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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit

Gene

cnaA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Fe3+By similarityNote: Binds 1 Fe3+ ion per subunit.By similarity
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121IronBy similarity
Metal bindingi114 – 1141IronBy similarity
Metal bindingi140 – 1401IronBy similarity
Metal bindingi140 – 1401ZincBy similarity
Metal bindingi172 – 1721ZincBy similarity
Active sitei173 – 1731Proton donorBy similarity
Metal bindingi221 – 2211ZincBy similarity
Metal bindingi303 – 3031ZincBy similarity

GO - Molecular functioni

  1. calcium-dependent protein serine/threonine phosphatase activity Source: ASPGD
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. dephosphorylation Source: GOC
  2. G1/S transition of mitotic cell cycle Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Calmodulin-binding, Iron, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2B catalytic subunit (EC:3.1.3.16)
Alternative name(s):
Calmodulin-dependent calcineurin A subunit
Gene namesi
Name:cnaA
ORF Names:AN8820
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome III

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549Serine/threonine-protein phosphatase 2B catalytic subunitPRO_0000058834Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi162425.CADANIAP00006237.

Structurei

3D structure databases

ProteinModelPortaliP48457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172699.
InParanoidiP48457.
KOiK04348.
OMAiAHTTENH.
OrthoDBiEOG77M8X9.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRNLARAVA DKQPVPEIDF TLHVMEDGTQ VSTLERVVKE VQAPALNKPS
60 70 80 90 100
DDQFWDPEEP TKPNLQFLKQ HFYREGRLTE DQALWIIQAG TQILKSEPNL
110 120 130 140 150
LEMDAPITVC GDVHGQYYDL MKLFEVGGDP AETRYLFLGD YVDRGYFSIE
160 170 180 190 200
CVLYLWALKI WYPNTLWLLR GNHECRHLTD YFTFKLECKH KYSERIYEAC
210 220 230 240 250
IESFCALPLA AVMNKQFLCI HGGLSPELHT LEDIKSIDRF REPPTHGLMC
260 270 280 290 300
DILWADPLED FGQEKTGDYF IHNSVRGCSY FFSYPAACAF LEKNNLLSVI
310 320 330 340 350
RAHEAQDAGY RMYRKTRTTG FPSVMTIFSA PNYLDVYNNK AAVLKYENNV
360 370 380 390 400
MNIRQFNCTP HPYWLPNFMD VFTWSLPFVG EKITDMLIAI LNTCSKEELE
410 420 430 440 450
DETPSTISPA EPSPPMPMDT VDTESTEFKR RAIKNKILAI GRLSRVFQVL
460 470 480 490 500
REESERVTEL KTAAGGRLPA GTLMLGAEGI KQAITNFEDA RKVDLQNERL
510 520 530 540
PPSHDEVVRR SEEERRIALD RAQHEADNDT GLATVARRIS MKIPSTTRR
Length:549
Mass (Da):63,007
Last modified:November 16, 2011 - v3
Checksum:iECD795FCBBDF4991
GO

Sequence cautioni

The sequence AAA57873.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EAA60108.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti386 – 3872ML → IV in AAA57873 (PubMed:8013455).Curated
Sequence conflicti541 – 5411M → MVRRIR in AAA57873 (PubMed:8013455).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13919 Genomic DNA. Translation: AAA57873.1. Different initiation.
AACD01000162 Genomic DNA. Translation: EAA60108.1. Different initiation.
BN001303 Genomic DNA. Translation: CBF77949.1.
PIRiS46322.
RefSeqiXP_682089.1. XM_676997.1.

Genome annotation databases

EnsemblFungiiCADANIAT00006237; CADANIAP00006237; CADANIAG00006237.
GeneIDi2868443.
KEGGiani:AN8820.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13919 Genomic DNA. Translation: AAA57873.1. Different initiation.
AACD01000162 Genomic DNA. Translation: EAA60108.1. Different initiation.
BN001303 Genomic DNA. Translation: CBF77949.1.
PIRiS46322.
RefSeqiXP_682089.1. XM_676997.1.

3D structure databases

ProteinModelPortaliP48457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00006237.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00006237; CADANIAP00006237; CADANIAG00006237.
GeneIDi2868443.
KEGGiani:AN8820.2.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172699.
InParanoidiP48457.
KOiK04348.
OMAiAHTTENH.
OrthoDBiEOG77M8X9.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The calmodulin-dependent protein phosphatase catalytic subunit (calcineurin A) is an essential gene in Aspergillus nidulans."
    Rasmussen C.D., Garen C., Brining S., Kincaid R.L., Means R.L., Means A.R.
    EMBO J. 13:2545-2552(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. 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.
    , 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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiPP2B_EMENI
AccessioniPrimary (citable) accession number: P48457
Secondary accession number(s): C8V9L3, Q5ASB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 16, 2011
Last modified: January 7, 2015
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.