ID A0A5B9DS59_9HYPH Unreviewed; 815 AA.
AC A0A5B9DS59;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
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 Name=ligD {ECO:0000313|EMBL:QEE22037.1};
GN ORFNames=FNA67_18475 {ECO:0000313|EMBL:QEE22037.1};
OS Paradevosia tibetensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Devosiaceae; Paradevosia.
OX NCBI_TaxID=1447062 {ECO:0000313|EMBL:QEE22037.1, ECO:0000313|Proteomes:UP000321062};
RN [1] {ECO:0000313|EMBL:QEE22037.1, ECO:0000313|Proteomes:UP000321062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=fig4 {ECO:0000313|Proteomes:UP000321062};
RX PubMed=25829329; DOI=10.1099/ijs.0.000219;
RA Wang Y.X., Huang F.Q., Nogi Y., Pang S.J., Wang P.K., Lv J.;
RT "Youhaiella tibetensis gen. nov., sp. nov., isolated from subsurface
RT sediment.";
RL Int. J. Syst. Evol. Microbiol. 65:2048-2055(2015).
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; CP041690; QEE22037.1; -; Genomic_DNA.
DR RefSeq; WP_147657491.1; NZ_BMFM01000002.1.
DR AlphaFoldDB; A0A5B9DS59; -.
DR KEGG; yti:FNA67_18475; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000321062; 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 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; IPR052171; NHEJ_LigD.
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; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING 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:QEE22037.1};
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 REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..815
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 815 AA; 89778 MW; D71DE10F50A972B6 CRC64;
MAQLNTYRGK RDFSKTPEPS GRAAQPGGNR YVIHEHGATS HHYDLRLELD GVLKSWAVPK
GPSLNPDDKR LAVETEDHPV EYLDFEGVIP EGEYGGGPMI VWDRGVWAPM GDIEEAFRTG
DFKFRLAGEK LSGGWMLKRL KPKPGEDPDK VNWLFFKEHD PAASTSENIL ETRPQSVKSG
LTIDEVRPAP PRPKRPVKLE PGKLKGAVAA PMPTKIQPQL ATAIADPPPG PGEKTRWLHE
IKFDGYRTIA FLEDREARLI TRAGLDWTNR YRRLANTFAQ IPCRQAVIDG EVVVVGSDGV
TTFAALQEAL AENRSHDLTF FAFDLLYLDG YDLRNVALIE RKQLLADLLG PIISGKSAIQ
YSDHFEGEGA GLLALATEKG LEGIVSKRAD ARYEEARTAT WVKTKARKVG DFLIVGFTRS
EAAGGLGALG LGEMVDGKLE YRGKVGTGFD AHMLGELLEK LEPLVAAGAP LARAPKDLVR
VEPVYSAHVH FANRTNDGSL RHAVFMGLIE PELETNRPER KRLISDADLA SVSITNPTRR
LFGDDGPTKL DLAVYYGLVG DFMLPHIMGR PVTLVRSPSG KADDIFYQRH PFSGMPKSVG
AFDAINSDGE ARQYLSVEDP KGYLALAQFG VIEFHTWGCH HALLEKPDRI VFDLDPGEGI
TWRNIVDASR RVRAALESVR LNAFVKTSGG KGLHVVVPIR PRLDWKAVHK ATGAMAQAIA
AGDRDTFVAN MAKDKRKNRI FIDFHRNARG ATAAAPYSLR ARPGLPASTP LNWNQLESID
APEELNYSSL PQILNSSGDP WADIDEYASD LEPDR
//
