ID   MAG2_SCHPO              Reviewed;         213 AA.
AC   O94468;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 142.
DE   RecName: Full=Alkylbase DNA glycosidase-like protein mag2 {ECO:0000305|PubMed:18270439};
GN   Name=mag2 {ECO:0000303|PubMed:18270439}; ORFNames=SPBC23G7.11;
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 [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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   FUNCTION.
RX   PubMed=18270439; DOI=10.1266/ggs.82.489;
RA   Kanamitsu K., Tanihigashi H., Tanita Y., Inatani S., Ikeda S.;
RT   "Involvement of 3-methyladenine DNA glycosylases Mag1p and Mag2p in base
RT   excision repair of methyl methanesulfonate-damaged DNA in the fission yeast
RT   Schizosaccharomyces pombe.";
RL   Genes Genet. Syst. 82:489-494(2007).
RN   [4] {ECO:0007744|PDB:4HSB}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH DNA, DNA-BINDING,
RP   FUNCTION, AND MUTAGENESIS OF ASP-56.
RX   PubMed=23273506; DOI=10.1016/j.dnarep.2012.12.001;
RA   Adhikary S., Cato M.C., McGary K.L., Rokas A., Eichman B.F.;
RT   "Non-productive DNA damage binding by DNA glycosylase-like protein Mag2
RT   from Schizosaccharomyces pombe.";
RL   DNA Repair 12:196-204(2013).
RN   [5] {ECO:0007744|PDB:4B21, ECO:0007744|PDB:4B22, ECO:0007744|PDB:4B23, ECO:0007744|PDB:4B24}
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH DNA, INDUCTION,
RP   SUBCELLULAR LOCATION, DNA-BINDING, FUNCTION, AND MUTAGENESIS OF LYS-53.
RX   PubMed=23245849; DOI=10.1016/j.str.2012.11.004;
RA   Dalhus B., Nilsen L., Korvald H., Huffman J., Forstrom R.J., McMurray C.T.,
RA   Alseth I., Tainer J.A., Bjoras M.;
RT   "Sculpting of DNA at abasic sites by DNA glycosylase homolog mag2.";
RL   Structure 21:154-166(2013).
CC   -!- FUNCTION: Alkylbase DNA glycosidase-like protein that shows no DNA
CC       glycosylase activity for alkylated bases (PubMed:23273506,
CC       PubMed:23245849). The molecular role of mag2 appears to be abasic (AP)
CC       site recognition and protection, while possibly facilitating damage
CC       signaling by structurally sculpting the DNA substrate (PubMed:18270439,
CC       PubMed:23245849). Stimulates AP site binding to mismatch repair protein
CC       mutS (PubMed:23245849). {ECO:0000269|PubMed:18270439,
CC       ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372,
CC       ECO:0000269|PubMed:23245849}.
CC   -!- INDUCTION: Transcription is strongly induced following exposure to the
CC       alkylating agent methyl methanesulfonate (MMS) and oxidizing H(2)O(2).
CC       {ECO:0000269|PubMed:23245849}.
CC   -!- SIMILARITY: Belongs to the alkylbase DNA glycosidase AlkA family.
CC       {ECO:0000305}.
CC   -!- CAUTION: As a homolog of the DNA glycosidase mag1, has been identified
CC       to be an alkylbase DNA glycosidase (PubMed:18270439). However, further
CC       studies revealed that it did not have any DNA glycosylase activity for
CC       alkylated bases due to the loss of the active site 'Ser-56', and was
CC       rather involved in structural sculpting DNA to facilitate damage
CC       signaling (PubMed:23273506, PubMed:23245849).
CC       {ECO:0000269|PubMed:18270439, ECO:0000269|PubMed:23245849,
CC       ECO:0000269|PubMed:23273506}.
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DR   EMBL; CU329671; CAA22627.1; -; Genomic_DNA.
DR   PIR; T39957; T39957.
DR   RefSeq; NP_595869.1; NM_001021775.2.
DR   PDB; 4B21; X-ray; 1.45 A; A=1-213.
DR   PDB; 4B22; X-ray; 1.90 A; A=1-213.
DR   PDB; 4B23; X-ray; 2.00 A; A=1-213.
DR   PDB; 4B24; X-ray; 2.30 A; A=1-213.
DR   PDB; 4HSB; X-ray; 1.90 A; A=1-213.
DR   PDBsum; 4B21; -.
DR   PDBsum; 4B22; -.
DR   PDBsum; 4B23; -.
DR   PDBsum; 4B24; -.
DR   PDBsum; 4HSB; -.
