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Description:
Endonuclease III homolog (EC 4.2.99.18) (DNA-(apurinic or apyrimidinicsite) lyase).
Molecular weight: 40227
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 ) base-excision repair( GO:0006284 ) base-excision repair, AP site formation( GO:0006285 ) nucleotide-excision repair (and GO:0045001, a synonym)( GO:0006289 )
Important dates:
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
07-MAR-2006, entry version 44.
Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.
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 END3_SCHPO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AB191154 | BAD93307.1 | - |
| EMBL | Z67961 | CAA91893.1 | - |
| PIR | JC6066 | S62565. | |
| GeneDB_Spombe | SPAC30D11.07 | -.1 | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-000904-MONOMER | -.1 | |
| GO | GO:0005634 | C:nucleus | IDA. |
| GO | GO:0008534 | F:purine-specific oxidized base lesion DNA N-... | IMP. |
| GO | GO:0000703 | F:pyrimidine-specific oxidized base lesion DN... | IMP. |
| GO | GO:0006285 | P:base-excision repair, AP site formation | IMP. |
| GO | GO:0006289 | P:nucleotide-excision repair | IMP. |
| InterPro | IPR003265 | Endo_3c. | |
| InterPro | IPR004035 | EndoIII_FCL. | |
| InterPro | IPR004036 | EndoIII_HhH. | |
| InterPro | IPR000445 | HhH. | |
| Pfam | PF00633 | HHH | 1. |
| Pfam | PF00730 | HhH-GPD | 1. |
| SMART | SM00478 | ENDO3c | 1. |
| PROSITE | PS00764 | ENDONUCLEASE_III_1 | FALSE_NEG. |
| PROSITE | PS01155 | ENDONUCLEASE_III_2 | 1. |
Keywords:
4Fe-4S; Complete proteome; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sugimoto T., Ikeda S.;
RT "Isolation and characterization of the Schizosaccharomyces pombe cDNA
RT encoding the endonuclease III homologue, nth1.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP CHARACTERIZATION.
RX MEDLINE=96406995; PubMed=8811082; DOI=10.1093/nar/24.17.3307;
RA Roldan-Arjona T., Anselmino C., Lindahl T.;
RT "Molecular cloning and functional analysis of a Schizosaccharomyces
RT pombe homologue of Escherichia coli endonuclease III.";
RL Nucleic Acids Res. 24:3307-3312(1996).
Feature:
CHAIN 1 355 Endonuclease III homolog.
/FTId=PRO_0000102226.
METAL 210 210 Iron-sulfur (4Fe-4S) (By similarity).
METAL 217 217 Iron-sulfur (4Fe-4S) (By similarity).
METAL 220 220 Iron-sulfur (4Fe-4S) (By similarity).
METAL 228 228 Iron-sulfur (4Fe-4S) (By similarity).
Comments:
-!- FUNCTION: Has both an apurinic and/or apyrimidinic endonuclease
activity and a DNA N-glycosylase activity. Possesses glycosylase
activity on different types of DNA substrates with pyrimidines
damage. It can release both urea and thymine glycol from double-
stranded polymers.
-!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
apyrimidinic site in DNA is broken by a beta-elimination reaction,
leaving a 3'-terminal unsaturated sugar and a product with a
terminal 5'-phosphate.
-!- COFACTOR: Binds 1 4Fe-4S cluster which is not important for the
catalytic activity, but which is probably involved in the proper
positioning of the enzyme along the DNA strand (By similarity).
-!- SIMILARITY: Belongs to the nth/mutY family.
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Sequence length: 355
MSKDYGTPPE NWREVYDEIC KMKAKVVAPV DVQGCHTLGE RNDPKKFRFQ TLVALMLSSQ
TKDIVLGPTM RNLKEKLAGG LCLEDIQNID EVSLNKLIEK VGFHNRKTIY LKQMARILSE
KFQGDIPDTV EDLMTLPGVG PKMGYLCMSI AWNKTVGIGV DVHVHRICNL LHWCNTKTEE
QTRAALQSWL PKELWFELNH TLVGFGQTIC LPRGRRCDMC TLSSKGLCPS AFKEKSGITI
TKRKVKTIKR VKKRPASESP PLSPLSLPTD DLYYQSIEDK SLIKLEDLDP VDSISHMNEP
LKKEPAADID VDQKPPVAFH STTKETRSLR RSKRVAKKSS QYFSQQSLQD IEDLV