APE_ASFB7
ID APE_ASFB7 Reviewed; 296 AA.
AC Q65202;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Probable AP endonuclease {ECO:0000303|PubMed:16503634};
DE Short=APE;
DE EC=3.1.21.- {ECO:0000269|PubMed:16503634, ECO:0000269|PubMed:16641276};
DE AltName: Full=pE296R {ECO:0000303|PubMed:16641276};
GN OrderedLocusNames=Ba71V-134; ORFNames=E296R;
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 [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 [2]
RP SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION PHENOTYPE.
RX PubMed=16641276; DOI=10.1128/jvi.80.10.4847-4857.2006;
RA Redrejo-Rodriguez M., Garcia-Escudero R., Yanez-Munoz R.J., Salas M.L.,
RA Salas J.;
RT "African swine fever virus protein pE296R is a DNA repair
RT apurinic/apyrimidinic endonuclease required for virus growth in swine
RT macrophages.";
RL J. Virol. 80:4847-4857(2006).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16503634; DOI=10.1021/bi051772g;
RA Lamarche B.J., Tsai M.-D.;
RT "Contributions of an endonuclease IV homologue to DNA repair in the African
RT swine fever virus.";
RL Biochemistry 45:2790-2803(2006).
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]
RP INDUCTION.
RX PubMed=32075923; DOI=10.1128/jvi.00119-20;
RA Cackett G., Matelska D., Sykora M., Portugal R., Malecki M., Baehler J.,
RA Dixon L., Werner F.;
RT "The African Swine Fever Virus Transcriptome.";
RL J. Virol. 94:0-0(2020).
CC -!- FUNCTION: Endonuclease of the viral base excision repair system that
CC catalyzes DNA cleavage reaction at the apurinic or apyrimidinic sites
CC (AP sites) (PubMed:16503634, PubMed:16641276). Cleaves phosphodiester
CC bonds on the 5' side of AP sites (PubMed:16503634). In addition to
CC endonuclease activity, the AP endonuclease has a proofreading 3'-5'
CC exonuclease activity that is considerably more efficient in the
CC elimination of a mismatch than in that of a correctly paired base
CC (PubMed:16641276). Displays 3'-phosphatase and 3'-repair diesterase
CC activities (PubMed:16503634). The single nucleotide gaps generated by
CC the AP endonuclease are filled by the viral repair DNA polymerase X and
CC the DNA ligase (Probable). {ECO:0000269|PubMed:16503634,
CC ECO:0000269|PubMed:16641276, ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 3 Zn(2+) ions. {ECO:0000250|UniProtKB:P0C9C6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53 nM for dsDNA containing uracil {ECO:0000269|PubMed:16641276};
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16641276}. Host
CC cytoplasm {ECO:0000269|PubMed:16641276}. Virion
CC {ECO:0000269|PubMed:30185597}. Note=The early enzyme is localized in
CC the nucleus and the cytoplasm, while the late protein is found only in
CC the cytoplasm (PubMed:16641276). Found in association with viral
CC nucleoid (PubMed:30185597). {ECO:0000269|PubMed:16641276,
CC ECO:0000269|PubMed:30185597}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle
CC and accumulates at later times. {ECO:0000269|PubMed:32075923}.
CC -!- DISRUPTION PHENOTYPE: Decreases the growth rate of the virus to 2-4% of
CC the parental virus in swine macrophages. {ECO:0000269|PubMed:16641276}.
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 AP endonuclease 2 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00763}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18466; AAA65362.1; -; Genomic_DNA.
DR RefSeq; NP_042826.1; NC_001659.2.
DR SMR; Q65202; -.
DR GeneID; 22220362; -.
DR KEGG; vg:22220362; -.
DR Proteomes; UP000000624; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0046787; P:viral DNA repair; IDA:UniProtKB.
DR CDD; cd00019; AP2Ec; 1.
DR InterPro; IPR001719; AP_endonuc_2.
DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR InterPro; IPR036237; Xyl_isomerase-like_sf.
DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl.
DR PANTHER; PTHR21445; PTHR21445; 1.
DR Pfam; PF01261; AP_endonuc_2; 1.
DR SMART; SM00518; AP2Ec; 1.
DR SUPFAM; SSF51658; SSF51658; 1.
DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; DNA damage; DNA repair; Early protein; Endonuclease;
KW Exonuclease; Host cytoplasm; Host nucleus; Hydrolase; Late protein;
KW Metal-binding; Nuclease; Reference proteome; Virion; Zinc.
FT CHAIN 1..296
FT /note="Probable AP endonuclease"
FT /id="PRO_0000373138"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C9C6"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0C9C6"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0C9C6"
FT DISULFID 16..20
FT /evidence="ECO:0000250|UniProtKB:P0C9C6"
SQ SEQUENCE 296 AA; 33482 MW; BFDF4E258ED89AB2 CRC64;
MFGAFVSHRL WSDSGCTTTC ITNSIANYVA FGEQIGFPFK SAQVFIAGPR KAVINIQEDD
KVELLKMIVK HNLWVVAHGT YLDVPWSRRS AFVTHFIQQE LLICKEVGIK GLVLHLGAVE
PELIVEGLKK IKPVEGVVIY LETPHNKHHT YKYSTMEQIK ELFLRIRNTR LKQIGLCIDT
AHIWSSGVNI SSYNDAGQWL RSLENIHSVI PPSHIMFHLN DAATECGSGI DRHASLFEGM
IWKSYSHKIK KSGLYCFVEY ITRHQCPAIL ERNLGSSMQL QTALTAEFTT LKSLLK
