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Protein

Serine/threonine-protein phosphatase 2B catalytic subunit

Gene

cna-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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 bindingi128 – 1281IronBy similarity
Metal bindingi130 – 1301IronBy similarity
Metal bindingi156 – 1561IronBy similarity
Metal bindingi156 – 1561ZincBy similarity
Metal bindingi188 – 1881ZincBy similarity
Active sitei189 – 1891Proton donorBy similarity
Metal bindingi237 – 2371ZincBy similarity
Metal bindingi319 – 3191ZincBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. calcium-mediated signaling Source: EnsemblFungi
  2. cellular chloride ion homeostasis Source: EnsemblFungi
  3. cellular response to salt stress Source: EnsemblFungi
  4. cytosolic calcium ion homeostasis Source: EnsemblFungi
  5. fungal-type cell wall organization or biogenesis Source: EnsemblFungi
  6. negative regulation of calcium ion transport into cytosol Source: EnsemblFungi
  7. regulation of conjugation with cellular fusion Source: EnsemblFungi
  8. regulation of establishment or maintenance of cell polarity regulating cell shape Source: EnsemblFungi
  9. regulation of mitotic cytokinesis Source: EnsemblFungi
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:cna-1
ORF Names:99H12.070, NCU03804
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805 Componenti: Chromosome 2, Linkage Group V

Subcellular locationi

GO - Cellular componenti

  1. cell division site Source: EnsemblFungi
  2. cytosol Source: EnsemblFungi
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 558558Serine/threonine-protein phosphatase 2B catalytic subunitPRO_0000058833Add
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

STRINGi5141.NCU03804.1.

Structurei

3D structure databases

SMRiQ05681. Positions 46-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172699.
InParanoidiQ05681.
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.

Q05681-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESNNGTGAP GAFHTQQVDN AIRAIQHKRP LPEIDFTIHT MEDGSQVSTM
60 70 80 90 100
ERVCKDVQAP AMFKPSDEQF FEDETHTKPD IQFLKQHFYR EGRLTEEQAL
110 120 130 140 150
WIIREGTKLL RAEPNLLEMD APITVCGDVH GQYYDLMKLF EVGGDPAETR
160 170 180 190 200
YLFLGDYVDR GYFSIECVLY LWALKIHYPK TLWLLRGNHE CRHLTDYFTF
210 220 230 240 250
KLECKHKYSE AIYEACMESF CCLPLAAVMN KQFLCIHGGL SPELHTLDDI
260 270 280 290 300
RNIDRFREPP TQGLMCDILW ADPLEDFGQE KTTDFFVHNH VRGCSYFFSY
310 320 330 340 350
SAACHFLEKN NLLSIIRAHE AQDAGYRMYR KTRTTGFPSV MTIFSAPNYL
360 370 380 390 400
DVYNNKAAVL KYENNVMNIR QFNCTPHPYW LPNFMDVFTW SLPFVGEKIT
410 420 430 440 450
DMLIAILSTC SEEELREDSA TTSPGSASPA LPSAANQDPD SIEFKRRAIK
460 470 480 490 500
NKILAIGRLS RVFQVLREES ERVTELKTVS GGRLPAGTLM LGAEGIKNAI
510 520 530 540 550
SSFEDARKVD LQNERLPPSH DEVVKMQDEE RAQALERATR EADNDKKLQT

LSRRLSTS
Length:558
Mass (Da):63,914
Last modified:December 3, 2007 - v2
Checksum:iFDE74D72A000A55E
GO

Sequence cautioni

The sequence AAA33565.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC18243.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73032 mRNA. Translation: AAA33565.1. Different initiation.
AL451018 Genomic DNA. Translation: CAC18243.1. Sequence problems.
CM002240 Genomic DNA. Translation: ESA42471.1.
PIRiA40942.

Genome annotation databases

EnsemblFungiiEFNCRT00000003478; EFNCRP00000003478; EFNCRG00000003474.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73032 mRNA. Translation: AAA33565.1. Different initiation.
AL451018 Genomic DNA. Translation: CAC18243.1. Sequence problems.
CM002240 Genomic DNA. Translation: ESA42471.1.
PIRiA40942.

3D structure databases

SMRiQ05681. Positions 46-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5141.NCU03804.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEFNCRT00000003478; EFNCRP00000003478; EFNCRG00000003474.

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172699.
InParanoidiQ05681.
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. "Calmodulin-dependent protein phosphatase from Neurospora crassa. Molecular cloning and expression of recombinant catalytic subunit."
    Higuchi S., Tamura J., Rathna Giri P., Polli J.W., Kincaid R.L.
    J. Biol. Chem. 266:18104-18112(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
    Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
    Nucleic Acids Res. 31:1944-1954(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
  3. "The genome sequence of the filamentous fungus Neurospora crassa."
    Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
    , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
    Nature 422:859-868(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

Entry informationi

Entry nameiPP2B_NEUCR
AccessioniPrimary (citable) accession number: Q05681
Secondary accession number(s): Q1K7G7, Q9HEE2, V5INZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1996
Last sequence update: December 3, 2007
Last modified: March 31, 2015
This is version 91 of the entry and version 2 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.