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END4_MYCMS
ID   END4_MYCMS              Reviewed;         289 AA.
AC   Q6MUC7;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable endonuclease 4 {ECO:0000255|HAMAP-Rule:MF_00152};
DE            EC=3.1.21.2 {ECO:0000255|HAMAP-Rule:MF_00152};
DE   AltName: Full=Endodeoxyribonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
DE   AltName: Full=Endonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152};
GN   Name=nfo {ECO:0000255|HAMAP-Rule:MF_00152}; OrderedLocusNames=MSC_0105;
OS   Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT   PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL   Genome Res. 14:221-227(2004).
CC   -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC       phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating
CC       a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00152}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end-
CC         products.; EC=3.1.21.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00152};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00152};
CC       Note=Binds 3 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_00152};
CC   -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00152}.
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DR   EMBL; BX293980; CAE76757.1; -; Genomic_DNA.
DR   RefSeq; NP_975115.1; NC_005364.2.
DR   AlphaFoldDB; Q6MUC7; -.
DR   SMR; Q6MUC7; -.
DR   STRING; 272632.MSC_0105; -.
DR   EnsemblBacteria; CAE76757; CAE76757; MSC_0105.
DR   KEGG; mmy:MSC_0105; -.
DR   PATRIC; fig|272632.4.peg.109; -.
DR   eggNOG; COG0648; Bacteria.
DR   HOGENOM; CLU_025885_4_1_14; -.
DR   OMA; NPRGWAT; -.
DR   Proteomes; UP000001016; Chromosome.
DR   GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd00019; AP2Ec; 1.
DR   HAMAP; MF_00152; Nfo; 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; PS00729; AP_NUCLEASE_F2_1; 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..289
FT                   /note="Probable endonuclease 4"
FT                   /id="PRO_0000190856"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         150
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         187
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         218
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   BINDING         263
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
SQ   SEQUENCE   289 AA;  33160 MW;  163ABD20F017ECA5 CRC64;
     MDKILLGCHV SMNKQNNYLV GSVNEAISYK ANTFMIFTGP PQSTLRTNTN HLYINQMHEL
     MNSYKIDAKD LVVHAPYIIN IANSVDQNKW KFTVDFLIQE IKRCEEIKIP TLVLHPGSYT
     TGNYKDSLNQ IIKALNIVSN YQVNVKIALE TMSGKGTEVC SRLEDFKYIL DNVKNKDKVG
     VCLDTCHLHD AGYDLSKWTE FKEQMKQNFS LDKVLCIHLN DSKNMISSHK DRHANIGYGY
     VGFDTLVNVV FDKDFSNISK ILETPYIDKT PPYKIEIEDL LNKTFTNRL
 
 
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