ID MYH1_SCHPO Reviewed; 461 AA.
AC Q10159; O74679;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 24-JAN-2024, entry version 164.
DE RecName: Full=Adenine DNA glycosylase;
DE EC=3.2.2.31;
GN Name=myh1; Synonyms=myh; ORFNames=SPAC26A3.02;
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], FUNCTION, AND SUBUNIT.
RX PubMed=9737967; DOI=10.1074/jbc.273.39.25098;
RA Lu A.-L., Fawcett W.P.;
RT "Characterization of the recombinant MutY homolog, an adenine DNA
RT glycosylase, from yeast Schizosaccharomyces pombe.";
RL J. Biol. Chem. 273:25098-25105(1998).
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: Adenine glycosylase active on G-A mispairs. Has glycosylase
CC and nicking activities and is active at A/G and A/GO sites.
CC {ECO:0000269|PubMed:9737967}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes free adenine bases from 7,8-dihydro-8-
CC oxoguanine:adenine mismatched double-stranded DNA, leaving an
CC apurinic site.; EC=3.2.2.31;
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a
CC role in catalysis, but is probably involved in the proper positioning
CC of the enzyme along the DNA strand. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9737967}.
CC -!- INTERACTION:
CC Q10159; P78955: hus1; NbExp=4; IntAct=EBI-767574, EBI-767597;
CC Q10159; P22193: rad1; NbExp=2; IntAct=EBI-767574, EBI-767637;
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
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; AF053340; AAC36207.1; -; mRNA.
DR EMBL; CU329670; CAA93225.1; -; Genomic_DNA.
DR PIR; T38390; T38390.
DR PIR; T43679; T43679.
DR RefSeq; NP_594145.1; NM_001019569.2.
DR AlphaFoldDB; Q10159; -.
DR SMR; Q10159; -.
DR BioGRID; 279177; 18.
DR IntAct; Q10159; 4.
DR STRING; 284812.Q10159; -.
DR MaxQB; Q10159; -.
DR PaxDb; 4896-SPAC26A3-02-1; -.
DR EnsemblFungi; SPAC26A3.02.1; SPAC26A3.02.1:pep; SPAC26A3.02.
DR GeneID; 2542727; -.
DR KEGG; spo:SPAC26A3.02; -.
DR PomBase; SPAC26A3.02; myh1.
DR VEuPathDB; FungiDB:SPAC26A3.02; -.
DR eggNOG; KOG2457; Eukaryota.
DR HOGENOM; CLU_012862_0_0_1; -.
DR InParanoid; Q10159; -.
DR OMA; QQTRMET; -.
DR PhylomeDB; Q10159; -.
DR Reactome; R-SPO-110331; Cleavage of the damaged purine.
DR PRO; PR:Q10159; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISM:PomBase.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IDA:PomBase.
DR GO; GO:0035485; F:adenine/guanine mispair binding; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032357; F:oxidized purine DNA binding; IDA:PomBase.
DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IDA:PomBase.
DR GO; GO:0006284; P:base-excision repair; EXP:PomBase.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IMP:PomBase.
DR GO; GO:0045007; P:depurination; IDA:PomBase.
DR GO; GO:0006974; P:DNA damage response; IMP:PomBase.
DR GO; GO:0006298; P:mismatch repair; IDA:PomBase.
DR CDD; cd03431; DNA_Glycosylase_C; 1.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR044298; MIG/MutY.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR PANTHER; PTHR42944; ADENINE DNA GLYCOSYLASE; 1.
DR PANTHER; PTHR42944:SF1; ADENINE DNA GLYCOSYLASE; 1.
DR Pfam; PF10576; EndIII_4Fe-2S; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF14815; NUDIX_4; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome.
FT CHAIN 1..461
FT /note="Adenine DNA glycosylase"
FT /id="PRO_0000102242"
FT DOMAIN 296..437
FT /note="Nudix hydrolase"
FT MOTIF 340..366
FT /note="Nudix box"
FT ACT_SITE 69
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 226
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT SITE 172
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT CONFLICT 7
FT /note="S -> F (in Ref. 1; AAC36207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 52931 MW; 5908E880202E2242 CRC64;
MSDSNHSLDL HSYTQLEVER FRESLIQFYD KTKRILPWRK KECIPPSEDS PLEDWEQPVQ
RLYEVLVSEI MLQQTRVETV KRYYTKWMET LPTLKSCAEA EYNTQVMPLW SGMGFYTRCK
RLHQACQHLA KLHPSEIPRT GDEWAKGIPG VGPYTAGAVL SIAWKQPTGI VDGNVIRVLS
RALAIHSDCS KGKANALIWK LANELVDPVR PGDFNQALME LGAITCTPQS PRCSVCPISE
ICKAYQEQNV IRDGNTIKYD IEDVPCNICI TDIPSKEDLQ NWVVARYPVH PAKTKQREER
ALVVIFQKTD PSTKEKFFLI RKRPSAGLLA GLWDFPTIEF GQESWPKDMD AEFQKSIAQW
ISNDSRSLIK KYQSRGRYLH IFSHIRKTSH VFYAIASPDI VTNEDFFWIS QSDLEHVGMC
ELGLKNYRAA LEIKKRKVTS LSNFKEPKLT SARRIVTKAE C
//
