ID B1KQN5_SHEWM Unreviewed; 288 AA. AC B1KQN5; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 80. DE SubName: Full=ATP dependent DNA ligase {ECO:0000313|EMBL:ACA86274.1}; DE Flags: Precursor; GN OrderedLocusNames=Swoo_1990 {ECO:0000313|EMBL:ACA86274.1}; OS Shewanella woodyi (strain ATCC 51908 / MS32). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA86274.1, ECO:0000313|Proteomes:UP000002168}; RN [1] {ECO:0000313|EMBL:ACA86274.1, ECO:0000313|Proteomes:UP000002168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Lykidis A., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella woodyi ATCC 51908."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. 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=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|ARBA:ARBA00001968}; 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; CP000961; ACA86274.1; -; Genomic_DNA. DR RefSeq; WP_012324620.1; NC_010506.1. DR AlphaFoldDB; B1KQN5; -. DR STRING; 392500.Swoo_1990; -. DR KEGG; swd:Swoo_1990; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_021047_0_0_6; -. DR Proteomes; UP000002168; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR CDD; cd07896; Adenylation_kDNA_ligase_like; 1. DR CDD; cd08041; OBF_kDNA_ligase_like; 1. DR Gene3D; 3.30.1490.70; -; 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; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR029319; DNA_ligase_OB. DR InterPro; IPR012340; NA-bd_OB-fold. DR PANTHER; PTHR47810; DNA LIGASE; 1. DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF14743; DNA_ligase_OB_2; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. PE 4: Predicted; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; KW Ligase {ECO:0000313|EMBL:ACA86274.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000002168}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..288 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002767301" FT DOMAIN 87..202 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|Pfam:PF01068" FT DOMAIN 216..281 FT /note="DNA ligase OB-like" FT /evidence="ECO:0000259|Pfam:PF14743" SQ SEQUENCE 288 AA; 32411 MW; A2CC2FC3C0E131CB CRC64; MKTLNRKWGE LVLFLLLFMS LSSVAGGEDA KLIQLATDAE IEGEITQYLI SEKLDGVRGF WDGEQLYTRS GLRIVTPAWF THSFPTYPLD GELWMGRGTF EQVSGLVRRK TPLESEWKKV TFMVFDFPES KLSFGQRYQY YVKALADISP YLSVIEQTQV PNVEQLNAKL ALVVNGGGEG LMLHKQDALY VAGRNRDLIK LKPFYDAEAT VIAHLPGKGQ FSGLLGALLV ETPEGVRFKI GTGFSLEERR QPPKLGDIIT YKYLGFTQKG TPRFASFLRV RVNSKVTQ //