ID DNLJ_THEFI Reviewed; 670 AA. AC Q9ZHI0; Q9ZFY4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 24-JAN-2024, entry version 125. 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=Tfi DNA ligase; GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; OS Thermus filiformis. OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=276; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9749531; RA Kim H.K., Kwon S.-T.; RT "Cloning, nucleotide sequence, and expression of the DNA ligase-encoding RT gene from Thermus filiformis."; RL Mol. Cells 8:438-443(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-586. RC STRAIN=Tok6A1; RX PubMed=9889274; DOI=10.1093/nar/27.3.788; RA Tong J., Cao W., Barany F.; RT "Biochemical properties of a high fidelity DNA ligase from Thermus species RT AK16D."; RL Nucleic Acids Res. 27:788-794(1999). RN [3] RP FUNCTION, ACTIVE SITE, COFACTOR, INTERACTION WITH DNA, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15268945; DOI=10.1016/j.femsle.2004.06.018; RA Jeon H.J., Shin H.-J., Choi J.J., Hoe H.-S., Kim H.-K., Suh S.W., RA Kwon S.-T.; RT "Mutational analyses of the thermostable NAD+-dependent DNA ligase from RT Thermus filiformis."; RL FEMS Microbiol. Lett. 237:111-118(2004). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEXES WITH AMP AND ZINC IONS, RP AND ACTIVE SITE. RX PubMed=10698952; DOI=10.1093/emboj/19.5.1119; RA Lee J.Y., Chang C., Song H.K., Moon J., Yang J.K., Kim H.-K., Kwon S.-T., RA Suh S.W.; RT "Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and RT functional implications."; RL EMBO J. 19:1119-1129(2000). 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. {ECO:0000255|HAMAP-Rule:MF_01588, ECO:0000269|PubMed:15268945}. 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:0000269|PubMed:15268945}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. CC {ECO:0000269|PubMed:15268945}; CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF061572; AAC68862.1; -; Genomic_DNA. DR EMBL; AF092866; AAD13192.1; -; Genomic_DNA. DR PDB; 1DGS; X-ray; 2.90 A; A/B=1-670. DR PDB; 1V9P; X-ray; 2.90 A; A/B=1-584. DR PDBsum; 1DGS; -. DR PDBsum; 1V9P; -. DR AlphaFoldDB; Q9ZHI0; -. DR SMR; Q9ZHI0; -. DR STRING; 276.THFILI_03970; -. DR BRENDA; 6.5.1.2; 6336. DR EvolutionaryTrace; Q9ZHI0; -. 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; cd17748; BRCT_DNA_ligase_like; 1. DR CDD; cd00114; LIGANc; 1. DR Gene3D; 3.30.1490.70; -; 1. DR Gene3D; 6.20.10.30; -; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 1.10.287.610; Helix hairpin bin; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR001679; DNA_ligase. DR InterPro; IPR018239; DNA_ligase_AS. DR InterPro; IPR033136; DNA_ligase_CS. 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 NCBIfam; TIGR00575; dnlj; 1. DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1. DR PANTHER; PTHR23389:SF9; DNA LIGASE; 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 Pfam; PF12826; HHH_2; 1. DR Pfam; PF14520; HHH_5; 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 domain; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF47781; RuvA domain 2-like; 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 Metal-binding; NAD; Zinc. FT CHAIN 1..670 FT /note="DNA ligase" FT /id="PRO_0000161769" FT DOMAIN 586..670 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 ECO:0000269|PubMed:10698952, ECO:0000269|PubMed:15268945" 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..119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000305|PubMed:10698952" 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 226 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 291 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 315 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588, FT ECO:0000305|PubMed:10698952" FT BINDING 409 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588, FT ECO:0000269|PubMed:10698952" FT BINDING 412 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588, FT ECO:0000269|PubMed:10698952" FT BINDING 425 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588, FT ECO:0000269|PubMed:10698952" FT BINDING 430 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588, FT ECO:0000269|PubMed:10698952" FT CONFLICT 104..111 FT /note="ALGRKRPF -> LAEAPS (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="Missing (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 133..139 FT /note="LVFGATR -> WSTGS (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 232 FT /note="L -> LGL (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 257 FT /note="G -> C (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 274 FT /note="F -> G (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 290 FT /note="V -> L (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 296 FT /note="A -> T (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 299 FT /note="R -> G (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 399 FT /note="E -> K (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 408 FT /note="T -> A (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT CONFLICT 545 FT /note="L -> I (in Ref. 1; AAC68862)" FT /evidence="ECO:0000305" FT HELIX 3..25 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 34..37 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 38..47 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 52..54 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 60..63 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 91..100 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 132..137 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 141..147 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 167..176 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 179..192 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 200..208 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 213..218 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:1DGS" FT TURN 230..233 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 240..249 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 258..262 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 263..276 FT /evidence="ECO:0007829|PDB:1DGS" FT TURN 277..280 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 287..294 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 296..300 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 308..315 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 321..332 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 336..349 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 352..358 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 362..367 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 375..381 FT /evidence="ECO:0007829|PDB:1DGS" FT TURN 382..384 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 385..391 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 393..395 FT /evidence="ECO:0007829|PDB:1DGS" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 417..419 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 422..424 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 434..442 FT /evidence="ECO:0007829|PDB:1DGS" FT TURN 444..447 FT /evidence="ECO:0007829|PDB:1V9P" FT HELIX 454..462 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 469..475 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 478..481 FT /evidence="ECO:0007829|PDB:1DGS" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:1V9P" FT HELIX 491..500 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 501..503 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 506..512 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 520..528 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 533..536 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 541..545 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 552..563 FT /evidence="ECO:0007829|PDB:1DGS" FT HELIX 565..576 FT /evidence="ECO:0007829|PDB:1DGS" SQ SEQUENCE 670 AA; 76594 MW; 21F0FCAF9B9515FA CRC64; MTREEARRRI NELRDLIRYH NYRYYVLADP EISDAEYDRL LRELKELEER FPEFKSPDSP TEQVGARPLE PTFRPVRHPT RMYSLDNAFT YEEVLAFEER LERALGRKRP FLYTVEHKVD GLSVNLYYEE GVLVFGATRG DGEVGEEVTQ NLLTIPTIPR RLKGVPDRLE VRGEVYMPIE AFLRLNEELE ERGEKVFKNP RNAAAGSLRQ KDPRVTAKRG LRATFYALGL GLEESGLKSQ YELLLWLKEK GFPVEHGYEK ALGAEGVEEV YRRFLAQRHA LPFEADGVVV KLDDLALWRE LGYTARAPRF ALAYKFPAEE KETRLLDVVF QVGRTGRVTP VGVLEPVFIE GSEVSRVTLH NESYIEELDI RIGDWVLVHK AGGVIPEVLR VLKERRTGEE RPIRWPETCP ECGHRLVKEG KVHRCPNPLC PAKRFEAIRH YASRKAMDIE GLGEKLIERL LEKGLVRDVA DLYHLRKEDL LGLERMGEKS AQNLLRQIEE SKHRGLERLL YALGLPGVGE VLARNLARRF GTMDRLLEAS LEELLEVEEV GELTARAILE TLKDPAFRDL VRRLKEAGVS MESKEEVSDL LSGLTFVLTG ELSRPREEVK ALLQRLGAKV TDSVSRKTSY LVVGENPGSK LEKARALGVA VLTEEEFWRF LKEKGAPVPA //