GenomeNet

Database: UniProt
Entry: Q12X08
LinkDB: Q12X08
Original site: Q12X08 
ID   DNLI_METBU              Reviewed;         567 AA.
AC   Q12X08;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 77.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=Mbur_1088;
OS   Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 /
OS   ACE-M).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanococcoides.
OX   NCBI_TaxID=259564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6242 / NBRC 107633 / OCM 468 / ACE-M;
RX   PubMed=19404327; DOI=10.1038/ismej.2009.45;
RA   Allen M.A., Lauro F.M., Williams T.J., Burg D., Siddiqui K.S.,
RA   De Francisci D., Chong K.W., Pilak O., Chew H.H., De Maere M.Z.,
RA   Ting L., Katrib M., Ng C., Sowers K.R., Galperin M.Y., Anderson I.J.,
RA   Ivanova N., Dalin E., Martinez M., Lapidus A., Hauser L., Land M.,
RA   Thomas T., Cavicchioli R.;
RT   "The genome sequence of the psychrophilic archaeon, Methanococcoides
RT   burtonii: the role of genome evolution in cold adaptation.";
RL   ISME J. 3:1012-1035(2009).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
DR   EMBL; CP000300; ABE52018.1; -; Genomic_DNA.
DR   RefSeq; WP_011499166.1; NC_007955.1.
DR   ProteinModelPortal; Q12X08; -.
DR   SMR; Q12X08; -.
DR   STRING; 259564.Mbur_1088; -.
DR   EnsemblBacteria; ABE52018; ABE52018; Mbur_1088.
DR   GeneID; 3998025; -.
DR   KEGG; mbu:Mbur_1088; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000001979; 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:UniProtKB-EC.
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; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    567       DNA ligase.
FT                                /FTId=PRO_1000049869.
FT   ACT_SITE    262    262       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     260    260       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     267    267       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     282    282       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     312    312       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     352    352       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     427    427       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     433    433       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   567 AA;  62743 MW;  3942FDE27D6C32F0 CRC64;
     MTDFKEFADV CKQIEHISSS LEMTDVVSDM LKSISTEELP VVTHFVMGDV FPAWSVEQLG
     VGTSLLYSAL SESSGLSLKE IEDLVRSTGD IGETAVAALG KKKKNKKKNQ ASLSFFSEDA
     ASVSISIMDV FERFLDISRY SGAGSQSSKM RNLQFLFNSS SSEEARYLAR LTIEDLRIGV
     GEGIVRDAIS KAFDVPAGDI ERGFMLTNDL GLVAVAAKEG GIEEISKLRM ELDRPIKMML
     AQVTPSIEAA IKDLGMLAVE WKFDGARVQI HKKGDSINIF SRRLENVTLS LPDIVEAVKL
     HVKADSAILE GEAVAVDENG APRAFQDILK RFRRKYDVET MVREIPLTLN LFDILYLNGD
     VLMDQSLLRR REQLVACVEN CDSIKVDEQV LTDDVNVVND IYAAALNGGH EGVMLKNPEA
     SYSPGKRGKN WLKKKPIMET LDLVVIAAEW GYGKRANLIG SYALACFDPE DGKFLPIGKV
     ATGFSDEQLA ELTEVFSELI IGESGREIEL KPDVVFEIAF EEIQKSTNYG SGYALRFPRL
     VNVREDKSPE EAETIDRIES IYLSQRG
//
DBGET integrated database retrieval system