DNLI_ASFB7
ID DNLI_ASFB7 Reviewed; 419 AA.
AC P35970;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=DNA ligase {ECO:0000303|PubMed:15938630};
DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP];
GN Name=LIG; OrderedLocusNames=Ba71V-100; ORFNames=NP419L;
OS African swine fever virus (strain Badajoz 1971 Vero-adapted) (Ba71V)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=10498;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8438592; DOI=10.1006/viro.1993.1161;
RA Yanez R.J., Vinuela E.;
RT "African swine fever virus encodes a DNA ligase.";
RL Virology 193:531-536(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11831707; DOI=10.1006/viro.1995.1149;
RA Yanez R.J., Rodriguez J.M., Nogal M.L., Yuste L., Enriquez C.,
RA Rodriguez J.F., Vinuela E.;
RT "Analysis of the complete nucleotide sequence of African swine fever
RT virus.";
RL Virology 208:249-278(1995).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15938630; DOI=10.1021/bi047706g;
RA Lamarche B.J., Showalter A.K., Tsai M.-D.;
RT "An error-prone viral DNA ligase.";
RL Biochemistry 44:8408-8417(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=30185597; DOI=10.1128/jvi.01293-18;
RA Alejo A., Matamoros T., Guerra M., Andres G.;
RT "A Proteomic Atlas of the African Swine Fever Virus Particle.";
RL J. Virol. 92:0-0(2018).
RN [5] {ECO:0007744|PDB:6IMJ, ECO:0007744|PDB:6IMK, ECO:0007744|PDB:6IML, ECO:0007744|PDB:6IMN}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), DOMAIN, AND DNA-BINDING.
RX PubMed=30674878; DOI=10.1038/s41467-019-08296-w;
RA Chen Y., Liu H., Yang C., Gao Y., Yu X., Chen X., Cui R., Zheng L., Li S.,
RA Li X., Ma J., Huang Z., Li J., Gan J.;
RT "Structure of the error-prone DNA ligase of African swine fever virus
RT identifies critical active site residues.";
RL Nat. Commun. 10:387-387(2019).
CC -!- FUNCTION: Very low-fidelity DNA ligase that seals nicks in double-
CC stranded DNA during DNA repair (PubMed:15938630). Together with the
CC viral repair DNA polymerase X, fills the single nucleotide gaps
CC generated by the AP endonuclease (PubMed:15938630). It is not essential
CC for viral replication and recombination (PubMed:15938630). Displays a
CC very low adenylation activity towards DNA with 3'-dideoxy- or 3'-amino-
CC terminated nicks compared to regular nick DNA (PubMed:15938630).
CC {ECO:0000269|PubMed:15938630}.
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, ECO:0000269|PubMed:15938630};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:30185597}. Note=Found
CC in association with the viral nucleoid. {ECO:0000269|PubMed:30185597}.
CC -!- DOMAIN: The N-terminus domain (NTD) plays a critical role in DNA-
CC binding, catalytic complex assembly and catalysis.
CC {ECO:0000269|PubMed:30674878}.
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; X65373; CAA46445.1; -; Genomic_DNA.
DR EMBL; U18466; AAA65329.1; -; Genomic_DNA.
DR PIR; A45397; A45397.
DR RefSeq; NP_042793.1; NC_001659.2.
DR PDB; 6IMJ; X-ray; 2.55 A; A/B=1-419.
DR PDB; 6IMK; X-ray; 2.50 A; A=1-419.
DR PDB; 6IML; X-ray; 2.35 A; A=1-419.
DR PDB; 6IMN; X-ray; 2.70 A; A/B=1-419.
DR PDBsum; 6IMJ; -.
DR PDBsum; 6IMK; -.
DR PDBsum; 6IML; -.
DR PDBsum; 6IMN; -.
DR SMR; P35970; -.
DR GeneID; 22220329; -.
DR KEGG; vg:22220329; -.
DR Proteomes; UP000000624; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; DNA damage;
KW DNA recombination; DNA repair; DNA replication; Ligase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Virion.
FT CHAIN 1..419
FT /note="DNA ligase"
FT /id="PRO_0000059592"
FT REGION 1..120
FT /note="NTD"
FT /evidence="ECO:0000269|PubMed:30674878"
FT REGION 121..317
FT /note="AD domain"
FT /evidence="ECO:0000269|PubMed:30674878"
FT REGION 318..419
FT /note="OB domain"
FT /evidence="ECO:0000269|PubMed:30674878"
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:0000269|PubMed:30674878"
FT BINDING 151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:30674878"
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:0000269|PubMed:30674878"
FT BINDING 232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:30674878"
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:0000269|PubMed:30674878"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:30674878"
FT SITE 153
FT /note="Important for the catalytic efficiency"
FT /evidence="ECO:0000269|PubMed:30674878"
FT SITE 211
FT /note="Important for the catalytic efficiency"
FT /evidence="ECO:0000269|PubMed:30674878"
FT SITE 402
FT /note="Important for the catalytic efficiency"
FT /evidence="ECO:0000269|PubMed:30674878"
FT SITE 403
FT /note="Important for the catalytic efficiency"
FT /evidence="ECO:0000269|PubMed:30674878"
SQ SEQUENCE 419 AA; 48164 MW; 491A25A4B9CFD807 CRC64;
MLNQFPGQYS NNIFCFPPIE SETKSGKKAS WIICVQVVQH NTIIPITDEM FSTDVKDAVA
EIFTKFFVEE GAVRISKMTR VTEGKNLGKK NATTVVHQAF KDALSKYNRH ARQKRGAHTN
RGMIPPMLVK YFNIIPKTFF EEETDPIVQR KRNGVRAVAC QQGDGCILLY SRTEKEFLGL
DNIKKELKQL YLFIDVRVYL DGELYLHRKP LQWIAGQANA KTDSSELHFY VFDCFWSDQL
QMPSNKRQQL LTNIFKQKED LTFIHQVENF SVKNVDEALR LKAQFIKEGY EGAIVRNANG
PYEPGYNNYH SAHLAKLKPL LDAEFILVDY TQGKKGKDLG AILWVCELPN KKRFVVTPKH
LTYADRYALF QKLTPALFKK HLYGKELTVE YAELSPKTGI PLQARAVGFR EPINVLEII
