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Database: UniProt
Entry: P07717
LinkDB: P07717
Original site: P07717 
ID   DNLI_BPT3               Reviewed;         346 AA.
AC   P07717;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   22-FEB-2023, entry version 105.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=1.3;
OS   Enterobacteria phage T3 (Bacteriophage T3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Autographiviridae; Studiervirinae; Teetrevirus; Teetrevirus T3Luria.
OX   NCBI_TaxID=10759;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Luria;
RX   PubMed=3586029; DOI=10.1016/0022-2836(87)90261-0;
RA   Schmitt M.P., Beck P.J., Kearney C.A., Spence J.L., Digiovanni D.,
RA   Condreay J.P., Molineux I.J.;
RT   "Sequence of a conditionally essential region of bacteriophage T3,
RT   including the primary origin of DNA replication.";
RL   J. Mol. Biol. 193:479-495(1987).
CC   -!- FUNCTION: DNA ligase, which is expressed in the early stage of lytic
CC       development, has been implicated in T7 DNA synthesis and genetic
CC       recombination. It may also play a role in T7 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   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; X17255; CAA35125.1; -; Genomic_DNA.
DR   EMBL; X05031; CAA28700.1; -; Genomic_DNA.
DR   PIR; S09539; S09539.
DR   RefSeq; NP_523305.1; NC_003298.1.
DR   SMR; P07717; -.
DR   GeneID; 927441; -.
DR   KEGG; vg:927441; -.
DR   OrthoDB; 4135at10239; -.
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:0006266; P:DNA ligation; IEA:InterPro.
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   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; 2.
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.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA replication;
KW   Ligase; Metal-binding; Nucleotide-binding.
FT   CHAIN           1..346
FT                   /note="DNA ligase"
FT                   /id="PRO_0000059597"
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:0000250"
FT   BINDING         39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         55..57
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   346 AA;  39351 MW;  896D38E6AB80EE3B CRC64;
     MNIFNTNPFK AVSFVESAVK KALETSGYLI ADCKYDGVRG NIVVDNVAEA AWLSRVSKFI
     PALEHLNGFD KRWQQLLNDD RCIFPDGFML DGELMVKGVD FNTGSGLLRT KWVKRDNMGF
     HLTNVPTKLT PKGREVIDGK FEFHLDPKRL SVRLYAVMPI HIAESGEDYD VQNLLMPYHV
     EAMRSLLVEY FPEIEWLIAE TYEVYDMDSL TELYEEKRAE GHEGLIVKDP QGIYKRGKKS
     GWWKLKPECE ADGIIQGVNW GTEGLANEGK VIGFSVLLET GRLVDANNIS RALMDEFTSN
     VKAHGEDFYN GWACQVNYME ATPDGSLRHP SFEKFRGTED NPQEKM
//
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