APE_ASFWA
ID APE_ASFWA Reviewed; 296 AA.
AC P0C9C7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Probable AP endonuclease {ECO:0000250|UniProtKB:Q65202};
DE Short=APE {ECO:0000250|UniProtKB:Q65202};
DE EC=3.1.21.- {ECO:0000250|UniProtKB:Q65202};
GN OrderedLocusNames=War-144;
OS African swine fever virus (isolate Warthog/Namibia/Wart80/1980) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561444;
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: Endonuclease that plays a role in DNA repair (By similarity).
CC Cleaves phosphodiester bonds on the 5' side of apurinic or apyrimidinic
CC sites (AP sites) (By similarity). In addition to endonuclease activity,
CC the ASFV enzyme has a proofreading 3'-5' exonuclease activity that is
CC considerably more efficient in the elimination of a mismatch than in
CC that of a correctly paired base (By similarity). Displays 3'-
CC phosphatase and 3'-repair diesterase activities (By similarity). The
CC single nucleotide gaps generated by the AP endonuclease are filled by
CC the viral AP endonuclease and DNA ligase (Probable).
CC {ECO:0000250|UniProtKB:Q65202, ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00763};
CC Note=Binds 3 Zn(2+) ions. {ECO:0000250|UniProtKB:P0C9C6};
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:Q65202}. Host
CC cytoplasm {ECO:0000250|UniProtKB:Q65202}. Virion
CC {ECO:0000250|UniProtKB:Q65202}. Note=The early enzyme is localized in
CC the nucleus and the cytoplasm, while the late protein is found only in
CC the cytoplasm (By similarity). Found in association with viral nucleoid
CC (By similarity). {ECO:0000250|UniProtKB:Q65202}.
CC -!- INDUCTION: Expressed in the early phase of the viral replicative cycle
CC and accumulates at later times. {ECO:0000305}.
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:0000250}.
CC -!- MISCELLANEOUS: During infection, the protein is expressed at early
CC times and accumulates at later times. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00763}.
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DR EMBL; AY261366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9C7; -.
DR PRIDE; P0C9C7; -.
DR Proteomes; UP000000858; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Disulfide bond; DNA damage; DNA repair; Early protein; Endonuclease;
KW Exonuclease; Host cytoplasm; Host nucleus; Hydrolase; Metal-binding;
KW Nuclease; Virion; Zinc.
FT CHAIN 1..296
FT /note="Probable AP endonuclease"
FT /id="PRO_0000373141"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
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
