Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q92383 (MAG1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-3-methyladenine glycosylase 1

EC=3.2.2.21
Alternative name(s):
3-methyladenine DNA glycosidase 1
3MEA DNA glycosylase 1
Gene names
Name:mag1
ORF Names:SPAPB24D3.04c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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.

Sequence similarities

Belongs to the alkylbase DNA glycosidase AlkA family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA dealkylation involved in DNA repair

Inferred from direct assay PubMed 15722486PubMed 21960007. Source: PomBase

base-excision repair, AP site formation

Inferred from genetic interaction PubMed 15722486. Source: PomBase

depurination

Inferred from direct assay PubMed 21960007. Source: PomBase

recombinational repair

Inferred from mutant phenotype PubMed 15722486. Source: PomBase

   Cellular_componentnucleus

Inferred from direct assay PubMed 16823372. Source: PomBase

protein-DNA complex

Inferred from direct assay PubMed 21960007. Source: PomBase

   Molecular_functionDNA-1,N6-ethenoadenine N-glycosylase activity

Inferred from direct assay PubMed 21960007. Source: PomBase

DNA-3-methyladenine glycosylase activity

Inferred from genetic interaction Ref.1. Source: PomBase

DNA-3-methylguanine glycosylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

DNA-7-methyladenine glycosylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

DNA-7-methylguanine glycosylase activity

Inferred from direct assay PubMed 21960007. Source: PomBase

alkylated DNA binding

Inferred from direct assay PubMed 21960007. Source: PomBase

alkylbase DNA N-glycosylase activity

Inferred from direct assay PubMed 15722486. Source: PomBase

damaged DNA binding

Inferred from direct assay PubMed 15722486. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 228228DNA-3-methyladenine glycosylase 1
PRO_0000194881

Sites

Active site1701Proton acceptor By similarity
Site1501Determinant for substrate specificity and/or activity By similarity

Secondary structure

................................... 228
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q92383 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 4D134AB1EC377095

FASTA22826,381
        10         20         30         40         50         60 
MTLDIEEKEE IVTSLTKAEI HLSGLDENWK RLVKLVGNYR PNRSMEKKEP YEELIRAVAS 

        70         80         90        100        110        120 
QQLHSKAANA IFNRFKSISN NGQFPTPEEI RDMDFEIMRA CGFSARKIDS LKSIAEATIS 

       130        140        150        160        170        180 
GLIPTKEEAE RLSNEELIER LTQIKGIGRW TVEMLLIFSL NRDDVMPADD LSIRNGYRYL 

       190        200        210        220 
HRLPKIPTKM YVLKHSEICA PFRTAAAWYL WKTSKLADYT KPVRPKKH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a cDNA encoding a 3-methyladenine DNA glycosylase from the fission yeast Schizosaccharomyces pombe."
Memisoglu A., Samson L.
Gene 177:229-235(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76637 mRNA. Translation: AAC49524.1.
CU329670 Genomic DNA. Translation: CAC36900.1.
PIRJC5177.
RefSeqNP_593991.1. NM_001019417.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S6IX-ray2.28A/D1-228[»]
ProteinModelPortalQ92383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid279981. 30 interactions.
MINTMINT-4701520.
STRING4896.SPAPB24D3.04c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAPB24D3.04c.1; SPAPB24D3.04c.1:pep; SPAPB24D3.04c.
GeneID2543565.
KEGGspo:SPAPB24D3.04c.

Organism-specific databases

PomBaseSPAPB24D3.04c.

Phylogenomic databases

eggNOGCOG0122.
HOGENOMHOG000261908.
KOK01247.
OMAVEMFLIY.
OrthoDBEOG78SQVJ.
PhylomeDBQ92383.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
InterProIPR000035. Alkylbase_DNA_glycsylse_CS.
IPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR023170. HTH_base_excis_C.
[Graphical view]
PfamPF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
SM00278. HhH1. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
PROSITEPS00516. ALKYLBASE_DNA_GLYCOS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804573.

Entry information

Entry nameMAG1_SCHPO
AccessionPrimary (citable) accession number: Q92383
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references