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Protein

Adenine DNA glycosylase

Gene

myh1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adenine glycosylase active on G-A mispairs. Has glycosylase and nicking activities and is active at A/G and A/GO sites.1 Publication

Cofactori

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei69 – 691Proton donor/acceptorBy similarity
Sitei172 – 1721Transition state stabilizerBy similarity
Metal bindingi226 – 2261Iron-sulfur (4Fe-4S)By similarity
Metal bindingi233 – 2331Iron-sulfur (4Fe-4S)By similarity
Metal bindingi236 – 2361Iron-sulfur (4Fe-4S)By similarity
Metal bindingi242 – 2421Iron-sulfur (4Fe-4S)By similarity

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity Source: PomBase
  • adenine/guanine mispair binding Source: PomBase
  • metal ion binding Source: UniProtKB-KW
  • oxidized purine DNA binding Source: PomBase
  • purine-specific mismatch base pair DNA N-glycosylase activity Source: PomBase

GO - Biological processi

  • base-excision repair Source: PomBase
  • base-excision repair, AP site formation Source: PomBase
  • cellular response to DNA damage stimulus Source: PomBase
  • cellular response to UV Source: PomBase
  • depurination Source: PomBase
  • detection of DNA damage stimulus involved in DNA damage checkpoint Source: PomBase
  • mismatch repair Source: PomBase
  • positive regulation of phosphodiesterase I activity Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

ReactomeiR-SPO-110331. Cleavage of the damaged purine.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenine DNA glycosylase (EC:3.2.2.-)
Gene namesi
Name:myh1
Synonyms:myh
ORF Names:SPAC26A3.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.02.
PomBaseiSPAC26A3.02. myh1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Adenine DNA glycosylasePRO_0000102242Add
BLAST

Proteomic databases

MaxQBiQ10159.
PRIDEiQ10159.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
hus1P789554EBI-767574,EBI-767597
rad1P221932EBI-767574,EBI-767637

Protein-protein interaction databases

BioGridi279177. 18 interactions.
IntActiQ10159. 4 interactions.
MINTiMINT-1209697.

Structurei

3D structure databases

ProteinModelPortaliQ10159.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini296 – 437142Nudix hydrolaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi340 – 36627Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nth/MutY family.Curated
Contains 1 nudix hydrolase domain.Curated

Phylogenomic databases

InParanoidiQ10159.
KOiK03575.
OMAiAGKCNFF.
OrthoDBiEOG75B8F7.
PhylomeDBiQ10159.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR029119. MutY_C.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF10576. EndIII_4Fe-2S. 1 hit.
PF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSNHSLDL HSYTQLEVER FRESLIQFYD KTKRILPWRK KECIPPSEDS
60 70 80 90 100
PLEDWEQPVQ RLYEVLVSEI MLQQTRVETV KRYYTKWMET LPTLKSCAEA
110 120 130 140 150
EYNTQVMPLW SGMGFYTRCK RLHQACQHLA KLHPSEIPRT GDEWAKGIPG
160 170 180 190 200
VGPYTAGAVL SIAWKQPTGI VDGNVIRVLS RALAIHSDCS KGKANALIWK
210 220 230 240 250
LANELVDPVR PGDFNQALME LGAITCTPQS PRCSVCPISE ICKAYQEQNV
260 270 280 290 300
IRDGNTIKYD IEDVPCNICI TDIPSKEDLQ NWVVARYPVH PAKTKQREER
310 320 330 340 350
ALVVIFQKTD PSTKEKFFLI RKRPSAGLLA GLWDFPTIEF GQESWPKDMD
360 370 380 390 400
AEFQKSIAQW ISNDSRSLIK KYQSRGRYLH IFSHIRKTSH VFYAIASPDI
410 420 430 440 450
VTNEDFFWIS QSDLEHVGMC ELGLKNYRAA LEIKKRKVTS LSNFKEPKLT
460
SARRIVTKAE C
Length:461
Mass (Da):52,931
Last modified:October 1, 1996 - v1
Checksum:i5908E880202E2242
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71S → F in AAC36207 (PubMed:9737967).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053340 mRNA. Translation: AAC36207.1.
CU329670 Genomic DNA. Translation: CAA93225.1.
PIRiT38390.
T43679.
RefSeqiNP_594145.1. NM_001019569.2.

Genome annotation databases

EnsemblFungiiSPAC26A3.02.1; SPAC26A3.02.1:pep; SPAC26A3.02.
GeneIDi2542727.
KEGGispo:SPAC26A3.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053340 mRNA. Translation: AAC36207.1.
CU329670 Genomic DNA. Translation: CAA93225.1.
PIRiT38390.
T43679.
RefSeqiNP_594145.1. NM_001019569.2.

3D structure databases

ProteinModelPortaliQ10159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279177. 18 interactions.
IntActiQ10159. 4 interactions.
MINTiMINT-1209697.

Proteomic databases

MaxQBiQ10159.
PRIDEiQ10159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC26A3.02.1; SPAC26A3.02.1:pep; SPAC26A3.02.
GeneIDi2542727.
KEGGispo:SPAC26A3.02.

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.02.
PomBaseiSPAC26A3.02. myh1.

Phylogenomic databases

InParanoidiQ10159.
KOiK03575.
OMAiAGKCNFF.
OrthoDBiEOG75B8F7.
PhylomeDBiQ10159.

Enzyme and pathway databases

ReactomeiR-SPO-110331. Cleavage of the damaged purine.

Miscellaneous databases

PROiQ10159.

Family and domain databases

Gene3Di1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
3.90.79.10. 1 hit.
InterProiIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III-like_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR000445. HhH_motif.
IPR023170. HTH_base_excis_C.
IPR029119. MutY_C.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
PfamiPF10576. EndIII_4Fe-2S. 1 hit.
PF00633. HHH. 1 hit.
PF00730. HhH-GPD. 1 hit.
PF14815. NUDIX_4. 1 hit.
[Graphical view]
SMARTiSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMiSSF48150. SSF48150. 1 hit.
SSF55811. SSF55811. 1 hit.
PROSITEiPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the recombinant MutY homolog, an adenine DNA glycosylase, from yeast Schizosaccharomyces pombe."
    Lu A.-L., Fawcett W.P.
    J. Biol. Chem. 273:25098-25105(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiMYH1_SCHPO
AccessioniPrimary (citable) accession number: Q10159
Secondary accession number(s): O74679
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.