ID D1BX88_XYLCX Unreviewed; 592 AA. AC D1BX88; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN OrderedLocusNames=Xcel_2642 {ECO:0000313|EMBL:ACZ31656.1}; OS Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 / OS XIL07). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; OC Promicromonosporaceae; Xylanimonas. OX NCBI_TaxID=446471 {ECO:0000313|EMBL:ACZ31656.1, ECO:0000313|Proteomes:UP000002255}; RN [1] {ECO:0000313|Proteomes:UP000002255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07 RC {ECO:0000313|Proteomes:UP000002255}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Mikhailova N., Foster B., Clum A., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P., RA Woyke T., Wu D., Gehrich-Schroeter G., Schneider S., Pukall S.R., RA Klenk H.P., Eisen J.A.; RT "The complete chromosome of Xylanimonas cellulosilytica DSM 15894."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ31656.1, ECO:0000313|Proteomes:UP000002255} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15894 / CECT 5975 / LMG 20990 / XIL07 RC {ECO:0000313|Proteomes:UP000002255}; RX PubMed=21304672; DOI=10.4056/sigs.571102; RA Foster B., Pukall R., Abt B., Nolan M., Glavina Del Rio T., Chen F., RA Lucas S., Tice H., Pitluck S., Cheng J.-F., Chertkov O., Brettin T., RA Han C., Detter J.C., Bruce D., Goodwin L., Ivanova N., Mavromatis K., RA Pati A., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., RA Chang Y.-J., Jeffries C.D., Chain P., Rohde M., Goeker M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P., RA Lapidus A.; RT "Complete genome sequence of Xylanimonas cellulosilytica type strain RT (XIL07)."; RL Stand. Genomic Sci. 2:1-8(2010). 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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000256|RuleBase:RU004196}. 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; CP001821; ACZ31656.1; -; Genomic_DNA. DR AlphaFoldDB; D1BX88; -. DR STRING; 446471.Xcel_2642; -. DR KEGG; xce:Xcel_2642; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_005138_6_1_11; -. DR Proteomes; UP000002255; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1. DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR000977; DNA_ligase_ATP-dep. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR012308; DNA_ligase_ATP-dep_N. DR InterPro; IPR036599; DNA_ligase_N_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR NCBIfam; TIGR00574; dnl1; 1. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1. DR PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACZ31656.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000002255}. FT DOMAIN 361..485 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 87..109 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 592 AA; 60486 MW; 0B5305E500D788E3 CRC64; MPPRSAFRGA RPHIHGGGAV SRGPVSAAGG SIDSVLFHDV AVTSAGVAAT RSRLAKRELL AAALRAAAHG GMTGGDATAD GAAAGEGMAG GAATGGATTG GPGSDDGRAG EEVDVVATFL SGRVRQRRTG VGWRSLTSLP APASAPTLTP LDVDAALQTM ADAEGPGSAA VRGEAVRRLF AAATQDEQTF LRGLIVGELR QGALDSLLLD AVAAAADVPL AAVRRAAMFS APSGPIARAA LTGGAAALAA FRLEPGRPVR PMLASPAPDV AAALAGIGGP VAVEAKIDGI RVQLHKHGND VAVYTRSLDD VTERLPELVA LLRSLPVATA VLDGEAIALG ADGRPLAFQD TAARTGSHDA DATGRVPLTA FLFDALHLAG RDLVDAPESE RFAALERVAP PSALVRRIVT ADPDEATAFF AEVLASGHEG VVVKDLAAPY DAGRRGGAWV KVKPRHTLDL VVLAVERGSG RRSGWLSNIH LGARVPGAGP DSADGWVMLG KTFKGMSDEM LAWQTARFTE LADGPADGWV VRVRPEQVVE IAFDGVQRST RYPGGVALRF ARVLRYRDDK PAAEADTIDA VRAIAGGNAS GG //