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Database: UniProt
Entry: A0A1D8T6P7_9NOCA
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ID   A0A1D8T6P7_9NOCA        Unreviewed;       767 AA.
AC   A0A1D8T6P7;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, 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   ORFNames=BFN03_13610 {ECO:0000313|EMBL:AOW93338.1};
OS   Rhodococcus sp. WMMA185.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=679318 {ECO:0000313|EMBL:AOW93338.1, ECO:0000313|Proteomes:UP000178767};
RN   [1] {ECO:0000313|EMBL:AOW93338.1, ECO:0000313|Proteomes:UP000178767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMMA185 {ECO:0000313|EMBL:AOW93338.1,
RC   ECO:0000313|Proteomes:UP000178767};
RA   Bugni T.S., Adnani N., Braun D., Chevrette M., McDonald B., Rajski S.;
RT   "Draft Genome of Rhodococcus sp. WMMA185.";
RL   Submitted (AUG-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; CP017014; AOW93338.1; -; Genomic_DNA.
DR   RefSeq; WP_070379449.1; NZ_CP017014.1.
DR   AlphaFoldDB; A0A1D8T6P7; -.
DR   STRING; 679318.BFN03_13610; -.
DR   KEGG; rhw:BFN03_13610; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000178767; 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; 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; IPR016059; DNA_ligase_ATP-dep_CS.
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   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 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; PS00697; DNA_LIGASE_A1; 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:AOW93338.1};
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:UP000178767};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          559..673
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          309..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  85315 MW;  0E628D3F24B21947 CRC64;
     MYWRREVCMT AGTRQITIGG HRLSLTNLGK VLYPDSGTTK GEVVDYYTRI APAMLPHIAD
     RAATRKRWPN GVDSESFFEK NLASSVPAWL ERRSLEHSDR TVQYPLLNSV AALAWAGQQA
     ALELHVPQWR FEGQRRGSAT RIVFDLDPGP GAGLPECAEV ARAVRDLVAN LGWTTFPVTS
     GSKGIHLYVP LDRKLEGAGP STVAKQVATG LEALRPELVT ASMAKAVRAG KVFVDWSQNN
     PSKTTIAPYS LRGRSQPWVA APRTWDELDD PDLRQLRFEE VLERWESDGD LLAGLDPPWE
     GAATLAEYRR KRDPGRTPEP MPSVVRPGDN SRFVIQEHHA RRLHYDLRLE RDGVLVSWAV
     PKNVPTTPSE NRLAVRTEDH PLEYLTFAGT IPKGEYGGGV MTIWDSGTYD AEKWRDDEVI
     VRLRGEKARG RFALIHTKGD QWLMHLMKNQ EASGPGSSDL PRGLSPMLAT PGTLDGLESD
     AWAFEGKWDG VRVIAEVSGG RLRLMSRTGN DKTGDYPRLG WLAEALGDHE VVLDGEVVAF
     DDRGVSDFGL LQQGGEPHFL AFDVLYLDGV SLLRKKYTDR RRVLEALAAK VDDLVVPPQL
     HGPAQEALDF SRGKGWEGVV AKRRDSVYLP GKRGSSWIKV KNWRTQEVVI GGWRRGRGAR
     SEGIGSLLLG IPDSGGLRYV GRVGTGFTQR DLRELASMLH PLETATSPFI DTLPTADRRD
     AVWVTPTLVG EVRFMEWTES GRLRHPSWRG LRDDKAPEDV KVEVDRV
//
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