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Protein data for END4_SALTI:

Description:
Probable endonuclease IV (EC 3.1.21.2) (Endodeoxyribonuclease IV).

Molecular weight: 31210

View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):

DNA repair( GO:0006281 )


Important dates:
01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
07-MAR-2006, entry version 32.

Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Salmonella.

To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html

Links to references in other databases for protein END4_SALTI:

DatabasePointerAdd. info#1Add. info#2
EMBLAL627273CAD02585.1-
EMBLAE014613AAO68353.1-
HSSPP126381QUM
SMRQ8Z5931-285.1
GenomeReviewsAL513382_GRSTY2438.1
GenomeReviewsAE014613_GRt0652.1
BioCycSENT209261:T0652-MONOMER-.1
BioCycSENT90370:STY2438-MONOMER-.1
HAMAPMF_00152-1.
InterProIPR001719AP_endnuclease2.
InterProIPR012307Xylisom_TIMbarrl.
PfamPF01261AP_endonuc_21.
SMARTSM00518AP2Ec1.
TIGRFAMsTIGR00587nfo1.
PROSITEPS00729AP_NUCLEASE_F2_11.
PROSITEPS00730AP_NUCLEASE_F2_21.
PROSITEPS00731AP_NUCLEASE_F2_31.

General information about the databases mentioned above

Keywords:
Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease; Zinc.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX MEDLINE=21534947; PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA Whitehead S., Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella
RT enterica serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ty2 / ATCC 700931;
RX MEDLINE=22531367; PubMed=12644504;
RX DOI=10.1128/JB.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT and CT18.";
RL J. Bacteriol. 185:2330-2337(2003).

Feature:
CHAIN 1 285 Probable endonuclease IV.
/FTId=PRO_0000190866.
METAL 69 69 Zinc 1 (By similarity).
METAL 109 109 Zinc 1 (By similarity).
METAL 145 145 Zinc 1 (By similarity).
METAL 145 145 Zinc 2 (By similarity).
METAL 179 179 Zinc 2 (By similarity).
METAL 182 182 Zinc 3 (By similarity).
METAL 216 216 Zinc 2 (By similarity).
METAL 229 229 Zinc 3 (By similarity).
METAL 231 231 Zinc 3 (By similarity).
METAL 261 261 Zinc 2 (By similarity).

Comments:
-!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves
phosphodiester bonds at apurinic or apyrimidinic sites (AP sites)
to produce new 5' ends that are base-free deoxyribose 5-phosphate
residues. It preferentially attacks modified AP sites created by
bleomycin and neocarzinostatin (By similarity).
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphooligonucleotide end-products.
-!- COFACTOR: Binds 3 zinc ions (By similarity).
-!- SIMILARITY: Belongs to the AP endonuclease 2 family.
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Sequence length: 285

     MKYIGAHVSA AGGLANAPAR AAEIGATAFA LFTKNQRQWR AAPLTPQVID DFKIACEKYH
     FSAAQILPHD SYLINLGHPV SEALEKSRDA FLDEMQRCEQ LGLTLLNFHP GSHLMQIAQE
     DCLARIAESI NIALAQTEGV TAVIENTAGQ GSNLGFEFEQ LAAIIDGVED KSRVGVCIDT
     CHAFAAGYDL RTPEACEKTF AEFGKIVGFQ YLRGMHLNDA KSAFGSRVDR HHSLGEGNIG
     HDAFRWIMQD ARFDGIPLIL ETINPDIWAE EIAWLKAQQI AEAMA

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