ID   Q3JIW1_BURP1            Unreviewed;       980 AA.
AC   Q3JIW1;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 102.
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=BURPS1710b_A1335 {ECO:0000313|EMBL:ABA51818.1};
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA51818.1, ECO:0000313|Proteomes:UP000002700};
RN   [1] {ECO:0000313|EMBL:ABA51818.1, ECO:0000313|Proteomes:UP000002700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b {ECO:0000313|EMBL:ABA51818.1,
RC   ECO:0000313|Proteomes:UP000002700};
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) 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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000125; ABA51818.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3JIW1; -.
DR   EnsemblBacteria; ABA51818; ABA51818; BURPS1710b_A1335.
DR   KEGG; bpm:BURPS1710b_A1335; -.
DR   HOGENOM; CLU_008325_0_0_4; -.
DR   Proteomes; UP000002700; Chromosome II.
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; 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; 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; 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:ABA51818.1};
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          280..403
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          22..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..621
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..683
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  105516 MW;  0C63CB5DB13BC7A0 CRC64;
     MRGRGLRDSG GKHEQWLLIK ERDGDARDQA DYDVLRARPG SVLGGARSAR ARRGRAAEPT
     ERDAAAPKRA RASVPKGRAE AKTSGRAPRT VSNGTAGAGK GASKRASKRE GTNTGNGARS
     GKGSGKGAGE GVATSRRKRA AAPQSSDVDS ADTDSPAARG LALPAGLAAR FGLSGAKRAA
     LPRTLRPQLA TLVDTPTPGK DWLYEAKFDG YRVLIRIDRG AASRPIAVYT REGLDWSAKF
     AAQLDALARL PVDRGWLDGE AVVLDRAGVP DFQALQNALG AGRSNDVTLF LFDVPFLNGF
     DLRGVPLERR RALLAALVAA HASDVLRYSE SLAFEAADLL TGACDAGLEG LIGKRRDGRY
     VEGRSRSWIK LKCRRRQEFV IGGYTEPAGR RSGFGALLLG VYARAPGDEG ERRTRGAAET
     RDERRRASHA SRTSRTSRTS RTSRTSRAPD AGAARAPQAR PLALRYVGRV GTGFGERTLR
     ALARTLREHE TGRMPFADVP RERSGTPVHW VKPVLVAECE FAEWTGDGIV RQASFVGLRE
     DKPARTIVRE QPQSMETEAM NEHADEHTDE HTDARAERRT GGRTRRKARD DGARDAPALA
     RHPKRGDAGS SARKGARDGE AGKRAAAGSS PSSSPSSSTS TSPSISASGR TRGGGRSASR
     DRAGDADEGA NEDANDHAPR ERAGAPKVAG VRVSHPGRVI DPHTGTRKLD LVEYWEWIAP
     WLLPHLKGRP VSLVRAPADI GGELFFQKHA DKLEIPNVAL HPGLDPGHEA LITIDDVKGL
     VGAAQMGTIE LHTWNAHVSN IEKPDRAVFD LDPDPSLDWR AVIEAAQLTR ALLDELGLVS
     FCKTSGGKGL HVVVPLARHA GWDDVKAFAH AVARHMAATL PERFTATMGP RNRKGKIFVD
     YLRNNRGAST IAAYSVRARP GLGVSVPIAW DELPDTTGAA QWTLANLHER LDALKHDPWR
     AYAHVRQRVT AALRKRLSDG
//