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Q4WUR1 (PP2B_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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:
Serine/threonine-protein phosphatase 2B catalytic subunit

EC=3.1.3.16
Alternative name(s):
Calmodulin-dependent calcineurin A subunit
Gene names
Name:cnaA
ORF Names:AFUA_5G09360
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length534 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin.

Catalytic activity

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

Cofactor

Binds 1 Fe3+ ion per subunit By similarity.

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Composed of two components (A and B), the A component is the catalytic subunit and the B component confers calcium sensitivity By similarity.

Sequence similarities

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

Sequence caution

The sequence EAL91665.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 534534Serine/threonine-protein phosphatase 2B catalytic subunit
PRO_0000286158

Sites

Active site1491Proton donor By similarity
Metal binding881Iron By similarity
Metal binding901Iron By similarity
Metal binding1161Iron By similarity
Metal binding1161Zinc By similarity
Metal binding1481Zinc By similarity
Metal binding1971Zinc By similarity
Metal binding2791Zinc By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WUR1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 94B717B7011B1C1B

FASTA53461,107
        10         20         30         40         50         60 
MEDGTQVSTL ERVIKEVQAP ALSTPTDEMF WSPEDPSKPN LQFLKQHFYR EGRLTEEQAL 

        70         80         90        100        110        120 
WIIHAGTQIL RSEPNLLEMD APITVCGDVH GQYYDLMKLF EVGGDPSETR YLFLGDYVDR 

       130        140        150        160        170        180 
GYFSIECVLY LWALKIWYPN SLWLLRGNHE CRHLTDYFTF KLECKHKYSE RIYEACIESF 

       190        200        210        220        230        240 
CALPLAAVMN KQFLCIHGGL SPELHTLEDI KSIDRFREPP THGLMCDILW ADPLEEFGQE 

       250        260        270        280        290        300 
KTGDYFVHNS VRGCSYFFSY PAACAFLEKN NLLSIIRAHE AQDAGYRMYR KTRTTGFPSV 

       310        320        330        340        350        360 
MTIFSAPNYL DVYNNKAAVL KYENNVMNIR QFNCTPHPYW LPNFMDVFTW SLPFVGEKIT 

       370        380        390        400        410        420 
DMLIAILNTC SKEELEDETP TSVSPSAPSP PLPMDVESSE FKRRAIKNKI LAIGRLSRVF 

       430        440        450        460        470        480 
QVLREESERV TELKTAAGGR LPAGTLMLGA EGIKQAITNF EDARKVDLQN ERLPPSHEEV 

       490        500        510        520        530 
IKRSEEERRA ALERAQQEAD NDTGLATVAR RISMSAGSGR SRRQRDAARE TREA 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000003 Genomic DNA. Translation: EAL91665.1. Different initiation.
RefSeqXP_753703.1. XM_748610.1.

3D structure databases

ProteinModelPortalQ4WUR1.
SMRQ4WUR1. Positions 6-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00005983.

Proteomic databases

PRIDEQ4WUR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3511045.
KEGGafm:AFUA_5G09360.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172699.
KOK04348.
OrthoDBEOG77M8X9.

Family and domain databases

InterProIPR004843. Calcineurin-like_PHP_apaH.
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 namePP2B_ASPFU
AccessionPrimary (citable) accession number: Q4WUR1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 59 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