ID A0A411X7R2_9BURK Unreviewed; 900 AA.
AC A0A411X7R2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:QBI05071.1};
GN ORFNames=EYF70_15740 {ECO:0000313|EMBL:QBI05071.1};
OS Pseudoduganella albidiflava.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=321983 {ECO:0000313|EMBL:QBI05071.1, ECO:0000313|Proteomes:UP000292307};
RN [1] {ECO:0000313|EMBL:QBI05071.1, ECO:0000313|Proteomes:UP000292307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17472 {ECO:0000313|EMBL:QBI05071.1,
RC ECO:0000313|Proteomes:UP000292307};
RA Miess H., Frediansyhah A., Gross H.;
RT "Draft Genome Sequences of Six Type Strains of the Genus Massilia.";
RL Submitted (FEB-2019) 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; CP036401; QBI05071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411X7R2; -.
DR KEGG; mali:EYF70_15740; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000292307; 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; 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:QBI05071.1};
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 351..442
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 189..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 99566 MW; 3EBE19D53DD66548 CRC64;
MAMTDALKLY KAKRNFSITP EPAEGGEEGQ EALTFVIQKH WATRLHYDFR LELDGTMKSW
AVPKGPSYDS HDKRMAVHVE DHPISYNDFE GVIPEKQYGA GKVIIWDKGT WHPIGDPRKG
YRDGNLKFEL RGHKMHGRWA LVRMRRSGEK QEPWLLIKEN DEHVRPAGEF SVIDEMPDSV
KALGMPTAER LTPEAEEAES TAEEHQGKPA RKRAAGEKGK ATKTAATKAA AKKAPAKTKA
KAAAKAADPL ATVQLPATLS PELATLVDAP PADPENWIFE LKFDGYRLLA RVEGKSIELW
TRNGNNWTHK LEPLRATLEK MRLPDGWYDG EIVVHDTNGR PNFGLLQQAF DGEKTRNIVY
FIFDAPYLDG HDLRDVPLAQ RRELLQTVLG DAQGQVRFSA ELAAPPEEIV AAACRMGLEG
IIGKRRDALY TSRRSGDWIK LKCAQRQEFV IGGYTDPKGS RVGIGSLLLG YYDDAGKLHY
AGNVGAGFND TSLRDIIAKL KKVASDTNPF APTKAIEKRA HWVKPTLVAE VTFGEWTGSG
SIRHSVFHGL RTDKKAASIR REQAVHVEDV MQTQAESKSA GRKTSAKSGA RTKADPVSES
DVDSKLPATL KVTNADRLID PVSGMTKIGL VRYYALVSEL MLEHLKGRPL ALVRAPAGVG
GELFFQKHSE VGKLPGVKQL PQELDPDHPT MLEVPNVQGL LSCAQWNVVE FHTQNAFAKT
YEKPNRMVFD LDPGQGVSWQ QIQEAAQLMR AFLEQLGLPA FLKTSGGKGL HVVVPLKPQH
GWDAVKGFSS FIVEHMSRTL PDRFAFKSGP KNRVGKIFID YLRNGRGATT AAAWSARARP
GMGISVPVAW SELDHLKSGD QWTVATVHTR LDHGNEPWAD YAKSAVTLTK AMKQMGYKPA
//
