Reviewed, UniProtKB/Swiss-Prot Q10159 (MYH1_SCHPO)

Names and origin

Protein names

Recommended name:
    A/G-specific adenine DNA glycosylase
    EC=3.2.2.-

Gene names

Name:	myh1
Synonyms:	myh
ORF Names:	SPAC26A3.02

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA damage checkpoint Inferred from genetic interaction. Source: GeneDB_SPombe base-excision repair Inferred by curator. Source: GeneDB_SPombe cellular response to UV Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from direct assay. Source: GeneDB_SPombe endonuclease activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidized base lesion DNA N-glycosylase activity Traceable author statement. Source: GeneDB_SPombe protein binding Inferred from physical interaction. Source: IntAct purine-specific mismatch base pair DNA N-glycosylase activity Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
hus1	P78955	2	EBI-767574,EBI-767597
pcn1	Q03392	1	EBI-767574,EBI-768724
rad1	P22193	1	EBI-767574,EBI-767637
rad9	P26306	1	EBI-767574,EBI-768686

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	A/G-specific adenine DNA glycosylase		PRO_0000102242
Sites
	Metal binding	226	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	233	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	236	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	242	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	7	1	S → F in AAC36207. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q10159-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 5908E880202E2242	FASTA	461	52,931
	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

References

	« Hide 'large scale' referencesShow '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. , 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: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF053340 mRNA. Translation: AAC36207.1. CU329670 Genomic DNA. Translation: CAA93225.1.
PIR	T38390. T43679.
RefSeq	NP_594145.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q10159. 4 interactions.
STRING	Q10159.
Genome annotation databases
GeneID	2542727.
GenomeReviews	Gene locus myh1 in contig CU329670_GR.
KEGG	spo:SPAC26A3.02.
NMPDR	fig|4896.1.peg.4115.
Organism-specific databases
GeneDB_Spombe	SPAC26A3.02.
Phylogenomic databases
OMA	HIFSHIR
OrthoDB	EOG9JHDZK
Gene expression databases
ArrayExpress	Q10159.
Family and domain databases
InterPro	IPR011257. DNA_glycosylase. IPR004036. Endonuclease-III_CS2. IPR004035. Endouclease-III_FeS-bd_BS. IPR003651. Endouclease3_FeS-loop_motif. IPR003265. HhH-GPD_domain. IPR000445. HhH_motif. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view]
Gene3D	G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.
Pfam	PF10576. EndIII_4Fe-2S. 1 hit. PF00633. HHH. 1 hit. PF00730. HhH-GPD. 1 hit. [Graphical view]
SMART	SM00478. ENDO3c. 1 hit. SM00525. FES. 1 hit. [Graphical view]
PROSITE	PS00764. ENDONUCLEASE_III_1. 1 hit. PS01155. ENDONUCLEASE_III_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MYH1_SCHPO

Accession

Primary (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:	November 24, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)