DR   AlphaFoldDB; O94468; -.
DR   SMR; O94468; -.
DR   BioGRID; 277171; 5.
DR   STRING; 284812.O94468; -.
DR   MaxQB; O94468; -.
DR   PaxDb; 4896-SPBC23G7-11-1; -.
DR   EnsemblFungi; SPBC23G7.11.1; SPBC23G7.11.1:pep; SPBC23G7.11.
DR   GeneID; 2540646; -.
DR   KEGG; spo:SPBC23G7.11; -.
DR   PomBase; SPBC23G7.11; mag2.
DR   VEuPathDB; FungiDB:SPBC23G7.11; -.
DR   eggNOG; KOG1918; Eukaryota.
DR   HOGENOM; CLU_000445_72_5_1; -.
DR   InParanoid; O94468; -.
DR   OMA; YLLWHYY; -.
DR   PhylomeDB; O94468; -.
DR   PRO; PR:O94468; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0032993; C:protein-DNA complex; IBA:GO_Central.
DR   GO; GO:0032131; F:alkylated DNA binding; IBA:GO_Central.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IDA:PomBase.
DR   GO; GO:0140431; F:DNA-(abasic site) binding; IDA:PomBase.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IGI:PomBase.
DR   CDD; cd00056; ENDO3c; 1.
DR   Gene3D; 1.10.1670.40; -; 1.
DR   InterPro; IPR000035; Alkylbase_DNA_glycsylse_CS.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR003265; HhH-GPD_domain.
DR   PANTHER; PTHR43003; DNA-3-METHYLADENINE GLYCOSYLASE; 1.
DR   PANTHER; PTHR43003:SF15; DNA-3-METHYLADENINE GLYCOSYLASE; 1.
DR   Pfam; PF00730; HhH-GPD; 1.
DR   SMART; SM00478; ENDO3c; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   PROSITE; PS00516; ALKYLBASE_DNA_GLYCOS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA damage; DNA repair; Nucleus; Reference proteome.
FT   CHAIN           1..213
FT                   /note="Alkylbase DNA glycosidase-like protein mag2"
FT                   /id="PRO_0000194882"
FT   BINDING         53
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849,
FT                   ECO:0000269|PubMed:23273506"
FT   BINDING         54
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23273506"
FT   BINDING         61
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23273506"
FT   BINDING         91
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849,
FT                   ECO:0000269|PubMed:23273506"
FT   BINDING         94
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23273506"
FT   BINDING         96
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23273506"
FT   BINDING         97
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849,
FT                   ECO:0000269|PubMed:23273506"
FT   BINDING         99
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23273506"
FT   BINDING         102
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23273506"
FT   BINDING         137
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849,
FT                   ECO:0000269|PubMed:23273506"
FT   BINDING         138
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849,
FT                   ECO:0000269|PubMed:23273506"
FT   BINDING         140
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849,
FT                   ECO:0000269|PubMed:23273506"
FT   BINDING         143
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849,
FT                   ECO:0000269|PubMed:23273506"
FT   BINDING         163
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849,
FT                   ECO:0000269|PubMed:23273506"
FT   BINDING         164
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /ligand_note="abasic DNA"
FT                   /evidence="ECO:0000269|PubMed:23245849"
FT   MUTAGEN         53
FT                   /note="K->G: Looses the ability to bind abasic DNA."
FT                   /evidence="ECO:0000269|PubMed:23245849"
FT   MUTAGEN         56
FT                   /note="D->S: Endows DNA glycosylase activity."
FT                   /evidence="ECO:0000269|PubMed:23273506"
FT   HELIX           3..14
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   TURN            15..17
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           19..28
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           41..50
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   TURN            51..53
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           56..70
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           79..83
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           87..91
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           97..111
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           118..123
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           126..133
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           141..150
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           163..172
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           181..187
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           195..203
FT                   /evidence="ECO:0007829|PDB:4B21"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:4B21"
SQ   SEQUENCE   213 AA;  24292 MW;  21E7E34A181D80EE CRC64;
     MSKDSDYKRA EKHLSSIDNK WSSLVKKVGP CTLTPHPEHA PYEGIIRAIT SQKLSDAATN
     SIINKFCTQC SDNDEFPTPK QIMETDVETL HECGFSKLKS QEIHIVAEAA LNKQIPSKSE
     IEKMSEEELM ESLSKIKGVK RWTIEMYSIF TLGRLDIMPA DDSTLKNEAK EFFGLSSKPQ
     TEEVEKLTKP CKPYRTIAAW YLWQIPKLHR KGQ
//