ID F8CR28_MYXFH Unreviewed; 347 AA. AC F8CR28; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 57. DE SubName: Full=DNA ligase {ECO:0000313|EMBL:AEI63072.1}; DE EC=6.5.1.1 {ECO:0000313|EMBL:AEI63072.1}; GN OrderedLocusNames=LILAB_05755 {ECO:0000313|EMBL:AEI63072.1}; OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Myxococcaceae; Myxococcus. OX NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI63072.1, ECO:0000313|Proteomes:UP000000488}; RN [1] {ECO:0000313|EMBL:AEI63072.1, ECO:0000313|Proteomes:UP000000488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488}; RX PubMed=21868801; DOI=10.1128/JB.05516-11; RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.; RT "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW- RT 1."; RL J. Bacteriol. 193:5015-5016(2011). 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; CP002830; AEI63072.1; -; Genomic_DNA. DR AlphaFoldDB; F8CR28; -. DR STRING; 483219.LILAB_05755; -. DR KEGG; mfu:LILAB_05755; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_021047_2_0_7; -. DR Proteomes; UP000000488; 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:0008270; F:zinc ion binding; IEA:InterPro. 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; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR029319; DNA_ligase_OB. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR007527; Znf_SWIM. 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. DR PROSITE; PS00333; DNA_LIGASE_A2; 1. DR PROSITE; PS50966; ZF_SWIM; 1. PE 4: Predicted; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; KW Ligase {ECO:0000313|EMBL:AEI63072.1}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325}; KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}. FT DOMAIN 20..59 FT /note="SWIM-type" FT /evidence="ECO:0000259|PROSITE:PS50966" FT REGION 59..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 347 AA; 38117 MW; DB64E39BC08D5B8D CRC64; MADIADGEQV SVKGSGAKPY ILKNTGGVYS CSCPAWRNQS VAIERRTCKH LRRVRGDAAE DARIGGDATT APARPARTPS ASDDSKAPPL LLAQSWENDV DLTGWWMSEK LDGVRAYWDG KQFWSRLGNA FLAPEWFTAG LPDFPLDGEL FGGRKRFQRT VSIVRRQDRG DDWKELAFVV FDAPGVDGAF EARLERCRQW MEEAKPAYAQ WHAHARCDGT PHLRAELARV EGLGGEGLML RQPGSRYEAG RSHTLLKVKS FKDDEARVVG HVPGAGRHKG RLGALEVELR DGTRFNVGTG LSDAERAAPP PVGAIITFRY QELSNDGVPR FPSYVGVRVD AAPFAAS //