DNLI_THEON
ID DNLI_THEON Reviewed; 562 AA.
AC B6YTR4; Q2Q452;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000303|PubMed:16614906};
DE EC=6.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000269|PubMed:16614906};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP/NAD(+)] {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305};
DE AltName: Full=TNA1_lig {ECO:0000303|PubMed:16614906};
GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
GN OrderedLocusNames=TON_1515 {ECO:0000312|EMBL:ACJ17005.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NA1;
RX PubMed=16614906; DOI=10.1007/s10529-005-6070-6;
RA Kim Y.J., Lee H.S., Bae S.S., Jeon J.H., Yang S.H., Lim J.K., Kang S.G.,
RA Kwon S.T., Lee J.H.;
RT "Cloning, expression, and characterization of a DNA ligase from a
RT hyperthermophilic archaeon Thermococcus sp.";
RL Biotechnol. Lett. 28:401-407(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. Can use both ATP and
CC NAD(+), but NAD(+) may be a preferred nucleotide cofactor.
CC {ECO:0000269|PubMed:16614906}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00407,
CC ECO:0000269|PubMed:16614906};
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=6.5.1.6; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00407, ECO:0000269|PubMed:16614906};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16614906};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16614906};
CC Note=Not stimulated by Ca(2+), Mn(2+) and Ni(2+).
CC {ECO:0000269|PubMed:16614906};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:16614906};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:16614906};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305}.
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; DQ223722; ABC11973.1; -; Genomic_DNA.
DR EMBL; CP000855; ACJ17005.1; -; Genomic_DNA.
DR AlphaFoldDB; B6YTR4; -.
DR SMR; B6YTR4; -.
DR STRING; 523850.TON_1515; -.
DR PRIDE; B6YTR4; -.
DR EnsemblBacteria; ACJ17005; ACJ17005; TON_1515.
DR KEGG; ton:TON_1515; -.
DR PATRIC; fig|523850.10.peg.1528; -.
DR eggNOG; arCOG01347; Archaea.
DR HOGENOM; CLU_005138_6_0_2; -.
DR OMA; WLFEESY; -.
DR BRENDA; 6.5.1.6; 9350.
DR Proteomes; UP000002727; 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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding; NAD;
KW Nucleotide-binding; Zinc.
FT CHAIN 1..562
FT /note="DNA ligase"
FT /id="PRO_0000431840"
FT ACT_SITE 252
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 272
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 342
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 562 AA; 63655 MW; A54BDEB51585437D CRC64;
MGDMKYTELS DLYRRLEKTT LKTLKTKFVA DFLKKTPDEL LEVVPYLILG KVFPDWDERE
LGVGEKLLIK AVSMATGVQE REIENSVKDT GDLGESVALA LKKKKQKSFF SQPLTIKRVY
QTFIKIAEAS GEGSQDRKLK YLANIFMDAQ PEEGKYIART VLGMMRTGVA EGILRDAIAE
AFKVKAELVE RAYMLTSDFG YVAKVAKLEG NDGLGKVHIQ IGKPIRPMLA QNAASVKEAL
LEMGAEAAFE IKYDGARVQV HKDGDRVVIY SRRLENVTRS IPEVVDAIKA SIKSEKAIVE
GELVAVGEGG RPRPFQYVLR RFRRKYNIEE MIEKIPLELN LFDVLYVDGE PLIDTPFRER
RAKLEEIVEE GEKLKLAQQL VTKKVEEAEE FYKKALELGH EGLMAKRLDS VYEPGNRGKK
WLKIKPTMED LDLVIIGAEW GEGRRAHLLG SFLVAAYDPH SGEFVPVGKV GSGFTDEDLV
EFTKMLKPLI IGGEGKFVEI EPKVVIQVTY QEIQKSPKYR SGFALRFPRY VALREDKSPE
EADTIERIAQ LYEFQERFKA KK
