ID DNLI_BPT4 Reviewed; 487 AA. AC P00970; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 02-SEP-2026, entry version 120. DE RecName: Full=DNA ligase; DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135}; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP]; GN Name=30; OS Enterobacteria phage T4 (Bacteriophage T4). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Pantevenvirales; Straboviridae; Tevenvirinae; Tequatrovirus. OX NCBI_TaxID=10665; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6314278; DOI=10.1093/nar/11.20.7145; RA Armstrong J., Brown R.S., Tsugita A.; RT "Primary structure and genetic organization of phage T4 DNA ligase."; RL Nucleic Acids Res. 11:7145-7156(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003; RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.; RT "Bacteriophage T4 genome."; RL Microbiol. Mol. Biol. Rev. 67:86-156(2003). RN [3] {ECO:0007744|PDB:5WFY, ECO:0007744|PDB:6DRT, ECO:0007744|PDB:6DT1} RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 1-129 IN COMPLEX WITH DNA, AND RP INTERACTION WITH THE VIRAL SLIDING CLAMP. RX PubMed=30169742; DOI=10.1093/nar/gky776; RA Shi K., Bohl T.E., Park J., Zasada A., Malik S., Banerjee S., Tran V., RA Li N., Yin Z., Kurniawan F., Orellana K., Aihara H.; RT "T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a RT unique mode of sliding clamp interaction."; RL Nucleic Acids Res. 46:10474-10488(2018). CC -!- FUNCTION: DNA ligase, which is expressed in the early stage of lytic CC development, has been implicated in T4 DNA synthesis and genetic CC recombination. It may also play a role in T4 DNA repair. 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}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Interacts with the sliding clamp. CC {ECO:0000269|PubMed:30169742}. 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; X00039; CAA24921.1; -; Genomic_DNA. DR EMBL; AF158101; AAD42440.1; -; Genomic_DNA. DR PIR; A01201; LQBP34. DR RefSeq; NP_049813.1; NC_000866.4. DR PDB; 5WFY; X-ray; 1.40 A; A=1-129. DR PDB; 6DRT; X-ray; 2.12 A; D/E/F=225-237. DR PDB; 6DT1; X-ray; 2.75 A; A/E=1-487. DR MDRepo; P00970; -. DR SMR; P00970; -. DR BindingDB; P00970; -. DR ChEMBL; CHEMBL5733; -. DR GeneID; 1258680; -. DR KEGG; vg:1258680; -. DR OrthoDB; 4135at10239; -. DR BRENDA; 6.5.1.1; 19300. DR PRO; PR:P00970; -. DR Proteomes; UP000009087; 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:0003909; F:DNA ligase activity; IDA:CACAO. 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; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. 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; 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 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 PDBsum; 5WFY; -. DR PDBsum; 6DRT; -. DR PDBsum; 6DT1; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair; KW DNA replication; Ligase; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..487 FT /note="DNA ligase" FT /id="PRO_0000059595" FT REGION 229..237 FT /note="Interaction with the sliding clamp" FT /evidence="ECO:0000269|PubMed:30169742" FT ACT_SITE 159 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135" FT BINDING 164 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 182 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 217 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 217 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 344 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 359 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 365 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT HELIX 2..10 FT /evidence="ECO:0007829|PDB:5WFY" FT HELIX 15..24 FT /evidence="ECO:0007829|PDB:5WFY" FT TURN 25..27 FT /evidence="ECO:0007829|PDB:5WFY" FT HELIX 29..39 FT /evidence="ECO:0007829|PDB:5WFY" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:5WFY" FT TURN 58..61 FT /evidence="ECO:0007829|PDB:5WFY" FT HELIX 65..71 FT /evidence="ECO:0007829|PDB:5WFY" FT HELIX 72..76 FT /evidence="ECO:0007829|PDB:5WFY" FT TURN 77..79 FT /evidence="ECO:0007829|PDB:5WFY" FT HELIX 83..96 FT /evidence="ECO:0007829|PDB:5WFY" FT HELIX 99..110 FT /evidence="ECO:0007829|PDB:5WFY" FT STRAND 114..116 FT /evidence="ECO:0007829|PDB:5WFY" FT HELIX 119..125 FT /evidence="ECO:0007829|PDB:5WFY" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 143..149 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 162..169 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 174..176 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 177..180 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 191..200 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 202..207 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 212..222 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:6DRT" FT HELIX 254..265 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 271..275 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 277..286 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 287..291 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 300..310 FT /evidence="ECO:0007829|PDB:6DT1" FT TURN 311..313 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 315..319 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 322..327 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 328..340 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 345..349 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 357..367 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 370..381 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 388..395 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 399..405 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 422..427 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 436..445 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 454..458 FT /evidence="ECO:0007829|PDB:6DT1" FT STRAND 460..464 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 474..478 FT /evidence="ECO:0007829|PDB:6DT1" FT HELIX 481..485 FT /evidence="ECO:0007829|PDB:6DT1" SQ SEQUENCE 487 AA; 55293 MW; 39F8718DD067F8AA CRC64; MILKILNEIA SIGSTKQKQA ILEKNKDNEL LKRVYRLTYS RGLQYYIKKW PKPGIATQSF GMLTLTDMLD FIEFTLATRK LTGNAAIEEL TGYITDGKKD DVEVLRRVMM RDLECGASVS IANKVWPGLI PEQPQMLASS YDEKGINKNI KFPAFAQLKA DGARCFAEVR GDELDDVRLL SRAGNEYLGL DLLKEELIKM TAEARQIHPE GVLIDGELVY HEQVKKEPEG LDFLFDAYPE NSKAKEFAEV AESRTASNGI ANKSLKGTIS EKEAQCMKFQ VWDYVPLVEI YSLPAFRLKY DVRFSKLEQM TSGYDKVILI ENQVVNNLDE AKVIYKKYID QGLEGIILKN IDGLWENARS KNLYKFKEVI DVDLKIVGIY PHRKDPTKAG GFILESECGK IKVNAGSGLK DKAGVKSHEL DRTRIMENQN YYIGKILECE CNGWLKSDGR TDYVKLFLPI AIRLREDKTK ANTFEDVFGD FHEVTGL //