ID END4_CHLCV Reviewed; 289 AA.
AC Q824X6;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 68.
DE RecName: Full=Probable endonuclease 4;
DE EC=3.1.21.2;
DE AltName: Full=Endodeoxyribonuclease IV;
DE AltName: Full=Endonuclease IV;
GN Name=nfo; OrderedLocusNames=CCA_00012;
OS Chlamydophila caviae (strain GPIC).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydophila.
OX NCBI_TaxID=227941;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GPIC;
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B.,
RA Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J.,
RA White O., Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G.,
RA Bavoil P.M., Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
CC phosphodiester bonds at apurinic or apyrimidinic sites (AP sites)
CC to produce new 5'-ends that are base-free deoxyribose 5-phosphate
CC residues. It preferentially attacks modified AP sites created by
CC bleomycin and neocarzinostatin (By similarity).
CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC phosphooligonucleotide end-products.
CC -!- COFACTOR: Binds 3 zinc ions (By similarity).
CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family.
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DR EMBL; AE015925; AAP04765.1; -; Genomic_DNA.
DR RefSeq; NP_828887.1; NC_003361.3.
DR ProteinModelPortal; Q824X6; -.
DR STRING; 227941.CCA00012; -.
DR EnsemblBacteria; AAP04765; AAP04765; CCA_00012.
DR GeneID; 1217761; -.
DR KEGG; cca:CCA00012; -.
DR PATRIC; 20269002; VBIChlCav107360_0012.
DR eggNOG; COG0648; -.
DR KO; K01151; -.
DR OMA; INLGHPD; -.
DR ProtClustDB; PRK01060; -.
DR BioCyc; CCAV227941:GH8L-19-MONOMER; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:HAMAP.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:HAMAP.
DR GO; GO:0006281; P:DNA repair; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR Gene3D; 3.20.20.150; -; 1.
DR HAMAP; MF_00152; Nfo; 1; -.
DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
DR InterPro; IPR001719; Endodeoxyribonuclease_IV.
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; Xyl_isomerase-like_TIM-brl; 1.
DR TIGRFAMs; TIGR00587; nfo; 1.
DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1.
DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1.
DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1.
DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE 3: Inferred from homology;
KW Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase;
KW Metal-binding; Nuclease; Zinc.
FT CHAIN 1 289 Probable endonuclease 4.
FT /FTId=PRO_0000190831.
FT METAL 75 75 Zinc 1 (By similarity).
FT METAL 115 115 Zinc 1 (By similarity).
FT METAL 153 153 Zinc 1 (By similarity).
FT METAL 153 153 Zinc 2 (By similarity).
FT METAL 187 187 Zinc 2 (By similarity).
FT METAL 190 190 Zinc 3 (By similarity).
FT METAL 224 224 Zinc 2 (By similarity).
FT METAL 237 237 Zinc 3 (By similarity).
FT METAL 239 239 Zinc 3 (By similarity).
FT METAL 269 269 Zinc 2 (By similarity).
SQ SEQUENCE 289 AA; 32271 MW; 73C87816E94FE364 CRC64;
MQVFPPPQVP LLGAHTSTAG GLHNAIYEGQ EIGASTIQMF TANQRQWRRR PLTDSLINSF
KTALKETSLS YIMSHAGYLI NPGSPNPEIL EKSRICIQQE IQDCISLGIN FVNFHPGAAV
NDTKETCLDR IISSFSLMEP LFENSPPLVV LFETTAGQGT LVGSNFEELS YLIDNLNHKI
PVGVCIDTCH IFAAGYDITS PESWKRVLKN FDDVIGLSYL RAFHLNDSMF PLGQHKDRHA
PLGEGDIGIE SFKFLMTNED TRMIPKYLET PGGPDLWAKE IRQLQSFQK
//
