ID   D9QKL0_BRESC            Unreviewed;       859 AA.
AC   D9QKL0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE   AltName: Full=NHEJ DNA polymerase {ECO:0000256|ARBA:ARBA00029943};
GN   OrderedLocusNames=Bresu_0521 {ECO:0000313|EMBL:ADK99835.1};
OS   Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS   NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=633149 {ECO:0000313|EMBL:ADK99835.1, ECO:0000313|Proteomes:UP000002696};
RN   [1] {ECO:0000313|Proteomes:UP000002696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC   {ECO:0000313|Proteomes:UP000002696};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; CP002102; ADK99835.1; -; Genomic_DNA.
DR   RefSeq; WP_013267939.1; NC_014375.1.
DR   AlphaFoldDB; D9QKL0; -.
DR   STRING; 633149.Bresu_0521; -.
DR   KEGG; bsb:Bresu_0521; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_1_5; -.
DR   InParanoid; D9QKL0; -.
DR   OrthoDB; 9802472at2; -.
DR   BioCyc; BSUB633149:G1GM8-519-MONOMER; -.
DR   Proteomes; UP000002696; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014143; NHEJ_ligase_prk.
DR   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   NCBIfam; TIGR02776; NHEJ_ligase_prk; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF13298; LigD_N; 1.
DR   Pfam; PF21686; LigD_Prim-Pol; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADK99835.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002696};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          319..414
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          525..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  92688 MW;  730D210221BE2DEB CRC64;
     MKGELKTYQA KRRFAETPEP KGTKATRKGA APLRYLIQRH AATRLHYDFR IEFDGVLKSW
     AVTKAPSRDT TVKRLAVEVE DHPLDYGSFE GTIPDGNYGA GTVQLWDTGT WSPRHPETLE
     ADWAKGSIKM DLDGERLKGG WALVRLKSDR GKPSKWANWL LLKEKDAHAV PGEGDALAEI
     DASITTGRSL AEIAAGKTPG TPTRPTGRKA AARPKAAPSG ATLSKPPAFT PIQLCKVADH
     PPSGAGWAHE IKFDGYRVQI ATGGGKARLY TRSGLDWSQK FPEVVADAAR WPDGVIDGEL
     CALDPDHMPD FPALQAAISA GRTADLVFFA FDLLSEGTED LREKPLSHRK ARLSGHIDRM
     SRAARDRIRY VDHFASTGQA VLESACRMDL EGVISKKLDA PYTAGRSSTW LKSKCRGGDE
     VVIGGWSSEN GTRFRSLLVG VREGEGLRYL GRVGTGYSQA VMKTLLPALK AAASDASPFA
     GKGAPRGGRD IHWLKPVLVA EVTHGGYTES GSLRQAAFKG LRADKPAAEV TERPQTPTPT
     GKAAPATDLH VPGEPAPLAS ARGKVVVAGV TISNPDKILW PARDGHPAIT KAELARYYEA
     AADRILPHVA DRPTSIIRAP EGVGGETFFQ RHAMPGSNPR LKLIDVHERK PYVAVVDVGG
     LVAIGQSGGL ELHPWGCAPG EPEIPDQVTF DLDPDEGLDF EDVISAARVV RKKLEALGLH
     PFVKTTGGKG LHVVVPIKTD ARSRVTWDQN KAFAKGVSEA IRAEAPDRFT TTLAKKARGG
     KIFLDYLRNG RMATAVAPWS PRARPGAGIA FPLAWTQVKA GLDPTAFSLR TYPALLKKPD
     PWKDFRVSAV SLKGALKKL
//