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Description:
DNA-3-methyladenine glycosylase 1 (EC 3.2.2.21) (3-methyladenine DNAglycosidase 1) (3MEA DNA glycosylase 1).
Molecular weight: 26381
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
recombinational repair( GO:0000725 ) DNA repair( GO:0006281 ) base-excision repair( GO:0006284 ) base-excision repair, AP site formation( GO:0006285 )
Important dates:
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
07-MAR-2006, entry version 40.
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 MAG1_SCHPO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U76637 | AAC49524.1 | - |
| EMBL | AL590582 | CAC36900.1 | - |
| PIR | JC5177 | JC5177. | |
| GeneDB_Spombe | SPAPB24D3.04c | -.1 | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-001624-MONOMER | -.1 | |
| GO | GO:0003905 | F:alkylbase DNA N-glycosylase activity | IDA. |
| GO | GO:0003684 | F:damaged DNA binding | IDA. |
| GO | GO:0006285 | P:base-excision repair, AP site formation | IGI. |
| GO | GO:0000725 | P:recombinational repair | IMP. |
| InterPro | IPR000035 | AlbDNA_glycsylse. | |
| InterPro | IPR003265 | Endo_3c. | |
| Pfam | PF00730 | HhH-GPD | 1. |
| SMART | SM00478 | ENDO3c | 1. |
| PROSITE | PS00516 | ALKYLBASE_DNA_GLYCOS | 1. |
Keywords:
Complete proteome; DNA damage; DNA repair; Hydrolase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=97080527; PubMed=8921872; DOI=10.1016/0378-1119(96)00308-3;
RA Memisoglu A., Samson L.;
RT "Cloning and characterization of a cDNA encoding a 3-methyladenine DNA
RT glycosylase from the fission yeast Schizosaccharomyces pombe.";
RL Gene 177:229-235(1996).
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).
Feature:
CHAIN 1 228 DNA-3-methyladenine glycosylase 1.
/FTId=PRO_0000194881.
Comments:
-!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to
excise 3-methyladenine or 7-methyladenine from the damaged DNA
polymer formed by alkylation lesions. Can release ethylated and
propylated bases from DNA in addition to 3-methyladenine.
-!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3-
methyladenine, 3-methylguanine, 7-methylguanine and 7-
methyladenine.
-!- SIMILARITY: Belongs to the alkylbase DNA glycosidase alkA family.
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Sequence length: 228
MTLDIEEKEE IVTSLTKAEI HLSGLDENWK RLVKLVGNYR PNRSMEKKEP YEELIRAVAS
QQLHSKAANA IFNRFKSISN NGQFPTPEEI RDMDFEIMRA CGFSARKIDS LKSIAEATIS
GLIPTKEEAE RLSNEELIER LTQIKGIGRW TVEMLLIFSL NRDDVMPADD LSIRNGYRYL
HRLPKIPTKM YVLKHSEICA PFRTAAAWYL WKTSKLADYT KPVRPKKH