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Database: UniProt
Entry: B6YTR4
LinkDB: B6YTR4
Original site: B6YTR4 
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   07-JUN-2017, entry version 60.
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,
RP   COFACTOR, 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.,
RA   Kang S.G., 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.,
RA   Chun J., 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
CC       during DNA replication, DNA recombination and DNA repair. Can use
CC       both ATP and NAD(+), but NAD(+) may be a preferred nucleotide
CC       cofactor. {ECO:0000269|PubMed:16614906}.
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:16614906}.
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: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}.
DR   EMBL; DQ223722; ABC11973.1; -; Genomic_DNA.
DR   EMBL; CP000855; ACJ17005.1; -; Genomic_DNA.
DR   ProteinModelPortal; B6YTR4; -.
DR   SMR; B6YTR4; -.
DR   STRING; 523850.TON_1515; -.
DR   EnsemblBacteria; ACJ17005; ACJ17005; TON_1515.
DR   KEGG; ton:TON_1515; -.
DR   PATRIC; fig|523850.10.peg.1528; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BRENDA; 6.5.1.6; 9350.
DR   Proteomes; UP000002727; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro.
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-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; 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; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; NAD; Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN         1    562       DNA ligase.
FT                                /FTId=PRO_0000431840.
FT   ACT_SITE    252    252       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     250    250       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     257    257       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     272    272       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     302    302       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     342    342       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     417    417       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     423    423       ATP. {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
//
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