ID E1T7A9_BURSG Unreviewed; 974 AA.
AC E1T7A9;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=BC1003_1569 {ECO:0000313|EMBL:ADN57539.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN57539.1};
RN [1] {ECO:0000313|EMBL:ADN57539.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN57539.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome1 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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; CP002217; ADN57539.1; -; Genomic_DNA.
DR AlphaFoldDB; E1T7A9; -.
DR STRING; 640512.BC1003_1569; -.
DR KEGG; bgf:BC1003_1569; -.
DR eggNOG; COG1793; Bacteria.
DR eggNOG; COG3285; Bacteria.
DR HOGENOM; CLU_008325_0_0_4; -.
DR OrthoDB; 9802472at2; -.
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:ADN57539.1};
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 358..485
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 106386 MW; 93EF22410554A6FC CRC64;
MNDRLDLYNR KRRFDETPEP AGTRPAKKRG GRGAAHPEAA EGLSYVIQEH HARRLHYDFR
LELNGALLSW AVPKGPCLDP SVKRLAVHVE DHPVEYGSFE GEIPPGNYGA GTVIVWDRGT
WEPLGGPAEA ARAYRAGKLK FHLHGEKLHG GWTLVRSHMR GNADKEQWLL IKEPDDEARD
ESEYDILAER PGSVLGGESA PAKAKGKAKG GSRAATGKSQ MASVRGDPKR PDIVATRSNE
SLRELAASPA IEGAVKARLP AALKPQLATL VDATPPGDDW AYEIKFDGYR VLARIDASAK
GHGVQVFTRA GNDWTARFSR QVKAFGQLGL ESAWLDGEAV VLDENGVPSF QALQNAFDSN
RPQDIVVYLF DVPFLNGYDL RGVPLQQRRA ILRALLEPVD DSVLRFSNDF EFSADDLLKS
ACDMALEGII GKRRDSGYVS GRSATWIKLK CRRRQEFVIG GYSEPSGSRA AFGALLLGVH
DSKGKLQYAG RVGTGFDAAL LRSVKKELDA HETKRMPFAS PPRERSRTPV HWVEPVLVAE
CNFAEWTSDG IVRQASFVSL RKDKPARQIV KEAPRKGDDV QQQTDIEADT APKKRAARSK
GTGKTAAATA DELAEGTAEK NARKPVEPAA KSAAKPAAKA AAKSGASAKR TATSDTDNDT
ENDTHAQSPA SRSRKSASPA EVAGVRISHP DRVIDKSTGA RKIDLVQYYE SVARWMLPHL
ADRPVSLVRA PEDIGGELFF QKHTQKLSIP NITQHPGLDP GHPPLITVDS VKALVGAAQM
GTIEFHTWNG VASNIEKPDR VVFDLDPDPS LGWERMIEAA LLTRTLLEEL GLTSFCKTSG
GKGLHVVVPL AKHAGWDEVK GFSQAVAQHM ASTLPKYFSA KMGAQNRKQK IFVDYLRNNR
GSSTVAAFSV RARPGLGVSV PLAWDEVAQT TGGDQWNIRN LHERLAQLKS DPWAEYPKTR
QRITAAMRKR LSGA
//
