DNLJ_THET8
ID DNLJ_THET8 Reviewed; 676 AA.
AC P26996; Q5SJB7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
DE AltName: Full=Tth DNA ligase;
GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; Synonyms=lig, ligT;
GN OrderedLocusNames=TTHA1097;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1840584; DOI=10.1128/jb.173.16.5047-5053.1991;
RA Lauer G., Rudd E.A., McKay D.L., Ally A., Ally D., Backman K.C.;
RT "Cloning, nucleotide sequence, and engineered expression of Thermus
RT thermophilus DNA ligase, a homolog of Escherichia coli DNA ligase.";
RL J. Bacteriol. 173:5047-5053(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1756968; DOI=10.1016/0378-1119(91)90582-v;
RA Barany F., Gelfand D.H.;
RT "Cloning, overexpression and nucleotide sequence of a thermostable DNA
RT ligase-encoding gene.";
RL Gene 109:1-11(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP STRUCTURE BY NMR OF 588-676.
RG Northeast structural genomics consortium (NESG);
RT "Solution NMR structure of the BRCT domain from Thermus thermophilus DNA
RT ligase.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC stranded DNA using NAD as a coenzyme and as the energy source for the
CC reaction. It is essential for DNA replication and repair of damaged
CC DNA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01588};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermostable.;
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
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DR EMBL; M36417; AAA27487.1; -; Genomic_DNA.
DR EMBL; M74792; AAA27486.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70920.1; -; Genomic_DNA.
DR RefSeq; WP_011228436.1; NC_006461.1.
DR RefSeq; YP_144363.1; NC_006461.1.
DR PDB; 1L7B; NMR; -; A=588-676.
DR PDBsum; 1L7B; -.
DR AlphaFoldDB; P26996; -.
DR BMRB; P26996; -.
DR SMR; P26996; -.
DR STRING; 300852.55772479; -.
DR EnsemblBacteria; BAD70920; BAD70920; BAD70920.
DR GeneID; 3168641; -.
DR KEGG; ttj:TTHA1097; -.
DR PATRIC; fig|300852.9.peg.1077; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_007764_2_1_0; -.
DR OMA; HDVEHEI; -.
DR PhylomeDB; P26996; -.
DR EvolutionaryTrace; P26996; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
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 CDD; cd00114; LIGANc; 1.
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; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
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 Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF12826; HHH_2; 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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA replication; Ligase; Magnesium;
KW Manganese; Metal-binding; NAD; Reference proteome; Zinc.
FT CHAIN 1..676
FT /note="DNA ligase"
FT /id="PRO_0000161772"
FT DOMAIN 589..676
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT ACT_SITE 118
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 34..38
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 84..85
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 139
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 415
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:1L7B"
FT TURN 603..606
FT /evidence="ECO:0007829|PDB:1L7B"
FT HELIX 609..618
FT /evidence="ECO:0007829|PDB:1L7B"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:1L7B"
FT STRAND 628..630
FT /evidence="ECO:0007829|PDB:1L7B"
FT STRAND 634..636
FT /evidence="ECO:0007829|PDB:1L7B"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:1L7B"
FT HELIX 644..648
FT /evidence="ECO:0007829|PDB:1L7B"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:1L7B"
FT HELIX 657..668
FT /evidence="ECO:0007829|PDB:1L7B"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:1L7B"
SQ SEQUENCE 676 AA; 76905 MW; 60D23EF563851EE6 CRC64;
MTLEEARKRV NELRDLIRYH NYRYYVLADP EISDAEYDRL LRELKELEER FPELKSPDSP
TLQVGARPLE ATFRPVRHPT RMYSLDNAFN LDELKAFEER IERALGRKGP FAYTVEHKVD
GLSVNLYYEE GVLVYGATRG DGEVGEEVTQ NLLTIPTIPR RLKGVPERLE VRGEVYMPIE
AFLRLNEELE ERGERIFKNP RNAAAGSLRQ KDPRITAKRG LRATFYALGL GLEEVEREGV
ATQFALLHWL KEKGFPVEHG YARAVGAEGV EAVYQDWLKK RRALPFEADG VVVKLDELAL
WRELGYTARA PRFAIAYKFP AEEKETRLLD VVFQVGRTGR VTPVGILEPV FLEGSEVSRV
TLHNESYIEE LDIRIGDWVL VHKAGGVIPE VLRVLKERRT GEERPIRWPE TCPECGHRLL
KEGKVHRCPN PLCPAKRFEA IRHFASRKAM DIQGLGEKLI ERLLEKGLVK DVADLYRLRK
EDLVGLERMG EKSAQNLLRQ IEESKKRGLE RLLYALGLPG VGEVLARNLA ARFGNMDRLL
EASLEELLEV EEVGELTARA ILETLKDPAF RDLVRRLKEA GVEMEAKEKG GEALKGLTFV
ITGELSRPRE EVKALLRRLG AKVTDSVSRK TSYLVVGENP GSKLEKARAL GVPTLTEEEL
YRLLEARTGK KAEELV
