ID A0A1I7GZH3_9BRAD Unreviewed; 889 AA.
AC A0A1I7GZH3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=SAMN05192541_102529 {ECO:0000313|EMBL:SFU53837.1};
OS Bradyrhizobium arachidis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=858423 {ECO:0000313|EMBL:SFU53837.1, ECO:0000313|Proteomes:UP000199591};
RN [1] {ECO:0000313|EMBL:SFU53837.1, ECO:0000313|Proteomes:UP000199591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26795 {ECO:0000313|EMBL:SFU53837.1,
RC ECO:0000313|Proteomes:UP000199591};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FPBQ01000002; SFU53837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7GZH3; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000199591; Unassembled WGS sequence.
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:SFU53837.1};
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 349..443
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 97806 MW; E798488B4CE41E2B CRC64;
MLQKLSTYRK KRDFGKTPEP SGKTAVTPSE QRRFVIQKHD ATRLHYDLRL EFDGVFKSWA
VTKGPSLDPH DKRLAVEVED HPLDYGDFEG TIPEGQYGGG TVMLWDRGTW ESDDPDAGFK
KGDLKFTLHG DKLHGSWVLV RMRNRGGEKR TNWLLIKHRD DYASESEDIL SEDKSVASGR
AMDQIADGKG RAPKPFMLAK GAKAKADAVW QSNRAEEAKG KTVKPAPRTA LKAGKTAKTA
KKKATTATNA KEVAEMPDFV APQLCTSVER PPAGDGWCHE IKFDGYRVQL RVEDGTATLK
TRKGLDWTDK FASIAKEAGA LPDAMIDGEI VALDHNGAPN FSSLQAALSD GKTEDLIFFA
FDLLFAEGLD YRRLPLGERK ARLKELLEAR KRKSTQIRYV EHFESGGDAV LQSACKLELE
GVVSKKLDAP YRSGRTESWT KAKCRAGHEV VIGGYKTTNG KFRSLMAGVH RGDHLVFVGM
VGTGFGADKV KRIMPSLKAM EAKESPFGGK NAPKKTRDVH WLKPELVAEI EFAGFTADGN
IRQAAFKGLR QDKPAEEVEA ETPVDTELAK PSTRKRAVPK TGKKDAGAAE VMGVVISKPD
KELWPDVGDG EGVTKLDLAR YLEAVGSWMI EHIKGRPCSI LRAPDGIGGE KFFQRHAMQG
TSNLLELAKV SGDRKPYLQI DRVEGLAAVA QIGGVELHPW NCAPDAYDTP GRLVFDLDPA
PDVEFADVVD AAKEMRQRLT DVGMESFCKT TGGKGLHVVV PLLHGARDKV SWKEAKAFAQ
GVCQWMADDD PERYLLNMSK KLRNGKIFLD YLRNDRLSTA VAPLSPRARD GATVSMPVTW
AQVKGDLDPK RYTVRTVPGL LARSKAWDGY DDAAASIKAA MKKLAGKVK
//
