ID   F6EK72_HOYSD            Unreviewed;       750 AA.
AC   F6EK72;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
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:AEF42613.1};
GN   OrderedLocusNames=AS9A_4180 {ECO:0000313|EMBL:AEF42613.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS   (Amycolicicoccus subflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF42613.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF42613.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
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; CP002786; AEF42613.1; -; Genomic_DNA.
DR   RefSeq; WP_013808962.1; NC_015564.1.
DR   AlphaFoldDB; F6EK72; -.
DR   STRING; 443218.AS9A_4180; -.
DR   KEGG; asd:AS9A_4180; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_2_1_11; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000009235; 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; 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; 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:AEF42613.1};
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:UP000009235};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          544..667
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   750 AA;  83700 MW;  A22014DC6A57869F CRC64;
     MSKLVIDGYT VALTHLDKVL YPETGTTKGE IIAYYEAIAS VMLPHIRDRP ATRKRWPDGV
     TATPFFEKNI PFSAPDWIPR LPLEHKSRTV TYPLLNSTAA LVWIGQQAAL EVHVPQWIAR
     SGKPGPANRI VFDLDPGPGT TLADCAVVAK RIREIFREIG LPVYPVTSGS KGLHLYVPLV
     DPVSSAQASR VAQSVAASLE RALPELVTAT MSKAARPGKI FVDWSQNSAA KTTIAPYSLR
     GQSHPYVAAP RSWEELDDPH IAHLTFSDVL RRVDEFGDLL SPERPRPSES GPDRLALYRA
     KRDRALTPEP VPEPSENLKE NESEPLFVIQ EHHARRLHYD FRLERDGVLV SWAVPKNIPD
     TPDVNHLAVQ TEEHPMAYGS FAGEIPRGQY GAGEVKIWDR GTYTLEKWRD DEVIVELHGK
     RAQGRYALIK TGGKNWLMHK MKAPDANRRV RGIPRGLSPM LAKSASIKRL DAGEWAFEGK
     WDGYRAIAEI SEGTVRLLSR SGIDVTRDYP QLRQLSEDLG GHEVVLDGEL VGFGEEGVTS
     FARLREAPRE ATYLVFDVLY LDGTSLTRKP WSDRRKVLEA VAGLLRCASV PPLLTGSAED
     AIAESVQRGW EGVIAKRRDS IYLPGQRGTA WLKHKNWRTQ NVVVGGWKPG EGGHGGGIGA
     LLVGVMRDGK LRYAGRVGTG WSEKQRAELL ERLTLLVQEK SPFADWASEP ESSETQLRDV
     VWVRPEMEGT VRFQEWTSAR RLRHPVWMRS
//