ID F2R8H7_STRVP Unreviewed; 309 AA. AC F2R8H7; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 47. DE SubName: Full=ATP-dependent DNA ligase {ECO:0000313|EMBL:CCA53895.1}; DE EC=6.5.1.1 {ECO:0000313|EMBL:CCA53895.1}; GN OrderedLocusNames=SVEN_0608 {ECO:0000313|EMBL:CCA53895.1}; OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM OS 4526 / NBRC 13096 / PD 04745). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA53895.1, ECO:0000313|Proteomes:UP000006854}; RN [1] {ECO:0000313|EMBL:CCA53895.1, ECO:0000313|Proteomes:UP000006854} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA53895.1}; RX PubMed=21463507; DOI=10.1186/1471-2164-12-175; RA Pullan S.T., Bibb M.J., Merrick M.; RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae RT provides new insights into global nitrogen regulation in actinomycetes."; RL BMC Genomics 12:175-175(2011). 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; FR845719; CCA53895.1; -; Genomic_DNA. DR RefSeq; WP_015031814.1; NZ_JABVZO010000096.1. DR AlphaFoldDB; F2R8H7; -. DR STRING; 953739.SVEN_0608; -. DR GeneID; 69862809; -. DR KEGG; sve:SVEN_0608; -. DR PATRIC; fig|953739.5.peg.792; -. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_1_1_11; -. DR OrthoDB; 4296267at2; -. DR Proteomes; UP000006854; 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; cd04861; LigD_Pol_like; 1. DR Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1. DR InterPro; IPR014145; LigD_pol_dom. 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; PF21686; LigD_Prim-Pol; 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:CCA53895.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000006854}. FT DOMAIN 36..286 FT /note="DNA ligase D polymerase" FT /evidence="ECO:0000259|Pfam:PF21686" SQ SEQUENCE 309 AA; 34610 MW; F9411103C1BFAC89 CRC64; MTPTSRTAPP ERVRAGRRTV EIRRPDKVLF PGDGLTKADL AGYYRTVAHR MLPHLRGRPL MLERHPDGID GPAFMQKDVP DHFPDWVHRA ELPKEGGTVT YVLCEDTATL LYLAGQACTT PHRFLSRADR PDRPDRLVFD LDPADEDFAP VREAALGLHR LLDELELPSS LMTTGSRGLH VVVALDRRAP FDDVRAFARG VADVLASRHP DRFTTEARKN ARRGRLYLDV QRNGYAQTAV VPYAVRARPG APVAAPLAWS DLDDPDLTAR RWTVATVDGL LKDDPWHDPP RPRSLRRARD LLAELTRGG //