MAG2_SCHPO
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 03-AUG-2022, entry version 135.
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 an 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 acive 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 4896.SPBC23G7.11.1; -.
DR MaxQB; O94468; -.
DR PaxDb; O94468; -.
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; RTVAAWY; -.
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: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 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; 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
