ID DNLI_BPT7 Reviewed; 359 AA. AC P00969; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 02-SEP-2026, entry version 143. DE RecName: Full=DNA ligase; DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135, ECO:0000269|PubMed:8653795}; DE AltName: Full=DNA ligase gp1.3; DE AltName: Full=Gene product 1.3; DE Short=Gp1.3; GN OrderedLocusNames=1.3; OS Escherichia phage T7 (Bacteriophage T7). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Autographivirales; Autotranscriptaviridae; Studiervirinae; Teseptimavirus; OC Teseptimavirus T7. OX NCBI_TaxID=10760; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4; RA Dunn J.J., Studier F.W.; RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of RT T7 genetic elements."; RL J. Mol. Biol. 166:477-535(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9; RA Dunn J.J., Studier F.W.; RT "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to RT the beginning of gene 4."; RL J. Mol. Biol. 148:303-330(1981). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-359. RX PubMed=7001354; DOI=10.1093/nar/8.10.2119; RA Dunn J.J., Studier F.W.; RT "The transcription termination site at the end of the early region of RT bacteriophage T7 DNA."; RL Nucleic Acids Res. 8:2119-2132(1980). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5. RX PubMed=6254001; DOI=10.1073/pnas.77.7.3917; RA Saito H., Tabor S., Tamanoi F., Richardson C.C.; RT "Nucleotide sequence of the primary origin of bacteriophage T7 DNA RT replication: relationship to adjacent genes and regulatory elements."; RL Proc. Natl. Acad. Sci. U.S.A. 77:3917-3921(1980). RN [5] RP FUNCTION, AND MUTAGENESIS OF LYS-238 AND LYS-240. RX PubMed=10656817; DOI=10.1006/jmbi.1999.3423; RA Doherty A.J., Dafforn T.R.; RT "Nick recognition by DNA ligases."; RL J. Mol. Biol. 296:43-56(2000). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ATP, CATALYTIC RP ACTIVITY, AND DNA-BINDING. RX PubMed=8653795; DOI=10.1016/s0092-8674(00)81260-x; RA Subramanya H.S., Doherty A.J., Ashford S.R., Wigley D.B.; RT "Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7."; RL Cell 85:607-615(1996). CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA CC replication, DNA recombination and DNA repair in an ATP-dependent CC reaction. Binds specifically to DNA nicks containing a 3'-OH and a 5'- CC phosphate group. {ECO:0000269|PubMed:10656817}. 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:0000255|PROSITE- CC ProRule:PRU10135, ECO:0000269|PubMed:8653795}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000305}. 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; V01124; CAA24322.1; -; Genomic_DNA. DR EMBL; V01126; CAA24326.1; -; Genomic_DNA. DR EMBL; V01127; CAA24336.1; -; Genomic_DNA. DR EMBL; V01146; CAA24393.1; -; Genomic_DNA. DR PIR; E94615; LQBP37. DR RefSeq; NP_041963.1; NC_001604.1. DR PDB; 1A0I; X-ray; 2.60 A; A=2-349. DR SMR; P00969; -. DR MINT; P00969; -. DR GeneID; 1261055; -. DR KEGG; vg:1261055; -. DR OrthoDB; 4135at10239; -. DR BRENDA; 6.5.1.1; 736. DR EvolutionaryTrace; P00969; -. DR Proteomes; UP000000840; Segment. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. 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; IPR041559; DNA_ligase_ATP-dep_T7_C. DR InterPro; IPR016306; DNA_ligase_T7. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR050326; NAD_dep_DNA_ligaseB. DR PANTHER; PTHR47810; DNA LIGASE; 1. DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF17879; DNA_ligase_C; 1. DR PIRSF; PIRSF001600; DNA_ligase_phage_T3; 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; PS00333; DNA_LIGASE_A2; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. DR PDBsum; 1A0I; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair; KW DNA replication; DNA-binding; Ligase; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..359 FT /note="DNA ligase" FT /id="PRO_0000059598" FT ACT_SITE 34 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135" FT BINDING 32..35 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:8653795" FT BINDING 39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:8653795" FT BINDING 55..57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:8653795" FT BINDING 93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:8653795" FT BINDING 217 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 232 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:8653795" FT BINDING 238 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000305|PubMed:8653795" FT MUTAGEN 238 FT /note="K->A: Complete loss of transadenylation activity." FT /evidence="ECO:0000269|PubMed:10656817" FT MUTAGEN 240 FT /note="K->A: About 99% loss of transadenylation activity." FT /evidence="ECO:0000269|PubMed:10656817" FT STRAND 9..13 FT /evidence="ECO:0007829|PDB:1A0I" FT HELIX 16..26 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 27..33 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 37..45 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:1A0I" FT HELIX 61..66 FT /evidence="ECO:0007829|PDB:1A0I" FT HELIX 71..78 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 87..99 FT /evidence="ECO:0007829|PDB:1A0I" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:1A0I" FT HELIX 104..109 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 115..119 FT /evidence="ECO:0007829|PDB:1A0I" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 144..153 FT /evidence="ECO:0007829|PDB:1A0I" FT HELIX 154..159 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 163..166 FT /evidence="ECO:0007829|PDB:1A0I" FT HELIX 167..184 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 188..192 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 195..200 FT /evidence="ECO:0007829|PDB:1A0I" FT HELIX 201..212 FT /evidence="ECO:0007829|PDB:1A0I" FT TURN 213..215 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 219..222 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 230..240 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 243..253 FT /evidence="ECO:0007829|PDB:1A0I" FT TURN 257..259 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 277..281 FT /evidence="ECO:0007829|PDB:1A0I" FT HELIX 286..299 FT /evidence="ECO:0007829|PDB:1A0I" FT TURN 300..302 FT /evidence="ECO:0007829|PDB:1A0I" FT TURN 321..324 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 326..334 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 340..342 FT /evidence="ECO:0007829|PDB:1A0I" FT STRAND 344..348 FT /evidence="ECO:0007829|PDB:1A0I" SQ SEQUENCE 359 AA; 41133 MW; 43DA453B71BDF8DC CRC64; MMNIKTNPFK AVSFVESAIK KALDNAGYLI AEIKYDGVRG NICVDNTANS YWLSRVSKTI PALEHLNGFD VRWKRLLNDD RCFYKDGFML DGELMVKGVD FNTGSGLLRT KWTDTKNQEF HEELFVEPIR KKDKVPFKLH TGHLHIKLYA ILPLHIVESG EDCDVMTLLM QEHVKNMLPL LQEYFPEIEW QAAESYEVYD MVELQQLYEQ KRAEGHEGLI VKDPMCIYKR GKKSGWWKMK PENEADGIIQ GLVWGTKGLA NEGKVIGFEV LLESGRLVNA TNISRALMDE FTETVKEATL SQWGFFSPYG IGDNDACTIN PYDGWACQIS YMEETPDGSL RHPSFVMFRG TEDNPQEKM //