ID D6CV64_THIA3 Unreviewed; 296 AA.
AC D6CV64;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=ATP-dependent DNA ligase {ECO:0000313|EMBL:CAZ89183.1};
DE EC=6.5.1.1 {ECO:0000313|EMBL:CAZ89183.1};
GN OrderedLocusNames=THI_2564 {ECO:0000313|EMBL:CAZ89183.1};
OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ89183.1, ECO:0000313|Proteomes:UP000002372};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3As;
RA Genoscope - CEA;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22701 / CIP 110005 / 3As
RC {ECO:0000313|Proteomes:UP000002372};
RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT "Structure, function, and evolution of the Thiomonas spp. genome.";
RL PLoS Genet. 6:E1000859-E1000859(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
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DR EMBL; FP475956; CAZ89183.1; -; Genomic_DNA.
DR RefSeq; WP_013106468.1; NZ_CTRL01000047.1.
DR AlphaFoldDB; D6CV64; -.
DR KEGG; thi:THI_2564; -.
DR eggNOG; COG1793; Bacteria.
DR HOGENOM; CLU_021047_0_0_4; -.
DR OrthoDB; 9782700at2; -.
DR Proteomes; UP000002372; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR CDD; cd08041; OBF_kDNA_ligase_like; 1.
DR Gene3D; 3.30.1490.70; -; 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 InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR029319; DNA_ligase_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF14743; DNA_ligase_OB_2; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAZ89183.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002372}.
FT DOMAIN 99..214
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|Pfam:PF01068"
FT DOMAIN 228..293
FT /note="DNA ligase OB-like"
FT /evidence="ECO:0000259|Pfam:PF14743"
SQ SEQUENCE 296 AA; 32898 MW; 135D514C47E933AD CRC64;
MRPSPRRFPA PTLAGLRPLL LCGVLLTNLP WAQAEAPSPP PPALLLAETA SSQLDPAPYW
VSEKLDGVRA FWDGRVLRFR SGNPVPAPAW FTAALPSQPL DGELWIARES FDQVSGIVRS
NPPNDRDWKQ VRYMVFELPN APGSFTERIA RMRTLVERAQ APWLQMVPQF RVPNSAALKQ
QLDKIVKAGG EGLMLHRADA PYQTGRQDVL LKLKPWQDAE ATVIGYTPGK GKYAGLTGAL
NMQMPDGKIF RIGSGLSDAL RRNPPPIGAQ ITYRYQSLTP SGLPRFARYL RVREKE
//