ID C7NKD9_KYTSD Unreviewed; 878 AA. AC C7NKD9; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 68. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN OrderedLocusNames=Ksed_19790 {ECO:0000313|EMBL:ACV06977.1}; OS Kytococcus sedentarius (strain ATCC 14392 / DSM 20547 / CCM 314 / 541) OS (Micrococcus sedentarius). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae; OC Kytococcus. OX NCBI_TaxID=478801 {ECO:0000313|EMBL:ACV06977.1, ECO:0000313|Proteomes:UP000006666}; RN [1] {ECO:0000313|EMBL:ACV06977.1, ECO:0000313|Proteomes:UP000006666} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14392 / DSM 20547 / CCM 314 / 541 RC {ECO:0000313|Proteomes:UP000006666}; RX PubMed=21304632; DOI=10.4056/sigs.761; RA Sims D., Brettin T., Detter J.C., Han C., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F., RA Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N., RA Mavrommatis K., Chen A., Palaniappan K., D'haeseleer P., Chain P., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Schneider S., RA Goker M., Pukall R., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Kytococcus sedentarius type strain (541)."; RL Stand. Genomic Sci. 1:12-20(2009). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001686; ACV06977.1; -; Genomic_DNA. DR RefSeq; WP_015779917.1; NC_013169.1. DR AlphaFoldDB; C7NKD9; -. DR STRING; 478801.Ksed_19790; -. DR KEGG; kse:Ksed_19790; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_2_1_11; -. DR Proteomes; UP000006666; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. 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; 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 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACV06977.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}. FT DOMAIN 655..787 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 292..342 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 475..520 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..342 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 878 AA; 94745 MW; 1598F2222185E9DE CRC64; MARSERRTVR VGERTLSVSS LDKVLYPEAG TTKADVVHYY LSVAEVLLPQ LAGRPVTRKR WVDGVGTEGD PGEVFFRKDL EDSAPDWIPT GRIVHANRAN SYPLATEAAV LAWFAQVAAL ELHTPQWRFG PDGQPRRPDR LVLDLDPGEG VGLTECAQVA RWCREVLDGM ALEAFPVTSG SKGIHLYAAL DGTHDAEAVS AVAHELARAL EADHPDLVVS TMKRARRAGK VFLDWSQNNA SKTTVAPYSL RGRARPTVAA PRTWEELDDP GLAQLELDEV LDRVADGIDP VASLGAGTGP GGAGEVSSPA PDRLRTYRSM RDPDRTAEPV PADPPREREA PDGELPSFVI QEHHASSLHW DFRLEHSGVL VSWAVPKGPP LEHDTNRLAV MTEDHPLEYG TFEGTIAAGE YGAGEVTIWD AGTYERKKWR EGKEVIAVLH GRPDGGLGGV PRRFALIQAT GMGSERNWLL RLTDEQPGAG HPQDGSPEEV TAAPSPSRSR ADRSDSRTAR RALRRRPAPG FTVADLPAAM AATAGTPEQV ERAVAGGQEW AFEMKWDGYR VVAGVRTAGQ GPADADADAD AGAEREGAVV LASRNGKDLT DTFPAAVELT RLLRGEAAER GGAVLDGELV ALDDRGRPDF GLLQAALGDG PGVNAAGDPI ELRYLVFDLL QLGAPGDPED RQRSLLRIPW GERRELLREV LGTGGDAVSV PPAHTGTLAQ AQRASRGLGL EGVVAKRVDA VYLPGQRGSA WVKLKTQRHQ EVVVIGVRQG RGGRSGGIGS LLVAVGDDEG ELRYAGRVGT GFSAAQLADI EKTLRRIERK TPPVDDVPAA DRTDAWWVTP RLVGEVSLAG RTRDQRVRQA VWRGWRPDKE AGEVRWEV //