ID F4FEW8_MICM1 Unreviewed; 385 AA. AC F4FEW8; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 47. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN Name=ligC {ECO:0000313|EMBL:AEB43680.1}; GN OrderedLocusNames=VAB18032_12830 {ECO:0000313|EMBL:AEB43680.1}; OS Micromonospora maris (strain DSM 45365 / JCM 31040 / NBRC 109089 / NRRL OS B-24793 / AB-18-032) (Verrucosispora maris). OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales; OC Micromonosporaceae; Micromonospora. OX NCBI_TaxID=263358 {ECO:0000313|EMBL:AEB43680.1, ECO:0000313|Proteomes:UP000008308}; RN [1] {ECO:0000313|EMBL:AEB43680.1, ECO:0000313|Proteomes:UP000008308} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AB-18-032 {ECO:0000313|EMBL:AEB43680.1, RC ECO:0000313|Proteomes:UP000008308}; RX PubMed=21551311; DOI=10.1128/JB.05041-11; RA Roh H., Uguru G.C., Ko H.J., Kim S., Kim B.Y., Goodfellow M., Bull A.T., RA Kim K.H., Bibb M.J., Choi I.G., Stach J.E.; RT "Genome sequence of the abyssomicin- and proximicin-producing marine RT actinomycete Verrucosispora maris AB-18-032."; RL J. Bacteriol. 193:3391-3392(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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000256|ARBA:ARBA00007572}. 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; CP002638; AEB43680.1; -; Genomic_DNA. DR AlphaFoldDB; F4FEW8; -. DR STRING; 263358.VAB18032_12830; -. DR KEGG; vma:VAB18032_12830; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_008325_4_1_11; -. DR Proteomes; UP000008308; 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:InterPro. DR CDD; cd07905; Adenylation_DNA_ligase_LigC; 1. DR CDD; cd07970; OBF_DNA_ligase_LigC; 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; IPR044119; Adenylation_LigC-like. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR044117; OBF_LigC-like. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1. DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS00697; DNA_LIGASE_A1; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEB43680.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008308}. FT DOMAIN 137..250 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" SQ SEQUENCE 385 AA; 42901 MW; A94FCC9885D0EA41 CRC64; MICLTVVGGV WLTVAVDLPI NPPVEPMLAR SVASIPTGPG MTYEPKWDGF RCIIFRDGDE VELASRGGKL MTRYFPEVVE QARRQLPARC AVDGELIVIR RDSPNAAPRL DFELLAQRIH PAASRVKLLA ETTPADFVAF DLLALDGESL LDVPYPTRRA RLEQALAKVR PPVHVTQITT DADTARRWFD VFEGAGLDGL IAKPADLPYE PGKRLMFKVK HARTADVVVA GFRWHKSGPV VGSLLLGLYD DAQVLHHIGV SASFTMARRA ELLEELAPYR EVGAEHPWVH GDHERGQRIP GGVSRWTGTK NLEWEPLRPE LVVEVAYDAM EGDRFRHTAR FVRWRPDRDP LSCRYDQLDR PVRFDVDQVL RGDPTVTVGS GTGSA //