(data stored in SCRATCH zone)

SWISSPROT: END4_CHLAB

ID   END4_CHLAB              Reviewed;         289 AA.
AC   Q5L798;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   11-DEC-2019, entry version 82.
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=CAB012;
OS   Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=218497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27085 / S26/3;
RX   PubMed=15837807; DOI=10.1101/gr.3684805;
RA   Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA   Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA   Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA   Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT   "The Chlamydophila abortus genome sequence reveals an array of variable
RT   proteins that contribute to interspecies variation.";
RL   Genome Res. 15:629-640(2005).
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
CC       residues. It preferentially attacks modified AP sites created by
CC       bleomycin and neocarzinostatin. {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}.
DR   EMBL; CR848038; CAH63470.1; -; Genomic_DNA.
DR   RefSeq; WP_011096765.1; NC_004552.2.
DR   SMR; Q5L798; -.
DR   STRING; 218497.CAB012; -.
DR   PRIDE; Q5L798; -.
DR   EnsemblBacteria; CAH63470; CAH63470; CAB012.
DR   KEGG; cab:CAB012; -.
DR   eggNOG; ENOG4105EFU; Bacteria.
DR   eggNOG; COG0648; LUCA.
DR   HOGENOM; HOG000224893; -.
DR   KO; K01151; -.
DR   OMA; HPGSHLK; -.
DR   OrthoDB; 1088517at2; -.
DR   BioCyc; CABO218497:G1GI1-13-MONOMER; -.
DR   Proteomes; UP000001012; 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; PS00731; AP_NUCLEASE_F2_3; 1.
DR   PROSITE; PS51432; AP_NUCLEASE_F2_4; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5L798.
DR   SWISS-2DPAGE; Q5L798.
KW   DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease;
KW   Zinc.
FT   CHAIN           1..289
FT                   /note="Probable endonuclease 4"
FT                   /id="PRO_1000011297"
FT   METAL           75
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           115
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           153
FT                   /note="Zinc 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           153
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           187
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           190
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           224
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           237
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           239
FT                   /note="Zinc 3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
FT   METAL           269
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00152"
SQ   SEQUENCE   289 AA;  32109 MW;  70197136F4E84644 CRC64;
     MQVFPPPQVP LLGAHTSTSG GLQNAIYEGQ EIGASTVQMF TANQRQWRRR PLTDDLINSF
     KTALEETSLS YIMSHAGYLI NPGAPNPEIL EKSRICIQQE IQDCLSLGIT FVNFHPGAAV
     NDTKEACLDR IVSSFSLVEP LFEDSPPLVV LFETTAGQGT LVGSTFEELG YLIDKLKHKI
     PVGVCIDTCH IFASGYDITS PGSWKQVLKN FDDAIGLSYL RAFHLNDSMF PLGKHKDRHA
     PLGEGDIGME SFKFLMTDEL TRMIPKYLET PGGPDLWTKE IRQLKSFQK
//

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