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Description:
Endonuclease IV (EC 3.1.21.2) (Endodeoxyribonuclease IV).
Molecular weight: 31480
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:
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 1.
07-MAR-2006, entry version 12.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
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_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M22591 | AAA24216.1 | - |
| EMBL | U00007 | AAA60529.1 | - |
| EMBL | U00096 | AAC75220.1 | - |
| PIR | F64984 | NDEC4. | |
| PDB | 1QTW | X-ray | A=1-285. |
| PDB | 1QUM | X-ray | A=1-285. |
| GenomeReviews | U00096_GR | b2159.1 | |
| EchoBASE | EB0645 | -.1 | |
| EcoGene | EG10651 | nfo. | |
| GO | GO:0005515 | F:protein binding | IPI. |
| HAMAP | MF_00152 | - | 1. |
| InterPro | IPR001719 | AP_endnuclease2. | |
| Pfam | PF01261 | AP_endonuc_2 | 1. |
| SMART | SM00518 | AP2Ec | 1. |
| TIGRFAMs | TIGR00587 | nfo | 1. |
| PROSITE | PS00729 | AP_NUCLEASE_F2_1 | 1. |
| PROSITE | PS00730 | AP_NUCLEASE_F2_2 | 1. |
| PROSITE | PS00731 | AP_NUCLEASE_F2_3 | 1. |
Keywords:
3D-structure; Complete proteome; DNA damage; DNA repair; Endonuclease; Hydrolase; Manganese; Metal-binding; Nuclease; Zinc.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX MEDLINE=89033896; PubMed=2460435;
RA Saporito S.M., Cunningham R.P.;
RT "Nucleotide sequence of the nfo gene of Escherichia coli K-12.";
RL J. Bacteriol. 170:5141-5145(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP METAL-BINDING STUDIES.
RX MEDLINE=92078146; PubMed=1720775;
RA Levin J.D., Shapiro R., Demple B.;
RT "Metalloenzymes in DNA repair. Escherichia coli endonuclease IV and
RT Saccharomyces cerevisiae Apn1.";
RL J. Biol. Chem. 266:22893-22898(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.02 ANGSTROMS).
RX MEDLINE=99385796; PubMed=10458614; DOI=10.1016/S0092-8674(00)81968-6;
RA Hosfield D.J., Guan Y., Haas B.J., Cunningham R.P., Tainer J.A.;
RT "Structure of the DNA repair enzyme endonuclease IV and its DNA
RT complex: double-nucleotide flipping at abasic sites and three-metal-
RT ion catalysis.";
RL Cell 98:397-408(1999).
Feature:
CHAIN 1 285 Endonuclease IV.
/FTId=PRO_0000190838.
METAL 69 69 Zinc 1.
METAL 109 109 Zinc 1.
METAL 145 145 Zinc 1.
METAL 145 145 Zinc 2.
METAL 179 179 Zinc 2.
METAL 182 182 Zinc 3.
METAL 216 216 Zinc 2.
METAL 229 229 Zinc 3.
METAL 231 231 Zinc 3.
METAL 261 261 Zinc 2.
CONFLICT 10 10 A -> R (in Ref. 1).
CONFLICT 273 273 A -> T (in Ref. 2).
STRAND 3 7
TURN 11 12
HELIX 14 23
TURN 24 25
STRAND 28 30
HELIX 46 58
TURN 59 60
HELIX 63 65
STRAND 66 66
STRAND 69 69
TURN 72 73
TURN 76 77
HELIX 81 100
TURN 101 102
STRAND 105 108
STRAND 112 112
TURN 114 116
HELIX 119 136
STRAND 141 145
TURN 151 152
STRAND 153 153
HELIX 158 167
HELIX 171 173
STRAND 174 179
HELIX 180 186
TURN 187 187
HELIX 193 206
TURN 207 207
HELIX 209 211
STRAND 212 217
STRAND 219 220
TURN 224 225
STRAND 231 232
TURN 234 236
HELIX 242 248
TURN 249 249
HELIX 251 253
TURN 254 255
STRAND 257 260
HELIX 265 267
HELIX 268 278
TURN 279 280
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.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphooligonucleotide end-products.
-!- COFACTOR: Binds 3 zinc ions. Can also bind manganese.
-!- SUBUNIT: Monomer.
-!- INTERACTION:
P06959:aceF; NbExp=1; IntAct=EBI-555164, EBI-542707;
P33371:dusC; NbExp=1; IntAct=EBI-555164, EBI-562765;
P08177:lon; NbExp=1; IntAct=EBI-555164, EBI-547203;
P00391:lpdA; NbExp=1; IntAct=EBI-555164, EBI-542856;
P00490:malP; NbExp=1; IntAct=EBI-555164, EBI-551914;
P10408:secA; NbExp=1; IntAct=EBI-555164, EBI-543213;
-!- INDUCTION: Endonuclease IV is induced by agents which generate
superoxide radical anions.
-!- SIMILARITY: Belongs to the AP endonuclease 2 family.
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Sequence length: 285
MKYIGAHVSA AGGLANAAIR AAEIDATAFA LFTKNQRQWR AAPLTTQTID EFKAACEKYH
YTSAQILPHD SYLINLGHPV TEALEKSRDA FIDEMQRCEQ LGLSLLNFHP GSHLMQISEE
DCLARIAESI NIALDKTQGV TAVIENTAGQ GSNLGFKFEH LAAIIDGVED KSRVGVCIDT
CHAFAAGYDL RTPAECEKTF ADFARTVGFK YLRGMHLNDA KSTFGSRVDR HHSLGEGNIG
HDAFRWIMQD DRFDGIPLIL ETINPDIWAE EIAWLKAQQT EKAVA