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Database: UniProt
Entry: P00970
LinkDB: P00970
Original site: P00970 
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   08-NOV-2023, entry version 116.
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   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}.
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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   PDBsum; 5WFY; -.
DR   PDBsum; 6DRT; -.
DR   PDBsum; 6DT1; -.
DR   SMR; P00970; -.
DR   BindingDB; P00970; -.
DR   ChEMBL; CHEMBL5733; -.
DR   GeneID; 1258680; -.
DR   KEGG; vg:1258680; -.
DR   OrthoDB; 4135at10239; -.
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   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.
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   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:5WFY"
FT   HELIX           65..74
FT                   /evidence="ECO:0007829|PDB:5WFY"
FT   TURN            75..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
//
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