ID   G7UW13_PSEUP            Unreviewed;       289 AA.
AC   G7UW13;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=DNA ligase {ECO:0000313|EMBL:AER57671.1};
GN   OrderedLocusNames=DSC_15135 {ECO:0000313|EMBL:AER57671.1};
OS   Pseudoxanthomonas spadix (strain BD-a59).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER57671.1, ECO:0000313|Proteomes:UP000005870};
RN   [1] {ECO:0000313|EMBL:AER57671.1, ECO:0000313|Proteomes:UP000005870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BD-a59 {ECO:0000313|EMBL:AER57671.1,
RC   ECO:0000313|Proteomes:UP000005870};
RX   PubMed=22207748; DOI=10.1128/JB.06436-11;
RA   Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT   "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT   spadix BD-a59.";
RL   J. Bacteriol. 194:544-544(2012).
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};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
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DR   EMBL; CP003093; AER57671.1; -; Genomic_DNA.
DR   RefSeq; WP_014161844.1; NC_016147.2.
DR   AlphaFoldDB; G7UW13; -.
DR   STRING; 1045855.DSC_15135; -.
DR   KEGG; psd:DSC_15135; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_021047_0_0_6; -.
DR   OrthoDB; 9782700at2; -.
DR   Proteomes; UP000005870; 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:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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 replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000313|EMBL:AER57671.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..289
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003504446"
FT   DOMAIN          116..200
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          215..279
FT                   /note="DNA ligase OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF14743"
SQ   SEQUENCE   289 AA;  31659 MW;  713C7CD6AA4657DA CRC64;
     MRVMLLSLLL SLLLNCLLLG VPAHAEPPRL MLATGYHGHL ALADYLVSEK LDGVRGRWDG
     QALWTRGGAR IDAPAWFTRG WPTQPLDGEL WLGRGRFDAA SALVRAGNAD DPAWHDLHFM
     LFDLPADAGP FEARVARMQA LVKASGNAQL RLVEQRRIDN VAALDAQFAR VVAAGGEGLM
     LHRRDAHYLV GRSDALLKYK PYDDAEARVV AHLGGKGKYA GLLGALLVQL PDGRSFRIGS
     GFTDAQRAAP PPLGAWVTYR YNGLTSKGLP RFARFLHVRD EPPPPDPQR
//