APE_ASFM2
ID APE_ASFM2 Reviewed; 296 AA.
AC Q65246;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 85.
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=Mal-142; ORFNames=k4R, k5R;
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 [GENOMIC DNA].
RX PubMed=8021596; DOI=10.1099/0022-1317-75-7-1655;
RA Dixon L.K., Twigg S.R.F., Baylis S.A., Vydelingum S., Bristow C.,
RA Hammond J.M., Smith G.L.;
RT "Nucleotide sequence of a 55 kbp region from the right end of the genome of
RT a pathogenic African swine fever virus isolate (Malawi LIL20/1).";
RL J. Gen. Virol. 75:1655-1684(1994).
RN [2]
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 -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00763}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50842.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X71982; CAA50842.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY261361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; Q65246; -.
DR Proteomes; UP000000860; 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_0000373140"
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; 33507 MW; 26915D85CCD738CF CRC64;
MFGAFVSHRL WSDSGCTTTC ITNSIANYVA FGEQIGFPFK SAQVFIAGPR KAVINIQKDD
KVELLKMIDK HNLWVVAHGT YLDVPWSRRS AFVTHFIQQE LLICKEVGIK GLVLHLGAVE
PELIVEGLKK IKPVEGVIIY LETPHNKHHT YKYSTIEQIK ELFLRIRNTG LKQIGLCIDT
AHIWSSGVNI SSYNSARQWL RSLEDIHSVI PPSHIMFHLN DAATKCGSGV DRHASLFEGM
IWKSYSHKIK HSGLYCFVEY ITRHQCPAIL ERNLGSSMQL QTALTAEFNT LKSFLK
