ID A0LVI2_ACIC1 Unreviewed; 527 AA. AC A0LVI2; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 74. DE SubName: Full=DNA primase-like protein {ECO:0000313|EMBL:ABK53442.1}; GN OrderedLocusNames=Acel_1670 {ECO:0000313|EMBL:ABK53442.1}; OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B). OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae; OC Acidothermus. OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53442.1, ECO:0000313|Proteomes:UP000008221}; RN [1] {ECO:0000313|EMBL:ABK53442.1, ECO:0000313|Proteomes:UP000008221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / DSM 8971 / 11B RC {ECO:0000313|Proteomes:UP000008221}; RX PubMed=19270083; DOI=10.1101/gr.084848.108; RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V., RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C., RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.; RT "Complete genome of the cellulolytic thermophile Acidothermus RT cellulolyticus 11B provides insights into its ecophysiological and RT evolutionary adaptations."; RL Genome Res. 19:1033-1043(2009). 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; CP000481; ABK53442.1; -; Genomic_DNA. DR RefSeq; WP_011720505.1; NC_008578.1. DR AlphaFoldDB; A0LVI2; -. DR STRING; 351607.Acel_1670; -. DR KEGG; ace:Acel_1670; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_6_1_11; -. DR InParanoid; A0LVI2; -. DR OrthoDB; 9802472at2; -. DR Proteomes; UP000008221; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase 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; cd04865; LigD_Pol_like_2; 1. DR Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1. DR InterPro; IPR014144; LigD_PE_domain. DR InterPro; IPR014145; LigD_pol_dom. 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; PF13298; LigD_N; 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}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000008221}. FT DOMAIN 45..152 FT /note="DNA ligase D 3'-phosphoesterase" FT /evidence="ECO:0000259|Pfam:PF13298" FT DOMAIN 260..513 FT /note="DNA ligase D polymerase" FT /evidence="ECO:0000259|Pfam:PF21686" FT REGION 12..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 527 AA; 60093 MW; 0928BA0BA5CD73C3 CRC64; MADRRPGDLR EYRRRRNFCR TPEPAGRADP RHITRNSAEP RFVVQRHRAT RLHYDLRLEI NGVLVSWAVP KGPTLDPTVR RAAIHVEDHP LEYLDFEGAI PHGEYGGGDV IVWDTGTWRP HGTDDPAQAV VDGELHADFF GRKLRGRFVF VRRGTDEKSW LVLHKDDEHA VRGWNPEDYP RSVLSGATND DVARHPRRLW RGGRAHPVAQ HNDTEASADE IAALDALDDE GTWEVFGRRL KVTHLNKVIY PGRGRTHALT KRDLLRYAAR IAPVVMPYLA GRPFTMHRFP DGIDAPGFWH KQLPSHAPDW LPRWQNPSAK RGEAATYLVV DEPAALIWAV NFGAIEWHAW TSRTDRPDLP TWALVDIDPG SRTTWRELVE LALLHRDALD HLGVQGKPKL TGQRGIQIWI PIRRGPTFDD TRAWVEHLSK VVGSLMPDAV SWEWEKKRRA GRARLDFTQN AANKTLVAPY SPRPLPRAPV SAPVEWDELP HLRPDRFTVR TILDRLAERG DPFHALLTVN QQLPPLG //