DNLI_ASFM2
ID DNLI_ASFM2 Reviewed; 419 AA.
AC P26813;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=DNA ligase {ECO:0000250|UniProtKB:P35970};
DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN Name=LIG; OrderedLocusNames=Mal-108; ORFNames=g3L;
OS African swine fever virus (isolate Tick/Malawi/Lil 20-1/1983) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10500;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1614852; DOI=10.1093/nar/20.11.2667;
RA Hammond J.M., Kerr S.M., Smith G.L., Dixon L.K.;
RT "An African swine fever virus gene with homology to DNA ligases.";
RL Nucleic Acids Res. 20:2667-2671(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Very low-fidelity DNA ligase that seals nicks in double-
CC stranded DNA during DNA repair (By similarity). Together with the viral
CC repair DNA polymerase X, fills the single nucleotide gaps generated by
CC the AP endonuclease (By similarity). It is not essential for viral
CC replication and recombination (By similarity). Displays a very low
CC adenylation activity towards DNA with 3'-dideoxy- or 3'-amino-
CC terminated nicks compared to regular nick DNA (By similarity).
CC {ECO:0000250|UniProtKB:P35970}.
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 -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P35970}. Note=Found
CC in association with the viral nucleoid. {ECO:0000250|UniProtKB:P35970}.
CC -!- DOMAIN: The N-terminus domain (NTD) plays a critical role in DNA-
CC binding, catalytic complex assembly and catalysis.
CC {ECO:0000250|UniProtKB:P35970}.
CC -!- MISCELLANEOUS: Consistent with its intracellular location, ASFV encodes
CC its own replicative DNA polymerase and three base excision repair
CC enzymes: a class II AP endonuclease, the repair polymerase Pol X, and
CC an ATP-dependent DNA ligase.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000305}.
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DR EMBL; X65192; CAA46310.1; -; Genomic_DNA.
DR EMBL; X71982; CAA50805.1; -; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S23018; S23018.
DR SMR; P26813; -.
DR PRIDE; P26813; -.
DR Proteomes; UP000000860; Genome.
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: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: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_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF01068; DNA_ligase_A_M; 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; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Metal-binding; Nucleotide-binding;
KW Virion.
FT CHAIN 1..419
FT /note="DNA ligase"
FT /id="PRO_0000059594"
FT REGION 1..120
FT /note="NTD"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT REGION 121..317
FT /note="AD domain"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT REGION 318..419
FT /note="OB domain"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT ACT_SITE 151
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT BINDING 203
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT BINDING 291
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT SITE 153
FT /note="Important for the catalytic efficiency"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT SITE 211
FT /note="Important for the catalytic efficiency"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT SITE 402
FT /note="Important for the catalytic efficiency"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT SITE 403
FT /note="Important for the catalytic efficiency"
FT /evidence="ECO:0000250|UniProtKB:P35970"
FT CONFLICT 149..150
FT /note="HG -> QR (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 48041 MW; DA781C64CA1B10F0 CRC64;
MLSQFPGQCS NNVFCFPPIE SETKNGKKAS WIICVQVMQH NTILPITDEM FSTDVKDAVA
EIFTKFFVEE GAVRISKTTR VTEGKNLGKK NATTVVHQAF KDALSKYNRH ARQKRGAHTN
RGMIPPMLVK YFNIIPKTFF EEETDPIVHG KRNGVRAVAC QQGDGSILLY SRTEKEFLGL
DNIKKELKQL YLFIDVRVYL DGELYLHRKP LQWIAGQANA KADSSELHFY VFDCFWSDQL
QMPSNKRQQL LTNIFKQKED LTFIHQVENF SVKNEDEALR LKTQFIKEGY EGAIVRNANG
PYEPGYNNYH SPHLAKLKPL LDAEFILVDY TQGKKGKDLG AILWVCELPN KKRFVVTPKH
LTYADRYALF QKLTPALFKK HLYGKELTVE YAELSPKTGI PLQARAVGFR EPINVLEII
