DNLI_METTP
ID DNLI_METTP Reviewed; 552 AA.
AC A0B7F9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Mthe_0844;
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00407}.
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DR EMBL; CP000477; ABK14633.1; -; Genomic_DNA.
DR AlphaFoldDB; A0B7F9; -.
DR SMR; A0B7F9; -.
DR STRING; 349307.Mthe_0844; -.
DR EnsemblBacteria; ABK14633; ABK14633; Mthe_0844.
DR KEGG; mtp:Mthe_0844; -.
DR HOGENOM; CLU_005138_6_0_2; -.
DR OMA; WLFEESY; -.
DR Proteomes; UP000000674; 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 Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 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 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; SSF117018; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00574; dnl1; 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..552
FT /note="DNA ligase"
FT /id="PRO_1000049873"
FT ACT_SITE 246
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 296
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
SQ SEQUENCE 552 AA; 61188 MW; 4A0865A5F8711501 CRC64;
MTGFARFAEL CERISQTSGS LEKTDILASF LSDLESDDLR IVAGFVMGVV IPGTELGVGP
SLLYESISRA TGLSSDAVNE LLRATGDPGL VAYRAVERRK PLTLAAFSGS EGLEVQDVYQ
RFLSIAKASG RGSQEIRVKN LQYMFSEASP LEAKYIARLA MEDMRIGVGE GLVRDAIAKA
FGVSKEDVER AYNLTNDLGL VAEYAKLGRL NELGISINRP IKMMLAQIGE SIEASLAEGA
TAVEWKFDGA RVQIHKDKGN VRIFSRRLED VTSSLPEIRE IVRGHVRART AILDGEAVAT
GEDGRPLPFQ EILRRFRRKY GVARTAKTIP LKLHLFDIIY MDGASLLDEP LEERRRVLVS
VADPEIIAEQ VVTSDVHRVE EIYREALAAG HEGVMLKNPS STYTPGKRGK NWLKIKPLLE
SLDLVVIGAR WGEGKRANLL GSYRLACIDT DTGELKDVGW VATGITDEML AELTELFREL
IVKENGMEVE VHPEIVFEVG YEEIQRSPNY SSGYALRFPR LIAVRDDKSP SEADTLERIG
EIYRLQRGRS KK
