ID   B1Z4V9_BURA4            Unreviewed;       949 AA.
AC   B1Z4V9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=BamMC406_6340 {ECO:0000313|EMBL:ACB68772.1};
OS   Burkholderia ambifaria (strain MC40-6).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=398577 {ECO:0000313|EMBL:ACB68772.1, ECO:0000313|Proteomes:UP000001680};
RN   [1] {ECO:0000313|Proteomes:UP000001680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC40-6 {ECO:0000313|Proteomes:UP000001680};
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA   Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia ambifaria MC40-6.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001027; ACB68772.1; -; Genomic_DNA.
DR   RefSeq; WP_012372656.1; NC_010557.1.
DR   AlphaFoldDB; B1Z4V9; -.
DR   KEGG; bac:BamMC406_6340; -.
DR   HOGENOM; CLU_008325_0_1_4; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000001680; Chromosome 3.
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   CDD; cd04862; PaeLigD_Pol_like; 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   InterPro; IPR033651; PaeLigD_Pol-like.
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:ACB68772.1};
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          363..449
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          578..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..665
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   949 AA;  104991 MW;  290C4B1A9B99DE95 CRC64;
     MAGKLDPYRR KRHFGATPEP EGAHGRRTQA AAKAAARTRA RGAHPLRFVI QEHHARRLHY
     DFRLELDGTL KSWAVPKGPS FDPSVKRLAV HVEDHPLEYA SFEGQIPEGH YGAGSVVVWD
     EGTWTPDGGL AQAREGYRAG KLTFRLDGEK LHGGWALVRS GRQQGRQEQW LLIKERDDDA
     RSMDEFDVVG ERPGSVHDGA ASARADAKNG SARARGSRQG RSEKPATRAA RHDDRAHDGH
     AGAPVDPSRI EGAVRAPLPE HVAPQLATLV DGPPTQGDWC YELKFDGYRI LARISGKGAR
     RHVKLMTREG RDWTAKLRAQ RDALAALDVD AAWLDGEAVV LGKNGLPDFQ ALQNAFGGGH
     SDEITLFVFD LPYLDGYDLR DAPLTARRAL LEPLLADSDP TRLRFSPDLG DDVASLIASA
     CDTGLEGLIG KRAESRYRAG RSPAWIKLKC RRRQEFVIGG YTEPSGSRHG FGALLLGVHE
     PAADGKRRRG PGPLRYVGRV GTGFDTRMLD RLTPILRKHE RDKMPFDPPP RERSRTPVHW
     IEPVLVAECE FAEWTGDGIV RQAAFIALRD DKPAARIVRE VPKHTETEVQ MDQRETAQHE
     RHKPGRTAHA GRDTGDTSDT SDTSDTSDTS DTSDGKHPAR SRGSRRAEAD DTGPDQLGRV
     RISHPERVID SHSGTRKIDL ARYWQWVAPW LLPDLKGRPV SLVRAPGDIS GELFFQKHAE
     RREIPFVTQH DGLDPGHGPL LSLDSVDALL GAAQMGTIEL HTWNAHASNI ERPDRIVFDL
     DPDPALPWSA MIDAAQLVRG LLDELGLISF CKTSGGKGLH VVVPITRHMG WDEVKDFSRA
     VAQHVAGALP DRFTATMGPK HRRGKIFIDY LRNGRGASTI AAYSVRARPG LGVSVPLRWD
     EVPDTTGGAQ WTIDTLHERL DRLKRDPWDG YDDTRQRITA QMRARLGTS
//