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Description:
Exodeoxyribonuclease III (EC 3.1.11.2) (Exonuclease III) (EXO III) (APendonuclease VI).
Molecular weight: 30785
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-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
07-MAR-2006, entry version 7.
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 EX3_SALTI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AL627271 | CAD02052.1 | - |
| EMBL | AE014613 | AAO68838.1 | - |
| HSSP | P09030 | 1AKO | |
| SMR | P0A1B0 | 1-267.1 | |
| GenomeReviews | AL513382_GR | STY1812.1 | |
| GenomeReviews | AE014613_GR | t1181.1 | |
| InterPro | IPR000097 | APendonclse1. | |
| InterPro | IPR005135 | Exo_endo_phos. | |
| InterPro | IPR004808 | ExoIII_xth. | |
| Pfam | PF03372 | Exo_endo_phos | 1. |
| TIGRFAMs | TIGR00195 | exoDNase_III | 1. |
| TIGRFAMs | TIGR00633 | xth | 1. |
| PROSITE | PS00726 | AP_NUCLEASE_F1_1 | 1. |
| PROSITE | PS00727 | AP_NUCLEASE_F1_2 | 1. |
| PROSITE | PS00728 | AP_NUCLEASE_F1_3 | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; Exonuclease; Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nuclease.
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 1 268 Exodeoxyribonuclease III.
/FTId=PRO_0000200023.
ACT_SITE 259 259 Proton acceptor (By similarity).
METAL 34 34 Magnesium or manganese (By similarity).
SITE 153 153 Important for substrate recognition (By
similarity).
Comments:
-!- FUNCTION: Major apurinic-apyrimidinic endonuclease of E.coli. It
removes the damaged DNA at cytosines and guanines by cleaving on
the 3' side of the AP site by a beta-elimination reaction. It
exhibits 3'-5'-exonuclease, 3'-phosphomonoesterase, 3'-repair
diesterase and ribonuclease H activities (By similarity).
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
direction to yield nucleoside 5'-phosphates.
-!- SUBUNIT: Monomer (By similarity).
-!- SIMILARITY: Belongs to the DNA repair enzymes AP/exoA family.
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Sequence length: 268
MKFVSFNING LRARPHQLEA IVEKHQPDVI GLQETKVHDE MFPLEEVAKL GYNVFYHGQK
GHYGVALLTK ATPISVRRGF PDDGEEAQRR IIMAEIPSPL GNITVINGYF PQGESRDHPL
KFPAKAQFYQ NLQNYLETEL KCDNPVLIMG DMNISPTDLD IGIGEENRKR WLRTGKCSFL
PEEREWMSRL LKWGLVDTFR QANPQTMDKF SWFDYRSKGF VDNRGLRIDL LLASAPLAER
CAETGIDYDI RSMEKPSDHA PVWATFRV