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Database: UniProt
Entry: Q9HH07
LinkDB: Q9HH07
Original site: Q9HH07 
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   13-SEP-2023, entry version 93.
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   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   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   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
//
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