6UMR0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 33.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; ENVRTIR; -.
DR ProtClustDB; PRK07956; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA: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 HAMAP; MF_01588; DNA_ligase_A; 1; -.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR018239; DNA_ligase_AS.
DR InterPro; IPR004150; DNA_ligase_OB.
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; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR PANTHER; PTHR11107:SF5; PTHR11107:SF5; 1.
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; SSF52113; BRCT; 1.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF47781; RuvA_2_like; 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 DOMAIN 593 671 BRCT (By similarity).
FT NP_BIND 32 36 NAD (By similarity).
FT NP_BIND 81 82 NAD (By similarity).
FT ACT_SITE 115 115 N6-AMP-lysine intermediate (By
FT similarity).
FT METAL 408 408 Zinc (By similarity).
FT METAL 411 411 Zinc (By similarity).
FT METAL 426 426 Zinc (By similarity).
FT METAL 432 432 Zinc (By similarity).
FT BINDING 113 113 NAD (By similarity).
FT BINDING 136 136 NAD (By similarity).
FT BINDING 173 173 NAD (By similarity).
FT BINDING 290 290 NAD (By similarity).
FT BINDING 314 314 NAD (By similarity).
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
//
