ID A4VMW1_STUS1 Unreviewed; 568 AA. AC A4VMW1; DT 29-MAY-2007, integrated into UniProtKB/TrEMBL. DT 29-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN OrderedLocusNames=PST_2662 {ECO:0000313|EMBL:ABP80312.1}; OS Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Stutzerimonas. OX NCBI_TaxID=379731 {ECO:0000313|EMBL:ABP80312.1, ECO:0000313|Proteomes:UP000000233}; RN [1] {ECO:0000313|EMBL:ABP80312.1, ECO:0000313|Proteomes:UP000000233} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A1501 {ECO:0000313|EMBL:ABP80312.1, RC ECO:0000313|Proteomes:UP000000233}; RX PubMed=18495935; DOI=10.1073/pnas.0801093105; RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W., RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y., RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.; RT "Nitrogen fixation island and rhizosphere competence traits in the genome RT of root-associated Pseudomonas stutzeri A1501."; RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008). 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; CP000304; ABP80312.1; -; Genomic_DNA. DR RefSeq; WP_011913769.1; NC_009434.1. DR AlphaFoldDB; A4VMW1; -. DR KEGG; psa:PST_2662; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_005138_6_2_6; -. DR Proteomes; UP000000233; 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:ABP80312.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Reference proteome {ECO:0000313|Proteomes:UP000000233}. FT DOMAIN 337..469 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" SQ SEQUENCE 568 AA; 63680 MW; 222BDDE93F28A196 CRC64; MKAFATLYSR LDATTSSNAK LAAMRDYFRE ADPSDAAWAV YFLAGGRPRQ LVPTRALRET AMQAAGLPEW LFEESYQAVG DMAETISLLM SEAEHSSEDG LAVWMQDRLL PLRGLPPEEL AERLPALWAQ LDRLSLMVCI KLITGAFRVG VSKLLVTRAL ASLADLDPKR VAQRLVGYTD LSHRPSAEGY RALIAEESEH EHAQRGGQPY PFFLAHALQA PVDTFDTLLG APDNWFIEWK WDGIRAQLVK RDGQIWVWSR GEELVSERFP ELCELARCLP DGTVIDGEIL VWKHDPETPA GELFDAASTG EPSADGFGVQ PFALLQQRIG RKNLTAKVLQ DAPVAVLAYD LLEWQGDDWR QREHRERRQQ LEAVVGQCPS PQLMLSPLVS GADWQDLARQ REASRALGVE GMMIKARAAQ YGVGRTKDVG VWWKWKIDPY SVDAVLIYAQ RGHGRRASLY TDYTFAVWDG EPGDHERKLV PFAKAYSGLT DEEMRKVDAI VRKTTVEKFG PVRSVTPTLV FELGFEGIAA SSRHKSGIAV RFPRMLRWRL DKPVEEADTL ATLRELLG //