DPOLX_ASFM2
ID DPOLX_ASFM2 Reviewed; 174 AA.
AC P0C984;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Repair DNA polymerase X;
DE Short=Pol X;
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P42494};
GN OrderedLocusNames=Mal-105;
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 [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: Error-prone polymerase lacking a proofreading 3'-5'
CC exonuclease which catalyzes the gap-filling reaction during the DNA
CC repair process (By similarity). Specifically binds intermediates in the
CC single-nucleotide base-excision repair process (By similarity). Also
CC catalyzes DNA polymerization with low nucleotide-insertion fidelity (By
CC similarity). Probably acts as a strategic DNA mutase, which gives rise
CC to a rapid emergence of variants (By similarity). Generates mismatched
CC G-G pairs, in that case, the polymerase first binds the deoxynucleotide
CC followed by mismatch formation (By similarity). Together with the viral
CC DNA ligase, fills the single nucleotide gaps generated by the AP
CC endonuclease (Probable). Binds DNA with high affinity via the helix
CC alphaE (By similarity). {ECO:0000250|UniProtKB:P42494, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000250|UniProtKB:P42494};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P42494};
CC Note=In the presence of magnesium, pol X shows a strong preference for
CC the ssDNA gaps having one and two nucleotides.;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P42494}. Note=Found
CC in association with viral nucleoid. {ECO:0000250|UniProtKB:P42494}.
CC -!- DOMAIN: Small DNA polymerase formed from only a palm and a C-terminal
CC subdomain (By similarity). The total DNA-binding site of pol X is
CC composed of two DNA-binding subsites (By similarity).
CC {ECO:0000250|UniProtKB:P42494}.
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR BMRB; P0C984; -.
DR SMR; P0C984; -.
DR Proteomes; UP000000860; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276; PTHR11276; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 3: Inferred from homology;
KW Disulfide bond; DNA damage; DNA repair; DNA-binding;
KW DNA-directed DNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transferase; Virion.
FT CHAIN 1..174
FT /note="Repair DNA polymerase X"
FT /id="PRO_0000373083"
FT REGION 42..51
FT /note="Involved in ssDNA binding"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P42494"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P42494"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P42494"
FT SITE 115
FT /note="Stabilizes dGTP in a syn confromation to overcome
FT the Watson-Crick base pairing constraint"
FT /evidence="ECO:0000250|UniProtKB:P42494"
FT DISULFID 81..86
FT /evidence="ECO:0000250|UniProtKB:P42494"
SQ SEQUENCE 174 AA; 20330 MW; ADFD3D0994AA2461 CRC64;
MLTLIQGKKI VNYLRSRLAF EYNGQLIKIL SKNIVAVGSL RREEKMLNDV DLLIIVPEKK
CLKHVLPNIR IKGLSFSVKV CGERKCVLFI EWEKKTYQLD LFTALAEEKP YAIFHFTGPV
SYLIRIRAAL KKKNYKLNQY GLFKNQTLVP LKITTEKELI KELGFTYRIP KKRL
