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P49444 (PP2C1_PARTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Protein phosphatase 2C 1

Short name=PP2C 1
EC=3.1.3.16
Gene names
ORF Names:GSPATT00029903001
OrganismParamecium tetraurelia [Reference proteome]
Taxonomic identifier5888 [NCBI]
Taxonomic lineageEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaPeniculidaParameciidaeParamecium

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Enzyme with a broad specificity.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 magnesium or manganese ions per subunit By similarity.

Subcellular location

Membrane; Peripheral membrane protein.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the PP2C family.

Ontologies

Keywords
   Cellular componentMembrane
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotein dephosphorylation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 300300Protein phosphatase 2C 1
PRO_0000057765

Sites

Metal binding571Manganese 1 By similarity
Metal binding571Manganese 2 By similarity
Metal binding581Manganese 1; via carbonyl oxygen By similarity
Metal binding2371Manganese 2 By similarity
Metal binding2891Manganese 2 By similarity

Experimental info

Sequence conflict441P → H in CAA85448. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49444 [UniParc].

Last modified October 23, 2007. Version 2.
Checksum: B9EF98B4F78F24EC

FASTA30033,699
        10         20         30         40         50         60 
MGPYLSQPKR DKTTTTGQGK SVIFAASEMQ GWRNTMEDAH IHRPDIIQDV SVFGVFDGHG 

        70         80         90        100        110        120 
GREVAQFVEK HFVDELLKNK NFKEQKFEEA LKETFLKMDE LLLTPEGQKE LNQYKATDTD 

       130        140        150        160        170        180 
ESYAGCTANV ALIYKNTLYV ANAGDSRSVL CRNNTNHDMS VDHKPDNPEE KSRIERAGGF 

       190        200        210        220        230        240 
VSDGRVNGNL NLSRALGDLE YKRDNKLRSN EQLIIALPDV KKTELTPQDK FILMGCDGVF 

       250        260        270        280        290        300 
ETLNHQELLK QVNSTIGQAQ VTEELLKKAA EDLLDQLLAP DTSQGTGCDN MTTILVYLRR 

« Hide

References

« Hide 'large scale' references
[1]"A membrane-bound protein phosphatase type 2C from Paramecium tetraurelia. Purification, characterization, and cloning."
Klumpp S., Hanke C., Donella-Deana A., Beyer A., Kellner R., Pinna L.A., Schultz J.E.
J. Biol. Chem. 269:32774-32780(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Stock 51.
[2]"Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia."
Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R. expand/collapse author list , Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., Cohen J., Wincker P.
Nature 444:171-178(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Stock d4-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z36985 mRNA. Translation: CAA85448.1.
CT868001 Genomic DNA. Translation: CAK59272.1.
PIRA55804.
RefSeqXP_001426670.1. XM_001426633.1.
UniGenePte.1455.

3D structure databases

ProteinModelPortalP49444.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsCAK59272; CAK59272; GSPATT00029903001.
GeneID5012454.
KEGGptm:GSPATT00029903001.

Phylogenomic databases

KOK17499.

Family and domain databases

Gene3D3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR000222. PP2C_Mn2_Asp60_BS.
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. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP2C1_PARTE
AccessionPrimary (citable) accession number: P49444
Secondary accession number(s): A0BL55
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 23, 2007
Last modified: May 14, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families