DNLI_ASFP4
ID DNLI_ASFP4 Reviewed; 419 AA.
AC P0C990;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 33.
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 OrderedLocusNames=Pret-112;
OS African swine fever virus (isolate Tick/South Africa/Pretoriuskop Pr4/1996)
OS (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561443;
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].
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 -!- 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; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C990; -.
DR Proteomes; UP000000859; 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_0000373089"
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 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"
SQ SEQUENCE 419 AA; 48208 MW; 655614DC7B9D1533 CRC64;
MLNHFPGHCS NNIFCFPPIE SETKSGKKAS WIICVQVVQH NTIIPITDEM FSTDVKDAVA
EIFTKFFVEE GTVRISKMTR ITEGKNLGKK NATTVVHQAF KDALSKYNRH ARQKRGAHTN
RGMIPPMLVK YFNIIPKTFF EEETDPIVQR KRNGVRAVAC QQGDGSILLY SRTEKEFLGL
DNIKKELKQL YLFIDVRVYL DGELYLHRKP LQWIAGQANA KTDSSELHFY VFDCFWSDQL
QMPSNKRQQL LTNIFKQKED LTFIHQVENF SVKNEDEALR LKAQFIKEGY EGAIVRNVNG
PYEPGYNNYH SAHLAKLKPL LDAEFILVDY TQGKKGKDLG AILWVCELPN KKRFVVTPKH
LTYADRYALF QKLTPALFKK HLYGKELTVE YAELSPKTGI PLQARAVGFR EPINVLEII
