DNLI_THEFM
ID DNLI_THEFM Reviewed; 559 AA.
AC Q9HH07;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000303|PubMed:15251207};
DE EC=6.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000269|PubMed:15251207};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP/NAD(+)] {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305};
GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
OS Thermococcus fumicolans.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=46540;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15251207; DOI=10.1016/j.femsle.2004.05.045;
RA Rolland J.-L., Gueguen Y., Persillon C., Masson J.-M., Dietrich J.;
RT "Characterization of a thermophilic DNA ligase from the archaeon
RT Thermococcus fumicolans.";
RL FEMS Microbiol. Lett. 236:267-273(2004).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. Shows high activity with
CC either ATP or NAD(+). {ECO:0000269|PubMed:15251207}.
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:15251207};
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:15251207};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00407,
CC ECO:0000269|PubMed:15251207};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1160 uM for ATP {ECO:0000269|PubMed:15251207};
CC KM=690 uM for NAD(+) {ECO:0000269|PubMed:15251207};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:15251207};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius. Loses half of its activity
CC in 15 min at 90 degrees Celsius. {ECO:0000269|PubMed:15251207};
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305}.
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DR EMBL; AJ133713; CAC21199.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9HH07; -.
DR SMR; Q9HH07; -.
DR PRIDE; Q9HH07; -.
DR KEGG; ag:CAC21199; -.
DR BRENDA; 6.5.1.6; 6299.
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.
FT CHAIN 1..559
FT /note="DNA ligase"
FT /id="PRO_0000059621"
FT ACT_SITE 249
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 339
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"
FT BINDING 420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
SQ SEQUENCE 559 AA; 63598 MW; 173DCFF6FC0110BB CRC64;
MKYSELAGLY RRLEKTTLKT LKTRFVADFL KNVPDELLEI VPYLILGKVF PDWDERELGV
GEKLLIKAVS IATGVPEGEI ENSIKDTGDL GESIALAVKK KKQKSFFSQP LTIKRVYDTF
VKVAESQGEG SQDRKMKYLA NLFMDAQPEE AKYIARTVLG TMRTGVAEGI LRDAIAEAFK
VKAELVERAY MLTSDFGYVT KVAKLEGNEG LSKVRIQVGK PVRPMLAQNA ASVKDALLEM
GGEAAFEIKY DGARVQVHKD GDRVVIYSRR LENVTRSIPE IVEAVRSQLR PEKAIVEGEL
VAVGDGGKPR PFQYVLRRFR RKYNIEEMIE RIPLELNLFD VLYVDGESLV DTPFMERRKR
LEEAVEESER IKLAQQLVTK KAEEAEEFYR RALELGHEGL MAKRLDSVYE PGNRGKKWLK
IKPTMEDLDL VIIGAEWGEG RRAHLLGSFL VAAYDQHRGE FVPVGKVGSG FTDEDLAEFT
KMLKPLIVRE EGKYVEIEPR VVIQVTYQEI QKSPKYESGF ALRFPRYVAL REDKSPEEAD
TIERISELYG LQERFKAKR
