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O74489 (QOR_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable quinone oxidoreductase
EC=1.6.5.5
Alternative name(s):
NADPH:quinone reductase
Gene names
Name:zta1
ORF Names:SPCC1442.16c, SPCC285.01c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

NADPH + 2 quinone = NADP+ + 2 semiquinone.

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmRNA metabolic process

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionNADPH:quinone reductase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

mRNA 3'-UTR AU-rich region binding

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Probable quinone oxidoreductase
PRO_0000339115

Amino acid modifications

Modified residue1911Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
O74489 [UniParc].

Last modified August 1, 1999. Version 2.
Checksum: 534A8ED20C98C0AB

FASTA32934,947
        10         20         30         40         50         60 
MSNLLVQVSK TGPSSVLQVI TKEIPKPAPN GLVIKNAYAG LNYIDTYLRT GLYTAPLPYI 

        70         80         90        100        110        120 
PGKEAAGVVA AVGDKVEADF KVGDRVVYLT PFGAYAQYTN VPTTLVSKVS EKIPLKIASA 

       130        140        150        160        170        180 
ALLQGLTAYT LIEEAYPVKT GDTVVVHAAA GGVGLLLCQM LRARNVHVIA TASTAAKRRI 

       190        200        210        220        230        240 
AIKNGAEIAC SYEDLTKVVA DYTNGKGVDA AYDSVGIDTL SSSLDALRNG GTMVSFGNAS 

       250        260        270        280        290        300 
GAIDAIPLKF LSARCLKFVR PSLFGYITGH AVFEGYVSRL WKEILDNNLN IAIHHIFKLS 

       310        320 
EAKEAHDAIE SRATTGKLLL LCNEDLADA

« Hide

References

[1]"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.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329672 Genomic DNA. Translation: CAA21450.1.
PIRT40981.
T41247.
RefSeqNP_588330.1. NM_001023321.1.

3D structure databases

HSSPHSSP built from PDB template 1QOR based on UniProtKB P28304.
ProteinModelPortalO74489.
ModBaseSearch...

Protein-protein interaction databases

STRINGO74489.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1442.16c.1; SPCC1442.16c.1:pep; SPCC1442.16c.
GeneID2538826.
GenomeReviewsGene locus zta1 in contig CU329672_GR.
KEGGspo:SPCC1442.16c.
NMPDRfig|4896.1.peg.668.

Organism-specific databases

GeneDB_SpombeSPCC1442.16c.

Phylogenomic databases

eggNOGfuNOG04420.
GeneTreeEFGT00050000000744.
HOGENOMHBG753318.
OMALTIGHEY.
OrthoDBEOG470XSC.

Gene expression databases

ArrayExpressO74489.

Family and domain databases

InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00344.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQOR_SCHPO
AccessionPrimary (citable) accession number: O74489
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: August 1, 1999
Last modified: December 14, 2011
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents