Q92383 (MAG1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 process	DNA damage DNA repair
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA dealkylation involved in DNA repair Inferred from direct assay. Source: GeneDB_Spombe base-excision repair, AP site formation Inferred from genetic interaction. Source: GeneDB_Spombe recombinational repair Inferred from mutant phenotype. Source: GeneDB_Spombe
Cellular component	nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	DNA-3-methyladenine glycosylase activity Inferred from electronic annotation. Source: EC DNA-3-methylguanine glycosylase activity Inferred from electronic annotation. Source: EC DNA-7-methyladenine glycosylase activity Inferred from electronic annotation. Source: EC DNA-7-methylguanine glycosylase activity Inferred from electronic annotation. Source: EC damaged DNA binding Inferred from direct assay. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 228	228	DNA-3-methyladenine glycosylase 1		PRO_0000194881
Sites
	Active site	170	1	Proton acceptor By similarity
	Site	150	1	Determinant for substrate specificity and/or activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92383 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 4D134AB1EC377095	FASTA	228	26,381
	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

References

	« Hide 'large scale' referencesShow '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: 8921872] [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. , 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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U76637 mRNA. Translation: AAC49524.1. CU329670 Genomic DNA. Translation: CAC36900.1.
PIR	JC5177.
RefSeq	NP_593991.1. NM_001019417.1.
3D structure databases
ProteinModelPortal	Q92383.
ModBase	Search...
Protein-protein interaction databases
STRING	Q92383.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAPB24D3.04c.1; SPAPB24D3.04c.1:pep; SPAPB24D3.04c.
GeneID	2543565.
GenomeReviews	Gene locus mag1 in contig CU329670_GR.
KEGG	spo:SPAPB24D3.04c.
NMPDR	fig|4896.1.peg.3961.
Organism-specific databases
GeneDB_Spombe	SPAPB24D3.04c.
Phylogenomic databases
eggNOG	fuNOG07498.
GeneTree	EFGT00050000005429.
HOGENOM	HBG544181.
OMA	QLHAKAG.
OrthoDB	EOG45HW6S.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001624-MONOMER.
Gene expression databases
ArrayExpress	Q92383.
Family and domain databases
InterPro	IPR000035. 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]
Gene3D	G3DSA:1.10.340.30. DNA_glycosylase. 1 hit. G3DSA:1.10.1670.10. HTH_base_excis_C. 1 hit.
KO	K01247.
Pfam	PF00730. HhH-GPD. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. SM00278. HhH1. 1 hit. [Graphical view]
SUPFAM	SSF48150. DNA_glycsylse. 1 hit.
PROSITE	PS00516. ALKYLBASE_DNA_GLYCOS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MAG1_SCHPO

Accession

Primary (citable) accession number: Q92383

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program