MAG1_SCHPO
ID MAG1_SCHPO Reviewed; 228 AA.
AC Q92383;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=DNA-3-methyladenine glycosylase 1;
DE EC=3.2.2.21;
DE AltName: Full=3-methyladenine DNA glycosidase 1;
DE AltName: Full=3MEA DNA glycosylase 1;
GN Name=mag1; ORFNames=SPAPB24D3.04c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 / ATCC 24843;
RX 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-
CC methyladenine or 7-methyladenine from the damaged DNA polymer formed by
CC alkylation lesions. Can release ethylated and propylated bases from DNA
CC in addition to 3-methyladenine.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-
CC methylguanine, 7-methylguanine and 7-methyladenine.; EC=3.2.2.21;
CC -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC {ECO:0000305}.
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DR EMBL; U76637; AAC49524.1; -; mRNA.
DR EMBL; CU329670; CAC36900.1; -; Genomic_DNA.
DR PIR; JC5177; JC5177.
DR RefSeq; NP_593991.1; NM_001019417.2.
DR PDB; 3S6I; X-ray; 2.28 A; A/D=1-228.
DR PDBsum; 3S6I; -.
DR AlphaFoldDB; Q92383; -.
DR SMR; Q92383; -.
DR BioGRID; 279981; 30.
DR STRING; 4896.SPAPB24D3.04c.1; -.
DR MaxQB; Q92383; -.
DR PaxDb; Q92383; -.
DR EnsemblFungi; SPAPB24D3.04c.1; SPAPB24D3.04c.1:pep; SPAPB24D3.04c.
DR GeneID; 2543565; -.
DR KEGG; spo:SPAPB24D3.04c; -.
DR PomBase; SPAPB24D3.04c; mag1.
DR VEuPathDB; FungiDB:SPAPB24D3.04c; -.
DR eggNOG; KOG1918; Eukaryota.
DR HOGENOM; CLU_000445_72_5_1; -.
DR InParanoid; Q92383; -.
DR OMA; WSPYRTI; -.
DR PhylomeDB; Q92383; -.
DR PRO; PR:Q92383; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032993; C:protein-DNA complex; IDA:PomBase.
DR GO; GO:0032131; F:alkylated DNA binding; IDA:PomBase.
DR GO; GO:0003905; F:alkylbase DNA N-glycosylase activity; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; IDA:PomBase.
DR GO; GO:0052820; F:DNA-1,N6-ethenoadenine N-glycosylase activity; IDA:PomBase.
DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IBA:GO_Central.
DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IDA:PomBase.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IGI:PomBase.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:PomBase.
DR CDD; cd00056; ENDO3c; 1.
DR InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT CHAIN 1..228
FT /note="DNA-3-methyladenine glycosylase 1"
FT /id="PRO_0000194881"
FT ACT_SITE 170
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT SITE 150
FT /note="Determinant for substrate specificity and/or
FT activity"
FT /evidence="ECO:0000250"
FT HELIX 17..23
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:3S6I"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:3S6I"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 87..92
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 105..120
FT /evidence="ECO:0007829|PDB:3S6I"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 189..196
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:3S6I"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3S6I"
SQ SEQUENCE 228 AA; 26381 MW; 4D134AB1EC377095 CRC64;
MTLDIEEKEE IVTSLTKAEI HLSGLDENWK RLVKLVGNYR PNRSMEKKEP YEELIRAVAS
QQLHSKAANA IFNRFKSISN NGQFPTPEEI RDMDFEIMRA CGFSARKIDS LKSIAEATIS
GLIPTKEEAE RLSNEELIER LTQIKGIGRW TVEMLLIFSL NRDDVMPADD LSIRNGYRYL
HRLPKIPTKM YVLKHSEICA PFRTAAAWYL WKTSKLADYT KPVRPKKH
