ID DNLI_METKA Reviewed; 559 AA. AC Q8TWN3; DT 13-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407}; DE EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407}; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407}; GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407}; OrderedLocusNames=MK0999; OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938). OC Archaea; Euryarchaeota; Methanomada group; Methanopyri; Methanopyrales; OC Methanopyraceae; Methanopyrus. OX NCBI_TaxID=190192; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938; RX PubMed=11930014; DOI=10.1073/pnas.032671499; RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., RA Koonin E.V., Kozyavkin S.A.; RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and RT monophyly of archaeal methanogens."; RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002). CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA CC replication, DNA recombination and DNA repair. {ECO:0000255|HAMAP- CC Rule:MF_00407}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho- CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00407}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00407}; CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000255|HAMAP-Rule:MF_00407}. 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; AE009439; AAM02212.1; -; Genomic_DNA. DR AlphaFoldDB; Q8TWN3; -. DR SMR; Q8TWN3; -. DR STRING; 190192.MK0999; -. DR PaxDb; 190192-MK0999; -. DR EnsemblBacteria; AAM02212; AAM02212; MK0999. DR KEGG; mka:MK0999; -. DR PATRIC; fig|190192.8.peg.1047; -. DR HOGENOM; CLU_005138_6_0_2; -. DR InParanoid; Q8TWN3; -. DR OrthoDB; 31274at2157; -. DR Proteomes; UP000001826; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1. DR CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1. DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00407; DNA_ligase; 1. DR InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc. DR InterPro; IPR000977; DNA_ligase_ATP-dep. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR012308; DNA_ligase_ATP-dep_N. DR InterPro; IPR036599; DNA_ligase_N_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR NCBIfam; TIGR00574; dnl1; 1. DR PANTHER; PTHR45674:SF7; DNA LIGASE; 1. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS00697; DNA_LIGASE_A1; 1. DR PROSITE; PS00333; DNA_LIGASE_A2; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination; KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..559 FT /note="DNA ligase" FT /id="PRO_0000059605" FT ACT_SITE 250 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 248 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 255 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 270 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 300 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 341 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 417 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 423 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 559 AA; 63337 MW; 8C810526CC76402A CRC64; MYYSSLAEAF ERLERISSRK AKISLIAQFL RQCPEDVVDT VALFLANQVF PGWDPRDLGI GSKLMRKVIA TATGSTDSEV TELFKRLGDL GLTAEELLKR RKTSTLLDSR PLMVGEVRET FEKIAEVEGE GAVKRKMRLM MGLLARAKPK EARYLVRQAL SELRTGVRES TVEEAIAQAF GVSRKLVERA HMLSNDLGLV AKVAMTKGEE GLREIDLRPM RPIKPMLAQA ARNVKEALAE VGGKGAVEIK LDGARVQVHS DGEEVRVYTR RIEDVTHALP DIVEAVKDCV DADEFILEGE AVAINPETGK PRPFQELLHR IKRKYDIEEV RKEIPVELHL FDCLYVDGES LVDTPFRERR RRLEEIVRER EGEVMLVEQV ITDDPKEAAE MFHRALEMGH EGVMVKDLDA NYTPGVRGKK MLKVKPVLET LDCVVIGGIW GKGKRKGLIG SYLLAVWDEN KENLLEVGKV GTGMDDETLE RLTKMFEDLI VEESGREVRF KPEVVFEVEF EDIQKSPKYS SGFALRFPRL VRVRDDLGPE DADTIEKVRR IYEEVLQKH //