APE_ASFK5
ID APE_ASFK5 Reviewed; 296 AA.
AC P0C9C8;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Probable AP endonuclease;
DE Short=APE {ECO:0000250|UniProtKB:Q65202};
DE EC=3.1.21.-;
DE AltName: Full=pE296R {ECO:0000250|UniProtKB:Q65202};
GN OrderedLocusNames=Ken-146;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
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 of the viral base excision repair system that
CC catalyzes DNA cleavage reaction at the apurinic or apyrimidinic sites
CC (AP sites) (By similarity). Cleaves phosphodiester bonds on the 5' side
CC of AP sites (By similarity). In addition to endonuclease activity, the
CC AP endonuclease 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 repair DNA polymerase X and the 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 -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00763}.
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DR EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; P0C9C8; -.
DR Proteomes; UP000000861; 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_0000373142"
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; 33460 MW; D273A07866F2BEC9 CRC64;
MFGAFVSHRL WSDSGCTTTC IANSIANYVA FGEQIEFPFK SAQVFIAGPR KAVINIQEED
KAELSKMIAK HNLWVVAHGT YLDVPWSSRS AFVTHFIHQE LLICKEVGIK GLVLHLGAVE
PELIVEGLKK IKPVEEVVIY LETPHNKHHA YKYSTIEQIK ELFLRIRNSR LKHIGLCIDT
AHIWSSGVNI SGYNDAGQWL RSLENIHSVI PPSHIMFHLN DAATECGSGI DRHASLFEGM
IWKSYSHKIK HSGLYCFVEY ITRHQCPAIL ERNLGSSMQL QTALTTEFHT LKSLLK
