ID DNLI_FOWPN Reviewed; 564 AA.
AC Q67480; Q9J5G0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 08-NOV-2023, entry version 99.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN Name=LIG; OrderedLocusNames=FPV043; ORFNames=A50R;
OS Fowlpox virus (strain NVSL) (FPV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Chitovirales; Poxviridae; Chordopoxvirinae; Avipoxvirus; Fowlpox virus.
OX NCBI_TaxID=928301;
OH NCBI_TaxID=7742; Vertebrata.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FP-9 / Isolate HP-438;
RX PubMed=8077953; DOI=10.1099/0022-1317-75-9-2495;
RA Skinner M.A., Moore J.B., Binns M.M., Smith G.L., Boursnell M.E.G.;
RT "Deletion of fowlpox virus homologues of vaccinia virus genes between the 3
RT beta-hydroxysteroid dehydrogenase (A44L) and DNA ligase (A50R) genes.";
RL J. Gen. Virol. 75:2495-2498(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10729156; DOI=10.1128/jvi.74.8.3815-3831.2000;
RA Afonso C.L., Tulman E.R., Lu Z., Zsak L., Kutish G.F., Rock D.L.;
RT "The genome of fowlpox virus.";
RL J. Virol. 74:3815-3831(2000).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. It is not essential for
CC viral replication and recombination.
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; Z29716; CAA82805.1; -; Genomic_DNA.
DR EMBL; AF198100; AAF44387.1; -; Genomic_DNA.
DR PIR; S41974; S41974.
DR RefSeq; NP_039006.1; NC_002188.1.
DR SMR; Q67480; -.
DR GeneID; 1486591; -.
DR KEGG; vg:1486591; -.
DR Proteomes; UP000008597; Segment.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; 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 CDD; cd07967; OBF_DNA_ligase_III; 1.
DR Gene3D; 3.30.1490.70; -; 1.
DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 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; IPR000977; DNA_ligase_ATP-dep.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR InterPro; IPR036599; DNA_ligase_N_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR00574; dnl1; 1.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1.
DR Pfam; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..564
FT /note="DNA ligase"
FT /id="PRO_0000059591"
FT ACT_SITE 236
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 281
FT /note="K -> N (in Ref. 1; CAA82805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 564 AA; 64487 MW; 85B5D829FEE89FA0 CRC64;
MEVTLKEFRE LCTSISTESS YVKKTKLISE FIHRGRDYND VYIITKLLLP GTGKLIYNIN
DKQLVKLFSK IFCHDADEMY KYVINIGDVA YVIGSFLKKS KSVVDYATES TLTLHEVDCF
LTRLSTVTRE NDQIKEIKKI IPRCTPNDLR HIIRLIKHDL RMNIGPKHVL SGLHKDAYGI
FKLCNNLEQV VQRSLEDNIK PLIELMVPLQ PMLASACKTF SEAVKKCPNG IIVEFKYDGE
RIQIHKHDKN FKYFSRSLKP ITPHKVTDFE ELLDRAFPSA KNMILDGEII LIDTETNQPL
PFGTLGINKK SMYHNACVCI FIFDCLYFND TVLIDKPLIE RRNIIHANIK EIPNRILLSE
VKNISTDEEL SKLLHIVLSK NIEGFVLKDA KGVYEPGMRR WLKIKKDYLD GCVMADKADL
VVLGAYYGKG NKSGILSSFL MGCYDTKSEK WCTVTKCSGG HTDLELQEIN DNLSVVPFDR
NAIPDWLSIN KIHYPDVIIS DISLAPVWEI IGSEFTRSST HTASNISIRF PRCSRIREDK
TYETANNLND IKQLYAVSIS PPEE
//
