ID   DPOLX_ASFP4             Reviewed;         174 AA.
AC   P0C983;
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};
DE   AltName: Full=AsfvPolX;
GN   OrderedLocusNames=Pret-109;
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: 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; AY261363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0C983; -.
DR   Proteomes; UP000000859; 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_0000373082"
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;  20335 MW;  AAE7D13EDD1AB4BE CRC64;
     MLTLIQGKKI VNDLRSRLAF EYNGQLIKIL SKNIIAVGSL RREEKMLNDV DLLIIVPEKK
     LLKHVLPNIR IKDFSFSVKV CGERKCVLFI EWKKNTYQLD LFTALAEEKP YAVLHFTGPV
     SYLIRIRAAL KKKNYKLNQY GLFKNQTLVP LKITTEKELI KELGFTYRIP KKRL