ID F0SQ31_RUBBR Unreviewed; 546 AA. AC F0SQ31; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 57. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN OrderedLocusNames=Plabr_3611 {ECO:0000313|EMBL:ADY61208.1}; OS Rubinisphaera brasiliensis (strain ATCC 49424 / DSM 5305 / JCM 21570 / IAM OS 15109 / NBRC 103401 / IFAM 1448) (Planctomyces brasiliensis). OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales; OC Planctomycetaceae; Rubinisphaera. OX NCBI_TaxID=756272 {ECO:0000313|EMBL:ADY61208.1, ECO:0000313|Proteomes:UP000006860}; RN [1] {ECO:0000313|Proteomes:UP000006860} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49424 / DSM 5305 / JCM 21570 / NBRC 103401 / IFAM 1448 RC {ECO:0000313|Proteomes:UP000006860}; RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., Lu M., RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F., RA Hugenholtz P., Woyke T., Wu D., Tindall B., Pomrenke H.G., Brambilla E., RA Klenk H.-P., Eisen J.A.; RT "The complete genome of Planctomyces brasiliensis DSM 5305."; RL Submitted (FEB-2011) 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 --------------------------------------------------------------------------- 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; CP002546; ADY61208.1; -; Genomic_DNA. DR RefSeq; WP_013629927.1; NC_015174.1. DR AlphaFoldDB; F0SQ31; -. DR STRING; 756272.Plabr_3611; -. DR KEGG; pbs:Plabr_3611; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_005138_6_2_0; -. DR OrthoDB; 9767858at2; -. DR Proteomes; UP000006860; 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: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; cd07897; Adenylation_DNA_ligase_Bac1; 1. DR CDD; cd07972; OBF_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; IPR026333; ATP_dep_DNA_lig_pp_1105_fam. 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; IPR012308; DNA_ligase_ATP-dep_N. DR InterPro; IPR036599; DNA_ligase_N_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR NCBIfam; TIGR04120; DNA_lig_bact; 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; PS00697; DNA_LIGASE_A1; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADY61208.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000006860}. FT DOMAIN 305..436 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" SQ SEQUENCE 546 AA; 62521 MW; DBA2733AD23EFC26 CRC64; MKRFCELFRE LDGTTKTSRR HSALQDYFRE APANDAAWAT YILSGRRLKR LVKHGDLRAW GAELAELPDW LFEECYHMAG DLAETIALVI HEDRSRPVEG SLTHWMEEVV APLGEKSPEE QRTTLQHSWS QLDAWSRFVF NKLITGGLRI GVSQRSVVKA LAATFEIEPN VIAHRLMGPW EPTAEFFEQL VSEDAGEADL SQPYPFCLAH PFDAEPESLG AVEDWLADWK WDGIRAQAIR RGQAWFLWSR GEELLNERFP DFDDDLRSLP PGTVLDGELV GWKDGQVLPF GELQKRIARK RIGPKILRDV PVKFIAFDVL EHQGQDIRDT PMRQRRDTLE RLLVNRDEDS RLMISPAIEA ANWEEMASLR EQSRELGVEG IMLKHTESAY QTGRVSGSWW KWKIAPYTID AVLIYAQAGH GRRASLYTDY TFALWDGDTL VPFAKAYSGL TDAEIRKVDK FIRSNTQERF GPVRSVKAEL VFELAFENIQ ESTRHKSGVA VRFPRIHRWR QDKPPEQANT LQELKAMMPA QRLPLLEETP SAGGSE //