ID D9TD68_MICAI Unreviewed; 344 AA. AC D9TD68; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 54. DE SubName: Full=DNA ligase D, 3'-phosphoesterase domain protein {ECO:0000313|EMBL:ADL44706.1}; GN OrderedLocusNames=Micau_1144 {ECO:0000313|EMBL:ADL44706.1}; OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Micromonospora. OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL44706.1, ECO:0000313|Proteomes:UP000001908}; RN [1] {ECO:0000313|EMBL:ADL44706.1, ECO:0000313|Proteomes:UP000001908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442 RC {ECO:0000313|Proteomes:UP000001908}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., RA Hirsch A.M., Woyke T.; RT "Complete sequence of Micromonospora aurantiaca ATCC 27029."; RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases. 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; CP002162; ADL44706.1; -; Genomic_DNA. DR RefSeq; WP_013284345.1; NC_014391.1. DR AlphaFoldDB; D9TD68; -. DR STRING; 644283.Micau_1144; -. DR KEGG; mau:Micau_1144; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_008325_2_0_11; -. DR OrthoDB; 9802472at2; -. DR Proteomes; UP000001908; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.30.1490.70; -; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR014144; LigD_PE_domain. DR NCBIfam; TIGR02777; LigD_PE_dom; 1. DR PANTHER; PTHR39465:SF1; DNA LIGASE D 3'-PHOSPHOESTERASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR39465; DNA LIGASE D, 3'-PHOSPHOESTERASE DOMAIN; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF13298; LigD_N; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 4: Predicted; KW Ligase {ECO:0000313|EMBL:ADL44706.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001908}. FT DOMAIN 260..344 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..29 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 344 AA; 38668 MW; 15D4B01907AF8AD9 CRC64; MADRLEEYRR KRDAARTPEP VPERAPGRKR SARRAPRFVI QQHHARSLHW DLRLEHDGVL ASWAVPRGLP RDPGRNHLAV HTEDHPMEYL TFHGEIPAGE YGGGRMIVHD TGTYRAEKWR DDEVIVVLDG ERTKGRYVLF ATGGRGRDWM IRRTDPAPEG WTPMPELVRP MLPAEGGRLP RDAAAWGYEL RWAGVRAMAY VSGGRLRLLD GDDTEVTGDY PWTRAMAEAL APAEAVIDGV LVRIDPAGRV RPPTRRDGQF LAVDLLWLEG VSSLDVPYAQ RRDLLDGLAL TGPHWQTPPW FPGVGADALR AAREQGLPGV VAKRLDSPYE PGRRSRHWLS IDAS //