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Database: UniProt
Entry: A8Z6D9
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ID   END4_CAMC1              Reviewed;         283 AA.
AC   A8Z6D9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   14-MAY-2014, entry version 37.
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=Ccon26_00800; ORFNames=CCC13826_1104;
OS   Campylobacter concisus (strain 13826).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13826;
RA   Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA   Mandrell R.E., On S., Nelson K.E.;
RT   "Genome sequence of Campylobacter concisus 13826 isolated from human
RT   feces.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000792; ABW74720.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8Z6D9; -.
DR   SMR; A8Z6D9; 1-276.
DR   EnsemblBacteria; ABW74720; ABW74720; CCC13826_1104.
DR   OMA; IEQFKAN; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.20.150; -; 1.
DR   HAMAP; MF_00152; Nfo; 1.
DR   InterPro; IPR001719; AP_endonuc_2.
DR   InterPro; IPR018246; AP_endonuc_F2_Zn_BS.
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;
KW   Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase;
KW   Metal-binding; Nuclease; Zinc.
FT   CHAIN         1    283       Probable endonuclease 4.
FT                                /FTId=PRO_1000071526.
FT   METAL        69     69       Zinc 1 (By similarity).
FT   METAL       109    109       Zinc 1 (By similarity).
FT   METAL       145    145       Zinc 1 (By similarity).
FT   METAL       145    145       Zinc 2 (By similarity).
FT   METAL       179    179       Zinc 2 (By similarity).
FT   METAL       182    182       Zinc 3 (By similarity).
FT   METAL       216    216       Zinc 2 (By similarity).
FT   METAL       229    229       Zinc 3 (By similarity).
FT   METAL       231    231       Zinc 3 (By similarity).
FT   METAL       261    261       Zinc 2 (By similarity).
SQ   SEQUENCE   283 AA;  31041 MW;  31D964F50E618BC9 CRC64;
     MRYIGAHVSA AGGVSNAPIN AAKIGANAFA LFTKNQRQWS AKELSEGEIE QFKANLKASG
     ISADHVLPHA SYLINLGHPE KEARAKSLEA FIDEIERASK LGLKLLNFHP GSHLKQISQN
     ECLDNIARCI NEALKRTSGV KLVIENTAAQ GSNLGFDFAQ LAYLIERVDD ESRVGVCIDT
     CHAFAAGYDL RSKEAYAKTM GEFDAVIGYK FLSGMHLNDA KFGLGSKKDR HESLGKGELG
     LGAFENIIND DKIGEIPLIL ETIDESIWED EIKILRNLEK EKL
//
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