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   16-JUN-2009, entry version 59.
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.1;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN   Name=1.3;
OS   Enterobacteria phage T3 (Bacteriophage T3).
OC   Viruses; dsDNA viruses, no RNA stage; Caudovirales; Podoviridae;
OC   Autographivirinae; T7-like viruses.
OX   NCBI_TaxID=10759;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Luria;
RX   MEDLINE=87226207; 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
CC       lytic development, has been implicated in T7 DNA synthesis and
CC       genetic recombination. It may also play a role in T7 DNA repair.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m).
CC   -!- COFACTOR: Divalent metal cations (By similarity).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
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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; -.
DR   HSSP; P00969; 1A0I.
DR   SMR; P07717; 6-336.
DR   GeneID; 927441; -.
DR   BRENDA; 6.5.1.1; 164907.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:EC.
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   InterPro; IPR012310; DNA_ligase_A_M.
DR   InterPro; IPR016059; DNA_ligase_CS.
DR   InterPro; IPR016306; DNA_ligase_phage.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   PIRSF; PIRSF001600; DNA_ligase_phage_T3; 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;
KW   DNA replication; Ligase; Metal-binding; Nucleotide-binding.
FT   CHAIN         1    346       DNA ligase.
FT                                /FTId=PRO_0000059597.
FT   NP_BIND      32     35       ATP (By similarity).
FT   NP_BIND      55     57       ATP (By similarity).
FT   ACT_SITE     34     34       N6-AMP-lysine intermediate (By
FT                                similarity).
FT   METAL       223    223       Divalent metal cation (By similarity).
FT   BINDING      39     39       ATP (By similarity).
FT   BINDING      93     93       ATP (By similarity).
FT   BINDING     142    142       ATP (By similarity).
FT   BINDING     149    149       ATP (By similarity).
FT   BINDING     238    238       ATP (By similarity).
FT   BINDING     244    244       ATP (By similarity).
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
//