ID   END3_RICFE              Reviewed;         213 AA.
AC   Q4UK93;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Endonuclease III;
DE            EC=4.2.99.18;
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase;
GN   Name=nth; OrderedLocusNames=RF_1191;
OS   Rickettsia felis (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=42862;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
CC   -!- FUNCTION: Has both an apurinic and/or apyrimidinic endonuclease
CC       activity and a DNA N-glycosylase activity. Incises damaged DNA at
CC       cytosines, thymines and guanines. Acts on a damaged strand, 5'
CC       from the damaged site (By similarity).
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster. The cluster is not important for
CC       the catalytic activity, but which is probably involved in the
CC       proper positioning of the enzyme along the DNA strand (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the nth/mutY family.
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DR   EMBL; CP000053; AAY62042.1; -; Genomic_DNA.
DR   RefSeq; YP_247207.1; -.
DR   GeneID; 3401489; -.
DR   GenomeReviews; CP000053_GR; RF_1191.
DR   KEGG; rfe:RF_1191; -.
DR   NMPDR; fig|315456.3.peg.1191; -.
DR   HOGENOM; Q4UK93; -.
DR   OMA; Q4UK93; EPTIAVD.
DR   BioCyc; RFEL315456:RF_1191-MON; -.
DR   BRENDA; 4.2.99.18; 297363.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase a...; IEA:EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   InterPro; IPR004036; Endonuclease-III_CS2.
DR   InterPro; IPR005759; Endonuclease-III_Nth.
DR   InterPro; IPR004035; Endouclease-III_FeS-bd_CS1.
DR   InterPro; IPR003651; Endouclease3-like_FeS-loop.
DR   InterPro; IPR003583; Helix-hairpin-helix_DNA-bd.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   InterPro; IPR000445; HhH_motif.
DR   Pfam; PF10576; EndIII_4Fe-2S; 1.
DR   Pfam; PF00633; HHH; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SMART; SM00525; FES; 1.
DR   SMART; SM00278; HhH1; 1.
DR   TIGRFAMs; TIGR01083; nth; 1.
DR   PROSITE; PS00764; ENDONUCLEASE_III_1; FALSE_NEG.
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase;
KW   Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN         1    213       Endonuclease III.
FT                                /FTId=PRO_0000280932.
FT   METAL       187    187       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       194    194       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       197    197       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       203    203       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   213 AA;  24134 MW;  A949EE1DCC334D0F CRC64;
     MQAQIVNKIF EIFSKNNPSP KTELIYKNDF TLLVAVMLSA QATDISVNLA TKSLFETYDT
     TEKILELGED GLKKYIKSIG LFNSKAKNII ALCKILISNY QSSVPNDFKE LIKLPGVGRK
     TANVVLNCLF GMPTMAVDTH VFRVAKRIGL ARGNSPEIVE KELLQIINEK WLTHAHHWLI
     LHGRYICKAR KPDCDICPIK EYCEYYNSPI ISK
//