DNLI_NPVLD
ID DNLI_NPVLD Reviewed; 548 AA.
AC Q9YMV2;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=LdOrf-22;
OS Lymantria dispar multicapsid nuclear polyhedrosis virus (LdMNPV).
OC Viruses; Naldaviricetes; Lefavirales; Baculoviridae; Alphabaculovirus.
OX NCBI_TaxID=10449;
OH NCBI_TaxID=7088; Lepidoptera (butterflies and moths).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9887315; DOI=10.1006/viro.1998.9469;
RA Kuzio J., Pearson M.N., Harwood S.H., Funk C.J., Evans J.T., Slavicek J.M.,
RA Rohrmann G.F.;
RT "Sequence and analysis of the genome of a baculovirus pathogenic for
RT Lymantria dispar.";
RL Virology 253:17-34(1999).
RN [2]
RP CHARACTERIZATION.
RX PubMed=9765460; DOI=10.1128/jvi.72.11.9142-9149.1998;
RA Pearson M.N., Rohrmann G.F.;
RT "Characterization of a baculovirus-encoded ATP-dependent DNA ligase.";
RL J. Virol. 72:9142-9149(1998).
CC -!- FUNCTION: Able to ligate a double-stranded synthetic DNA substrate
CC containing a single nick and inefficiently ligated a 1 nucleotide gap
CC but did not ligate a 2 nucleotide gap. It is able to ligate short,
CC complementary overhangs but not blunt-ended double-stranded DNA. May be
CC implicated in DNA repair 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; AF081810; AAC70207.1; -; Genomic_DNA.
DR PIR; T30369; T30369.
DR RefSeq; NP_047658.1; NC_001973.1.
DR SMR; Q9YMV2; -.
DR GeneID; 1488619; -.
DR KEGG; vg:1488619; -.
DR BRENDA; 6.5.1.1; 3111.
DR Proteomes; UP000203997; Genome.
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 Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 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 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; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00574; dnl1; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Metal-binding; Nucleotide-binding.
FT CHAIN 1..548
FT /note="DNA ligase"
FT /id="PRO_0000059593"
FT REGION 515..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 361
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"
SQ SEQUENCE 548 AA; 61975 MW; 74F5A2A3CDC24419 CRC64;
MENHDSFYKF CQLCQSLYDA DDHQEKRDAL ERHFADFRGS AFMWRELLAP AESDAAADRE
LTLIFETILS IERTEQENVT RNLKCTIDGA AVPLSRESRI TVPQVYEFIN DLRGSGSRQE
RLRLIGQFAA GCTDEDLLTV FRVVSDHAHA GLSAEDVMEL VEPWERFQKP VPPALAQPCR
RLASVLVKHP EGALAEVKYD GERVQVHKAG SRFKFFSRTL KPVPEHKVAG CREHLTRAFP
RARNFILDAE IVMVDGSGEA LPFGTLGRLK QMEHADGHVC MYIFDCLRYN GVSYLNATPL
DFRRRVLQDE IVPIEGRVVL SAMERTNTLS ELRRFVHRTL ATGAEGVVLK GRLSSYAPNK
RDWFKMKKEH LCDGALVDTL DLVVLGAYYG TGRNCRKMSV FLMGCLDRES NVWTTVTKVH
SGLADAALTA LSKELRPLMA APRDDLPEWF DCNESMVPHL LAADPEKMPV WEIACSEMKA
NIGAHTAGVT MRFPRVKRFR PDKDWSTATD LQEAEQLIRN SQENTKKTFA RLATTYDGPS
PNKKLKLN
