DNLI_BPT3
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 03-AUG-2022, entry version 102.
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 Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC Escherichia virus T3.
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 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; 2.40.50.140; -; 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 Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF17879; DNA_ligase_C; 2.
DR PIRSF; PIRSF001600; DNA_ligase_phage_T3; 1.
DR SUPFAM; SSF50249; SSF50249; 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
