ID A8FDM8_BACP2 Unreviewed; 621 AA. AC A8FDM8; DT 13-NOV-2007, integrated into UniProtKB/TrEMBL. DT 13-NOV-2007, sequence version 1. DT 27-MAR-2024, entry version 81. 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 OrderedLocusNames=BPUM_1666 {ECO:0000313|EMBL:ABV62345.1}; OS Bacillus pumilus (strain SAFR-032). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62345.1, ECO:0000313|Proteomes:UP000001355}; RN [1] {ECO:0000313|EMBL:ABV62345.1, ECO:0000313|Proteomes:UP000001355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62345.1, RC ECO:0000313|Proteomes:UP000001355}; RX PubMed=17895969; DOI=10.1371/journal.pone.0000928; RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y., RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., RA Weinstock G.M.; RT "Paradoxical DNA repair and peroxide resistance gene conservation in RT Bacillus pumilus SAFR-032."; RL PLoS ONE 2:E928-E928(2007). 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 --------------------------------------------------------------------------- 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; CP000813; ABV62345.1; -; Genomic_DNA. DR RefSeq; WP_012010077.1; NC_009848.4. DR AlphaFoldDB; A8FDM8; -. DR STRING; 315750.BPUM_1666; -. DR KEGG; bpu:BPUM_1666; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_0_2_9; -. DR OrthoDB; 9802472at2; -. DR Proteomes; UP000001355; 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 Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR014146; LigD_ligase_dom. DR InterPro; IPR014145; LigD_pol_dom. DR InterPro; IPR014143; NHEJ_ligase_prk. 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; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF21686; LigD_Prim-Pol; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 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:ABV62345.1}; 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 106..207 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" SQ SEQUENCE 621 AA; 71989 MW; F75EFA5776EA9D3B CRC64; MKPMRLTAAH DVPTGADWVY ELKYDGFRVI LTWDQNEIHL ESRAGKRLNE QFPEVIEQCE QLRDHFAPLL PLTFDGELVF LLDEQQSDFA RVQQRGRLKN KEAIKLQAER FPCHLIAFDL LRCKGKSLID LPLMERKTQL QQVFKAAKLP SSVQLEHPSL LQLIHTDTNS EHMKKLMTTY LAEGLVAKKR TSKWHDHTRS KEWLKVKNWR YVSVIVTRFD KENGYFQGCI YQDHHLTEVV QFKHGFSKEE EQTLRTLFQT NGKQTGASAY EIPPSIVASI ACISFDGSAL REPRFSSFLL DTDPTACTFQ QMLKQLYPLP TVIEITHPEK PIVPALHLNK ADYLLYLRQA APYLLPFLRE RRLTLIRFPH GAGDEFFYQK STPDYAPDYV LTDQADDIAY TVCNDPQTLL WLGNQLAMEF HIPFETRDTD RPTEIVFDLD PPSVNEFHLA IEAAKRIKTL LDGLFLTAFI KTSGGKGLQV YIPLKKNAFT YEETRTFTAF ICQFLCEQAP ELFTLERLKK KRGNRLYLDY IQHDAGKTII APYSPRGNEL GLVATPLEWD ELRQDGLHPS LFTMPSVIER LKEKGDPFRR MRHLVNDDTF RQVLHRLEDM IPAHKMDIRG H //