MUTYH_ARATH
ID MUTYH_ARATH Reviewed; 630 AA.
AC F4JRF4; Q9SU12;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Adenine DNA glycosylase;
DE EC=3.2.2.31;
DE AltName: Full=MutY homolog;
DE Short=AtMYH;
GN Name=MYH; OrderedLocusNames=At4g12740; ORFNames=T20K18.90;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Involved in oxidative DNA damage repair. Initiates repair of
CC A*oxoG to C*G by removing the inappropriately paired adenine base from
CC the DNA backbone. Possesses both adenine and 2-OH-A DNA glycosylase
CC activities. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB40991.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78316.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL049640; CAB40991.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161534; CAB78316.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83174.1; -; Genomic_DNA.
DR PIR; T06632; T06632.
DR RefSeq; NP_193010.2; NM_117343.2.
DR AlphaFoldDB; F4JRF4; -.
DR SMR; F4JRF4; -.
DR STRING; 3702.AT4G12740.1; -.
DR PaxDb; F4JRF4; -.
DR PRIDE; F4JRF4; -.
DR EnsemblPlants; AT4G12740.1; AT4G12740.1; AT4G12740.
DR GeneID; 826886; -.
DR Gramene; AT4G12740.1; AT4G12740.1; AT4G12740.
DR KEGG; ath:AT4G12740; -.
DR Araport; AT4G12740; -.
DR TAIR; locus:2135828; AT4G12740.
DR eggNOG; KOG2457; Eukaryota.
DR HOGENOM; CLU_012862_0_0_1; -.
DR InParanoid; F4JRF4; -.
DR OrthoDB; 616758at2759; -.
DR PRO; PR:F4JRF4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JRF4; baseline and differential.
DR Genevisible; F4JRF4; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0035485; F:adenine/guanine mispair binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032357; F:oxidized purine DNA binding; IBA:GO_Central.
DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR CDD; cd03431; DNA_Glycosylase_C; 1.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR044298; MIG/MutY.
DR InterPro; IPR029119; MutY_C.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR PANTHER; PTHR42944; PTHR42944; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR Pfam; PF14815; NUDIX_4; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; DNA damage; DNA repair; Glycosidase; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1..630
FT /note="Adenine DNA glycosylase"
FT /id="PRO_0000421263"
FT DOMAIN 383..536
FT /note="Nudix hydrolase"
FT REGION 54..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 427..451
FT /note="Nudix box"
FT COMPBIAS 54..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..120
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 168
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P83847"
FT BINDING 341
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT SITE 287
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P83847"
SQ SEQUENCE 630 AA; 72000 MW; BCD53D14EAAEC662 CRC64;
MACLLRVALN PTFERSTVAS QRQNPKTILS FHCKVSSFKT KTMSQSFAPR EKLMRKCREK
KEAEREAERE AEREAEEEEK AEEAEAEADK EEAEEESEEE EEEEEEEAEA EEEALGGDIE
DLFSENETQK IRMGLLDWYD VNKRDLPWRN RRSESEKERR AYEVWVSEIM LQQTRVQTVM
KYYKRWMQKW PTIYDLGQAS LENLIVSRSR ELSFLRGNEK KEVNEMWAGL GYYRRARFLL
EGAKMVVAGT EGFPNQASSL MKVKGIGQYT AGAIASIAFN EAVPVVDGNV IRVLARLKAI
SANPKDRLTA RNFWKLAAQL VDPSRPGDFN QSLMELGATL CTVSKPSCSS CPVSSQCRAF
SLSEENRTIS VTDYPTKVIK AKPRHDFCCV CVLEIHNLER NQSGGRFVLV KRPEQGLLAG
LWEFPSVILN EEADSATRRN AINVYLKEAF RFHVELKKAC TIVSREELGE FVHIFTHIRR
KVYVELLVVQ LTGGTEDLFK GQAKDTLTWK CVSSDVLSTL GLTSAVRKVP PFRLQHIKRL
SLDVMVEKEQ ILECRCIQWL KHTSKAYLFL MSHQIEQPYR GNENSHDLLL TLFFMLLSFY
SSCLALGIKF GDLGLKLNSL VSTEKSDGDV
