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Q9HFQ2 (PP2A1_EMENI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 69. 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:
Serine/threonine-protein phosphatase PP2A catalytic subunit
Short name=Protein phosphatase 2a
EC=3.1.3.16
Gene names
Name:pphA
ORF Names:AN6391
OrganismEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]
Taxonomic identifier227321 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella ›

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Involved in hyphal morphogenesis.

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Sequence similarities

Belongs to the PPP phosphatase family. PP-2A subfamily.

Ontologies

Keywords
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMMethylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   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 – 329329Serine/threonine-protein phosphatase PP2A catalytic subunit
PRO_0000058868

Sites

Active site1381Proton donor By similarity
Metal binding771Iron By similarity
Metal binding791Iron By similarity
Metal binding1051Iron By similarity
Metal binding1051Manganese By similarity
Metal binding1371Manganese By similarity
Metal binding1871Manganese By similarity
Metal binding2611Manganese By similarity

Amino acid modifications

Modified residue3291Leucine methyl ester By similarity

Experimental info

Sequence conflict1331I → T in CAC13980. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9HFQ2 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 79308C0B11E95E23

FASTA32937,665
        10         20         30         40         50         60 
MDNNMEIDAA RSPEPHHLSP TTDPGSIPTL DGWIESLMTC KQLAEEDVRR LCDRAREVLQ 

        70         80         90        100        110        120 
EESNVQPVKC PVTVCGDIHG QFHDLMELFR IGGPNPDTNY LFMGDYVDRG YYSVETVTLL 

       130        140        150        160        170        180 
VCLKIRYPQR ITILRGNHES RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALIE 

       190        200        210        220        230        240 
NQIFCLHGGL SPSIDTLDNI RSLDRIQEVP HEGPMCDLLW SDPDDRCGWG ISPRGAGYTF 

       250        260        270        280        290        300 
GQDISEAFNH NNGLTLVARA HQLVMEGYNW SQDRNVVTIF SAPNYCYRCG NQAAIMEIDE 

       310        320 
HLKYTFLQFD PCPRAGEPMV SRRTPDYFL

« Hide

References

« Hide 'large scale' references
[1]"A type 2A protein phosphatase gene from Aspergillus nidulans is involved in hyphal morphogenesis."
Kosmidou E., Lunness P., Doonan J.H.
Curr. Genet. 39:25-34(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae."
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. expand/collapse author list , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.
Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]"The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. expand/collapse author list , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ291510 Genomic DNA. Translation: CAC13980.1.
AACD01000108 Genomic DNA. Translation: EAA58413.1.
BN001301 Genomic DNA. Translation: CBF69560.1.
RefSeqXP_663995.1. XM_658903.1.

3D structure databases

ProteinModelPortalQ9HFQ2.
SMRQ9HFQ2. Positions 30-329.
ModBaseSearch...

Proteomic databases

PRIDEQ9HFQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADANIAT00006588; CADANIAP00006588; CADANIAG00006588.
GeneID2871291.
KEGGani:AN6391.2.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172696.
KOK04382.
OMATFNHANR.
OrthoDBEOG4GTPNM.

Family and domain databases

InterProIPR004843. Metallo_PEstase_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePP2A1_EMENI
AccessionPrimary (citable) accession number: Q9HFQ2
Secondary accession number(s): C8V0P5, Q5AZ89
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: May 1, 2007
Last modified: April 3, 2013
This is version 69 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

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