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Q93YW5 (P2C58_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable protein phosphatase 2C 58
Short name=AtPP2C58
EC=3.1.3.16
Gene names
Ordered Locus Names:At4g28400
ORF Names:F20O9.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Sequence similarities

Belongs to the PP2C family.

Contains 1 PP2C-like domain.

Sequence caution

The sequence CAA16879.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79642.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmetabolic process

Inferred from electronic annotation. Source: GOC

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 283283Probable protein phosphatase 2C 58
PRO_0000367980

Regions

Domain34 – 275242PP2C-like

Sites

Metal binding721Manganese 1 By similarity
Metal binding721Manganese 2 By similarity
Metal binding731Manganese 1; via carbonyl oxygen By similarity
Metal binding2341Manganese 2 By similarity
Metal binding2731Manganese 2 By similarity

Amino acid modifications

Modified residue461Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q93YW5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0F885E060AA68BE7

FASTA28331,018
        10         20         30         40         50         60 
MAGSNILHKI KLKAGFCGSA PDMGRGKSKM WKNITHGFHC VKGKSSHPME DYVVSEFKKL 

        70         80         90        100        110        120 
EGHELGLFAI FDGHLGHDVA KYLQTNLFDN ILKEKDFWTD TENAIRNAYR STDAVILQQS 

       130        140        150        160        170        180 
LKLGKGGSTA VTGILIDGKK LVVANVGDSR AVMSKNGVAH QLSVDHEPSK EKKEIESRGG 

       190        200        210        220        230        240 
FVSNIPGDVP RVDGQLAVAR AFGDKSLKLH LSSEPDITHQ TIDDHTEFIL FASDGIWKVL 

       250        260        270        280 
SNQEAVDAIK SIKDPHAAAK HLIEEAISRK SKDDISCIVV KFH

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Genome-wide and expression analysis of protein phosphatase 2C in rice and Arabidopsis."
Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.
BMC Genomics 9:550-550(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[5]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL021749 Genomic DNA. Translation: CAA16879.1. Sequence problems.
AL161572 Genomic DNA. Translation: CAB79642.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE85481.1.
AY059737 mRNA. Translation: AAL24149.1.
AY091272 mRNA. Translation: AAM14211.1.
IPIIPI00523731.
PIRT04610.
RefSeqNP_567808.1. NM_118982.3.
UniGeneAt.24767.

3D structure databases

HSSPHSSP built from PDB template 1A6Q based on UniProtKB P35813.
ProteinModelPortalQ93YW5.
SMRQ93YW5. Positions 36-280.
ModBaseSearch...

Proteomic databases

PaxDbQ93YW5.
PRIDEQ93YW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G28400.1; AT4G28400.1; AT4G28400.
GeneID828957.
KEGGath:AT4G28400.

Organism-specific databases

TAIRAt4g28400.

Phylogenomic databases

eggNOGCOG0631.
HOGENOMHOG000233896.
InParanoidQ93YW5.
OMALEGHELG.
PhylomeDBQ93YW5.
ProtClustDBCLSN2685102.

Gene expression databases

GenevestigatorQ93YW5.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81606. PP2C-related. 1 hit.
PROSITEPS01032. PP2C. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP2C58_ARATH
AccessionPrimary (citable) accession number: Q93YW5
Secondary accession number(s): O49449
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 1, 2001
Last modified: May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

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