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Database: UniProt
Entry: A2BJX6
LinkDB: A2BJX6
Original site: A2BJX6 
ID   DNLI_HYPBU              Reviewed;         608 AA.
AC   A2BJX6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-OCT-2017, entry version 78.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000303|PubMed:23546841};
DE            EC=6.5.1.7 {ECO:0000269|PubMed:23546841};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP/ADP/GTP] {ECO:0000305};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=Hbut_0421;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Pyrodictiaceae; Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A.,
RA   Awayez M., She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=23546841; DOI=10.1007/s00792-013-0536-6;
RA   Kim J.H., Lee K.K., Sun Y., Seo G.J., Cho S.S., Kwon S.H., Kwon S.T.;
RT   "Broad nucleotide cofactor specificity of DNA ligase from the
RT   hyperthermophilic crenarchaeon Hyperthermus butylicus and its
RT   evolutionary significance.";
RL   Extremophiles 17:515-522(2013).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair. Can use
CC       ATP, ADP and GTP, but not CTP, TTP or NAD(+).
CC       {ECO:0000269|PubMed:23546841}.
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:23546841}.
CC   -!- CATALYTIC ACTIVITY: ADP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + phosphate. {ECO:0000269|PubMed:23546841}.
CC   -!- CATALYTIC ACTIVITY: GTP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       GMP + diphosphate. {ECO:0000269|PubMed:23546841}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:23546841};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:23546841};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:23546841};
CC       Temperature dependence:
CC         Optimum temperature is 75 degrees Celsius.
CC         {ECO:0000269|PubMed:23546841};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407, ECO:0000305}.
DR   EMBL; CP000493; ABM80287.1; -; Genomic_DNA.
DR   RefSeq; WP_011821605.1; NC_008818.1.
DR   ProteinModelPortal; A2BJX6; -.
DR   SMR; A2BJX6; -.
DR   STRING; 415426.Hbut_0421; -.
DR   EnsemblBacteria; ABM80287; ABM80287; Hbut_0421.
DR   GeneID; 4781994; -.
DR   KEGG; hbu:Hbut_0421; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; HBUT415426:GC56-421-MONOMER; -.
DR   Proteomes; UP000002593; 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:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; 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; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; GTP-binding; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN         1    608       DNA ligase.
FT                                /FTId=PRO_0000365248.
FT   ACT_SITE    268    268       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     266    266       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     273    273       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     288    288       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     318    318       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     358    358       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     435    435       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     441    441       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   608 AA;  68330 MW;  7D16CF4AEB60771E CRC64;
     MSMPFSVLAE TFEKLERVTA RTQMLLYLVE LFKKTPPEII DKVVYFIQGK LWPDWKGLPE
     LGIGEKMLIK AASIALHVSE KQIEQLVKKL GDTGKAIEMI KREKQQKQKA VGLLAFMQKP
     SGGESTLTVE KVYDTLARIA LVQGEGSRDI KLKLLAGLLA EASPREAKYI ARFVEGRLRL
     GVGDATIMEA LAVVYGGSAA MRSVVERAYN LRADLGMVAK ILATQGIDAL KNIKPEVGVP
     IRPMLAERLN DPVEIIKKLG GRALVEYKYD GERAQIHKKG DKIWIFSRRL ENITHMYPDV
     VEMAKKGIKA EEAIVEGEIV AIDPETGEFR PFQVLMHRRR KKDVHAVLSE IPVAVFLFDT
     LYVNGEDLTL KPLPARHEVL EKIIEQSDTW RIAEGIVTSD PQELESFFLK AIEDGAEGVM
     AKAIHDRSIY QAGARGWLWI KYKRDYKSEM SDTVDLVVIG AFYGKGRRGG KFGALLMAAY
     DPDTDTFKSV CKVGSGFTDE DLERLDDMLK PYISDKKPAR VDSQMKPDVW VEPTLVAEII
     GAELTLSPIH TCCYGWVKSG AGISIRFPRF IRWRPDKGPE DATTTKELYE MYKRQLRRIK
     EEEAPTGV
//
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