ID A4T6Z6_MYCGI Unreviewed; 766 AA. AC A4T6Z6; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 98. 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=Mflv_1828 {ECO:0000313|EMBL:ABP44308.1}; OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain OS PYR-GCK)). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP44308.1}; RN [1] {ECO:0000313|EMBL:ABP44308.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP44308.1}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABP44308.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP44308.1}; RX PubMed=23469141; RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.; RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH RT during Pyrene Degradation."; RL PLoS ONE 8:E58066-E58066(2013). 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; CP000656; ABP44308.1; -; Genomic_DNA. DR AlphaFoldDB; A4T6Z6; -. DR STRING; 350054.Mflv_1828; -. DR KEGG; mgi:Mflv_1828; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_2_1_11; -. DR OrthoDB; 9802472at2; -. 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:ABP44308.1}; 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 553..675 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 306..326 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 766 AA; 85317 MW; CF2195716041FCEE CRC64; MVDRYDRVKL TNPDKVLYPA SGTTKAQVFE YYVNVAEGML PHIAGRAVTR KRWPNGVEES SFFEKQLASS APDWLDRGTI AHKSGTTTYP VIDTVEGLAW IAQQAALEVH VPQWRFTRGG QSGAADGGDG KPGPATRIVF DLDPGEGVTF RQLCEVAHEV RELITDIGLT TFPLTSGSKG LHLYVPLEDP ISSRGASVLA KRVAQQLEQS MPKRVTATMT KSLRDGKVFL DWSQNNGNKT TIAPYSLRGR ERPTVAAPRT WDEIEDPDLR HLTFDEVLDR LERDGDLLAD LDPPLPATDK LTRYRSMRDR TKTPEPVPAE PPETGANDKF VIQEHHARRL HYDFRLERDG VLVSWAVPKN LPDTPSVNHL AVHTEDHPMD YIDFAGEIPK GEYGGGEVHI WDTGTYETEK FRDNPPDGPA KGGEVIVTLH GQKIEGRYAL IQTDGKNWLA HRMKDQQKPT AADLAPMLTT EGSVERLTRG QWAFEGKWDG YRLLVDADHG KLTLRSRRGR DVTAEYPQLK ALAADLADHH VILDGEAVAL DEDGVPSFGE MQNRARSTRV EFWAFDILFL DGRLLTKATY TDRRKLLEAL AEGGGLIVPP ALEGDGPEAL EYARSQRWEG VIAKKRDSTY QPGRRSSAWI KDKIWNTQEV VIGGWRQGEG GRTSGIGALV LGVPDDDGLH FVGRVGTGFT DKQLASLKKT LEPLRTDESP FAAELPKQDA KGVTFVRPEL VGEVRYSERT SDGRLRQASW RGLRDDKVPE DVRWEG //