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Reviewed, UniProtKB/Swiss-Prot O74489 (QOR_SCHPO)

Last modified November 25, 2008. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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 (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

NADPH + 2 quinone = NADP(+) + 2 semiquinone.

Subcellular location

Cytoplasm. Nucleus.

Sequence similarities

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

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Ontologies

Keywords

   Cellular componentCytoplasm
Nucleus
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytosol Ref.2

Inferred from direct assay. Source: GeneDB_SPombe

nucleus Ref.2

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionNADPH:quinone reductase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Probable quinone oxidoreductase
PRO_0000339115

Amino acid modifications

Modified residue1911Phosphoserine

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Sequences

Sequence LengthMass (Da)Tools
O74489-1 [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

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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: ATCC 38366 / 972.
[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.

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Cross-references

Sequence databases

CU329672 Genomic DNA. Translation: CAA21450.1.
PIRT40981.
T41247.
RefSeqNP_588330.1.

3D structure databases

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

Genome annotation databases

GeneID2538826.
KEGGspo:SPCC1442.16c.
NMPDRfig|4896.1.peg.668.

Organism-specific databases

GeneDB_SpombeSPCC1442.16c.

Gene expression databases

ArrayExpressO74489.

Family and domain databases

InterProIPR013154. AlcDHase_GroES-like.
IPR002085. AlcDHase_SF_Zn.
IPR013149. AlcDHase_Zn-bd.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: November 25, 2008
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents