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Database: UniProt/SWISS-PROT
Entry: DNLI_THEKO
LinkDB: DNLI_THEKO
Original site: DNLI_THEKO 
ID   DNLI_THEKO              Reviewed;         559 AA.
AC   Q9HHC4; Q5JHF2;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   07-NOV-2018, entry version 115.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000303|PubMed:11053387};
DE            EC=6.5.1.6 {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000269|PubMed:11053387};
DE   AltName: Full=Lig(Tk) {ECO:0000303|PubMed:11053387};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP/NAD(+)] {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407}; OrderedLocusNames=TK2140;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=11053387; DOI=10.1128/JB.182.22.6424-6433.2000;
RA   Nakatani M., Ezaki S., Atomi H., Imanaka T.;
RT   "A DNA ligase from a hyperthermophilic archaeon with unique cofactor
RT   specificity.";
RL   J. Bacteriol. 182:6424-6433(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon
RT   Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus
RT   genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair. Can also
CC       use NAD, but less efficiently than ATP.
CC       {ECO:0000269|PubMed:11053387}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000255|HAMAP-Rule:MF_00407,
CC       ECO:0000269|PubMed:11053387}.
CC   -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl
CC       + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m)
CC       + AMP + beta-nicotinamide D-nucleotide. {ECO:0000255|HAMAP-
CC       Rule:MF_00407, ECO:0000269|PubMed:11053387}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00407,
CC         ECO:0000269|PubMed:11053387};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:11053387};
CC       Temperature dependence:
CC         Still active at 100 degrees Celsius. Thermostable.
CC         {ECO:0000269|PubMed:11053387};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11053387}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD86329.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AB042527; BAB15949.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP006878; BAD86329.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_048053886.1; NC_006624.1.
DR   ProteinModelPortal; Q9HHC4; -.
DR   SMR; Q9HHC4; -.
DR   STRING; 69014.TK2140; -.
DR   EnsemblBacteria; BAD86329; BAD86329; TK2140.
DR   GeneID; 3235455; -.
DR   KEGG; tko:TK2140; -.
DR   PATRIC; fig|69014.16.peg.2096; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   InParanoid; Q9HHC4; -.
DR   KO; K10747; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; TKOD69014:G1G2A-2158-MONOMER; -.
DR   BRENDA; 6.5.1.1; 5246.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   Gene3D; 1.10.3260.10; -; 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; Complete proteome;
KW   Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW   DNA replication; Ligase; Magnesium; Metal-binding; NAD;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    559       DNA ligase.
FT                                /FTId=PRO_0000059615.
FT   ACT_SITE    249    249       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     247    247       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     254    254       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     269    269       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     299    299       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     339    339       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     414    414       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     420    420       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   559 AA;  63749 MW;  91AB32542E03D20D CRC64;
     MRYSELADLY RRLEKTTLKT LKTKFVADFL KKTPDELLEI VPYLILGKVF PDWDERELGV
     GEKLLIKAVS MATGVPEKEI EDSVRDTGDL GESVALAIKK KKQKSFFSQP LTIKRVYDTF
     VKIAEAQGEG SQDRKMKYLA NLFMDAEPEE GKYLARTVLG TMRTGVAEGI LRDAIAEAFR
     VKPELVERAY MLTSDFGYVA KIAKLEGNEG LSKVRIQIGK PIRPMLAQNA ASVKDALIEM
     GGEAAFEIKY DGARVQVHKD GDKVIVYSRR LENVTRSIPE VIEAIKAALK PEKAIVEGEL
     VAVGENGRPR PFQYVLRRFR RKYNIDEMIE KIPLELNLFD VMFVDGESLI ETKFIDRRNK
     LEEIVKESEK IKLAEQLITK KVEEAEAFYR RALELGHEGL MAKRLDSIYE PGNRGKKWLK
     IKPTMENLDL VIIGAEWGEG RRAHLLGSFL VAAYDPHSGE FLPVGKVGSG FTDEDLVEFT
     KMLKPYIVRQ EGKFVEIEPK FVIEVTYQEI QKSPKYKSGF ALRFPRYVAL REDKSPEEAD
     TIERVAELYE LQERFKAKK
//
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