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Q10159 (MYH1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
A/G-specific adenine DNA glycosylase
EC=3.2.2.-
Gene names
Name:myh1
Synonyms:myh
ORF Names:SPAC26A3.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Cofactor

Binds 1 4Fe-4S cluster. The cluster is not important for the catalytic activity, but which is probably involved in the proper positioning of the enzyme along the DNA strand By similarity.

Subunit structure

Monomer. Ref.1

Sequence similarities

Belongs to the Nth/MutY family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

hus1P789554EBI-767574,EBI-767597
rad1P221932EBI-767574,EBI-767637

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461A/G-specific adenine DNA glycosylase
PRO_0000102242

Sites

Metal binding2261Iron-sulfur (4Fe-4S) By similarity
Metal binding2331Iron-sulfur (4Fe-4S) By similarity
Metal binding2361Iron-sulfur (4Fe-4S) By similarity
Metal binding2421Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict71S → F in AAC36207. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q10159 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5908E880202E2242

FASTA46152,931
        10         20         30         40         50         60 
MSDSNHSLDL HSYTQLEVER FRESLIQFYD KTKRILPWRK KECIPPSEDS PLEDWEQPVQ 

        70         80         90        100        110        120 
RLYEVLVSEI MLQQTRVETV KRYYTKWMET LPTLKSCAEA EYNTQVMPLW SGMGFYTRCK 

       130        140        150        160        170        180 
RLHQACQHLA KLHPSEIPRT GDEWAKGIPG VGPYTAGAVL SIAWKQPTGI VDGNVIRVLS 

       190        200        210        220        230        240 
RALAIHSDCS KGKANALIWK LANELVDPVR PGDFNQALME LGAITCTPQS PRCSVCPISE 

       250        260        270        280        290        300 
ICKAYQEQNV IRDGNTIKYD IEDVPCNICI TDIPSKEDLQ NWVVARYPVH PAKTKQREER 

       310        320        330        340        350        360 
ALVVIFQKTD PSTKEKFFLI RKRPSAGLLA GLWDFPTIEF GQESWPKDMD AEFQKSIAQW 

       370        380        390        400        410        420 
ISNDSRSLIK KYQSRGRYLH IFSHIRKTSH VFYAIASPDI VTNEDFFWIS QSDLEHVGMC 

       430        440        450        460 
ELGLKNYRAA LEIKKRKVTS LSNFKEPKLT SARRIVTKAE C

« Hide

References

« Hide 'large scale' references
[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: 9737967] [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. expand/collapse author list , 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF053340 mRNA. Translation: AAC36207.1.
CU329670 Genomic DNA. Translation: CAA93225.1.
PIRT38390.
T43679.
RefSeqNP_594145.1. NM_001019569.1.

3D structure databases

ProteinModelPortalQ10159.
ModBaseSearch...

Protein-protein interaction databases

IntActQ10159. 4 interactions.
MINTMINT-1209697.
STRINGQ10159.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC26A3.02.1; SPAC26A3.02.1:pep; SPAC26A3.02.
GeneID2542727.
GenomeReviewsGene locus myh1 in contig CU329670_GR.
KEGGspo:SPAC26A3.02.
NMPDRfig|4896.1.peg.4115.

Organism-specific databases

GeneDB_SpombeSPAC26A3.02.

Phylogenomic databases

eggNOGfuNOG08833.
GeneTreeEFGT00050000008537.
HOGENOMHBG464473.
OMADEECETE.
OrthoDBEOG4HDX3M.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001766-MONOMER.

Gene expression databases

ArrayExpressQ10159.

Family and domain databases

InterProIPR011257. DNA_glycosylase.
IPR004036. Endonuclease-III_CS2.
IPR004035. Endouclease-III_FeS-bd_BS.
IPR003651. Endouclease3_FeS-loop_motif.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
[Graphical view]
Gene3DG3DSA:1.10.340.30. DNA_glycosylase. 1 hit.
G3DSA:1.10.1670.10. HTH_base_excis_C. 1 hit.
G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
KOK03575.
PfamPF10576. EndIII_4Fe-2S. 1 hit.
PF00730. HhH-GPD. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
SM00525. FES. 1 hit.
[Graphical view]
SUPFAMSSF48150. DNA_glycsylse. 1 hit.
SSF55811. NUDIX_hydrolase. 1 hit.
PROSITEPS00764. ENDONUCLEASE_III_1. 1 hit.
PS01155. ENDONUCLEASE_III_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMYH1_SCHPO
AccessionPrimary (citable) accession number: Q10159
Secondary accession number(s): O74679
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 14, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

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