ID   Q12AV7_POLSJ            Unreviewed;       306 AA.
AC   Q12AV7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   SubName: Full=ATP dependent DNA ligase {ECO:0000313|EMBL:ABE44335.1};
GN   OrderedLocusNames=Bpro_2416 {ECO:0000313|EMBL:ABE44335.1};
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE44335.1, ECO:0000313|Proteomes:UP000001983};
RN   [1] {ECO:0000313|Proteomes:UP000001983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX   PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE44335.1; -; Genomic_DNA.
DR   RefSeq; WP_011483333.1; NC_007948.1.
DR   AlphaFoldDB; Q12AV7; -.
DR   STRING; 296591.Bpro_2416; -.
DR   KEGG; pol:Bpro_2416; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_021047_0_0_4; -.
DR   OrthoDB; 9782700at2; -.
DR   Proteomes; UP000001983; 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:ABE44335.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001983}.
FT   DOMAIN          62..217
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|Pfam:PF01068"
FT   DOMAIN          231..301
FT                   /note="DNA ligase OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF14743"
SQ   SEQUENCE   306 AA;  33492 MW;  9B3FC4F38E913703 CRC64;
     MPAHTPSANT RLTIAPFRAQ TLALLLALAG LLTPALPLLA AETSPPLMLA KVYHVGVSLA
     DYWVSEKYDG VRGYWDGEKL LTRGGERIVA PAWFTADWPK VAMDGELWAG RGQFAKAVST
     VRQQTPDDAA WRAMRFMVFD LPAQGGPFTE RIPALNGVVS RIDQPWVQAV AQFKVANHRA
     LQNLLATTEK HAGEGLMLHR GASLYMGQRT DDLLKVKTHE DTEARVVAHI PGKGKYVGVL
     GALLVEMPGV DGKPGRRFKL GSGFNDEQRQ NPPVLGSTVT YRFRGLNGSG VPRFASFMRV
     REDQPV
//