ID A0A378TF67_9MYCO Unreviewed; 755 AA.
AC A0A378TF67;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 18-JUN-2025, 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=NCTC10821_02038 {ECO:0000313|EMBL:STZ58525.1};
OS Mycolicibacterium tokaiense.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Mycobacteriaceae; Mycolicibacterium.
OX NCBI_TaxID=39695 {ECO:0000313|EMBL:STZ58525.1, ECO:0000313|Proteomes:UP000254978};
RN [1] {ECO:0000313|EMBL:STZ58525.1, ECO:0000313|Proteomes:UP000254978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10821 {ECO:0000313|EMBL:STZ58525.1,
RC ECO:0000313|Proteomes:UP000254978};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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 -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent DNA
CC ligase family. {ECO:0000256|ARBA:ARBA00049981}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the LigD polymerase
CC family. {ECO:0000256|ARBA:ARBA00049990}.
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DR EMBL; UGQT01000001; STZ58525.1; -; Genomic_DNA.
DR RefSeq; WP_115278322.1; NZ_AP022600.1.
DR AlphaFoldDB; A0A378TF67; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000254978; 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; cd04863; MtLigD_Pol_like; 1.
DR CDD; cd07971; OBF_DNA_ligase_LigD; 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; IPR033649; MtLigD_Pol-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR052171; NHEJ_LigD.
DR NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR NCBIfam; TIGR02778; ligD_pol; 1.
DR NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR NCBIfam; NF007210; PRK09632.1; 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 3: Inferred from homology;
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:STZ58525.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000254978};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 545..667
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 295..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 83408 MW; A5CDAC93E52EC18A CRC64;
MERLGRVRLT NADKVLYPET GTTKGEVFDY YVAIAEVMVP HTAGRATTRK RWPNGVAEPA
FFEKQLASSA PDWLTRASVK HGSGTITYPI IDSQESLAWI AQQASLEVHV PQWRFDSGII
GPATRLVFDL DPGDDVPMSQ LCEVARAVRD LMDDVGLTVY PLTSGSKGLH LYARFDEPVS
SRGAVVLAKR VAQQLEQAMP KKVTSTMTKS LRTGKVFVDW SQNSASKTTI APYSLRGRER
PTVAAPRTWE ELDAPDALEH LTYAEVLARV ARDGDLLAAL DPDAPVSDKL STYRSMRDAG
KTPEPVPSSR PALGHDNTFV IQEHHARRLH YDFRLERGGV LVSWAVPKNL PDTPSVNHLA
VHTEDHPLEY ATFEGEIPKG EYGGGKVIVW DSGSYEAEKF RDPGVDGESV DGKKGEVIVT
LHGTRITGRY ALIQTGGKNW IAHRMKEQDQ PGVGDFAPML ATHGSVERLK SGPWAFEGKW
DGYRMLVEVD HGDLRLRSRS GRDVTAEFPQ LRSLAADLAD HHVVLDGEVV ALDSNGVPSF
GEMQNRARST RVEFWAFDLL VLDGRSLVRA KYSDRRRLLE AFADGTDLIV PEQIPGDGPQ
ALEYAREQRW EGVVAKKRDS TYQPGRRSAS WIKDKLWNTQ EVVIGGWRQG EGGRSSGIGA
LLMGVPGDGG LEFVGRVGTG FTDKELAKLK TLLTPVDESP FNATLVGPDA RGVTYVEPVH
VGEVRYSERT SDGRLRQPSW RGLRPDKSPD EVVWE
//
