END4_MIMIV
ID END4_MIMIV Reviewed; 312 AA.
AC Q5UPY4;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Putative endonuclease 4;
DE EC=3.1.21.2;
DE AltName: Full=Endodeoxyribonuclease IV;
DE AltName: Full=Endonuclease IV;
GN OrderedLocusNames=MIMI_R296;
OS Acanthamoeba polyphaga mimivirus (APMV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Imitervirales; Mimiviridae; Mimivirus.
OX NCBI_TaxID=212035;
OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rowbotham-Bradford;
RX PubMed=15486256; DOI=10.1126/science.1101485;
RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H.,
RA La Scola B., Susan M., Claverie J.-M.;
RT "The 1.2-megabase genome sequence of Mimivirus.";
RL Science 306:1344-1350(2004).
CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to
CC produce new 5'-ends that are base-free deoxyribose 5-phosphate residues
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC products.; EC=3.1.21.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00763};
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:0000255|PROSITE-ProRule:PRU00763};
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00763}.
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DR EMBL; AY653733; AAV50568.1; -; Genomic_DNA.
DR RefSeq; YP_003986798.1; NC_014649.1.
DR SMR; Q5UPY4; -.
DR GeneID; 9924911; -.
DR KEGG; vg:9924911; -.
DR Proteomes; UP000001134; Genome.
DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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 TIGRFAMs; TIGR00587; nfo; 1.
DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1.
DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW Reference proteome; Zinc.
FT CHAIN 1..312
FT /note="Putative endonuclease 4"
FT /id="PRO_0000190896"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 254
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00763"
SQ SEQUENCE 312 AA; 34857 MW; 71ECF69CBE7E6358 CRC64;
MQSNINICTL SIFIIESMTT RIGRHINISK GFVSAPEYAK NIGCSVFQIF LGAPQQILSK
ARQKDELIEF GKQLIKHDLI MVVHGSYTIN LCHPPGSKKF ETSIKSLVKD LNATNLIGDR
CLGVIIHMGK NISENKLTVD QAIDNYVTGI KTALSQTPDN TTIVLETGAS QGSEVASHID
GLAQIYWCLN DAERERVYFC IDTCHIWATG YDISSPTGVK KFFKEFDKKI GVEKISCIHF
NDSKTGLESK VDRHADLCYG EIGSNGLKAI AKFAKEYKIH LIMETPLDAI NPETNQEISY
NEEYNKVKSW LK
