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Protein

Tyrosine-protein phosphatase cdcA

Gene

cdcA

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

Functioni

Protein phosphatase which antagonizes mitotic cyclin-dependent kinase nimX, the inactivation of which is essential for exit from mitosis. To access its substrates, is released from nucleolar sequestration during mitosis. Plays an essential in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint. Involved in chromosome segregation, where it is required for meiosis I spindle dissambly as well as for establishing two consecutive chromosome segregation phases (By similarity). Required for the transcription of the two major endoglucanase genes eglA and eglB and growth on synthetic cellulose as the sole carbon source.By similarity1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei322 – 3221Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase cdcA (EC:3.1.3.48)
Gene namesi
Name:cdcA
ORF Names:AN5057
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome III

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595Tyrosine-protein phosphatase cdcAPRO_0000425254Add
BLAST

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00005331.

Structurei

3D structure databases

ProteinModelPortaliQ5B323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000198341.
InParanoidiQ5B323.
KOiK06639.
OMAiVYGVWKA.
OrthoDBiEOG7JQBXJ.

Family and domain databases

Gene3Di3.90.190.10. 2 hits.
InterProiIPR026070. CDC14.
IPR029260. DSPn.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR23339:SF27. PTHR23339:SF27. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5B323-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGSTAGYGQ IIEYIQDKLY LASYDHTPDA KTPFPYPAEQ PKSPSKRRAQ
60 70 80 90 100
ASPSKKRSPV YFTVDDTLLY NSFHADFGPL HIGHLYRFAV HFHDLLAANN
110 120 130 140 150
DRAIVFYSRT DARSRANAAC LVACYMVLIQ SWPPHLALAP IAQADPPYMP
160 170 180 190 200
FRDAGYSQAD FILNIQDVVY GVWKAKEQGV CGLRDFSLEE YEKFERVDMG
210 220 230 240 250
DFNWISPHFL AFASPQHQPV APIPRDSPEY AALPSTVSEV RSSRLPLPFK
260 270 280 290 300
NVLEHFATRG VGLVVRLNSE LYSPSYFTAL GISHIDMIFE DGTCPPLPLV
310 320 330 340 350
KKFIRMAHEM INVKHKAIAV HCKAGLGRTG CLIGAYLIYR YGFTANEVIA
360 370 380 390 400
FMRFMRPGMV VGPQQHWLHL NQGSFREWWF EDCMKEKLAQ MQPNPVTPGR
410 420 430 440 450
SPAKHRAAAV TTPPQNGHSK RSALGEIDNN EATPIYDDNL PAPTPGQPRK
460 470 480 490 500
SHRKDSRHHP YSRTASGSLV VDKDTRKTRR STDSSESEEE TQLRMLAKQR
510 520 530 540 550
SSKSPAASPG QRSISYSATV TASYTLNDDI HEDRENWGGA AQPPKTPVTS
560 570 580 590
KTSGAVSVSK VRSSSRRVTG ESKGVRKPSG RIGSTGSPVR VKAQA
Length:595
Mass (Da):66,129
Last modified:April 26, 2005 - v1
Checksum:i4C2999314618E2B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN001303 Genomic DNA. Translation: CBF76183.1.
AACD01000085 Genomic DNA. Translation: EAA60051.1.
RefSeqiXP_662661.1. XM_657569.1.

Genome annotation databases

EnsemblFungiiCADANIAT00005331; CADANIAP00005331; CADANIAG00005331.
GeneIDi2872855.
KEGGiani:AN5057.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BN001303 Genomic DNA. Translation: CBF76183.1.
AACD01000085 Genomic DNA. Translation: EAA60051.1.
RefSeqiXP_662661.1. XM_657569.1.

3D structure databases

ProteinModelPortaliQ5B323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00005331.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00005331; CADANIAP00005331; CADANIAG00005331.
GeneIDi2872855.
KEGGiani:AN5057.2.

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000198341.
InParanoidiQ5B323.
KOiK06639.
OMAiVYGVWKA.
OrthoDBiEOG7JQBXJ.

Family and domain databases

Gene3Di3.90.190.10. 2 hits.
InterProiIPR026070. CDC14.
IPR029260. DSPn.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR23339:SF27. PTHR23339:SF27. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF14671. DSPn. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  2. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "Analysis of all protein phosphatase genes in Aspergillus nidulans identifies a new mitotic regulator, fcp1."
    Son S., Osmani S.A.
    Eukaryot. Cell 8:573-585(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. "Gamma-tubulin regulates the anaphase-promoting complex/cyclosome during interphase."
    Nayak T., Edgerton-Morgan H., Horio T., Xiong Y., De Souza C.P., Osmani S.A., Oakley B.R.
    J. Cell Biol. 190:317-330(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Functional characterisation of the non-essential protein kinases and phosphatases regulating Aspergillus nidulans hydrolytic enzyme production."
    Brown N.A., de Gouvea P.F., Krohn N.G., Savoldi M., Goldman G.H.
    Biotechnol. Biofuels 6:91-91(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCDC14_EMENI
AccessioniPrimary (citable) accession number: Q5B323
Secondary accession number(s): C8V824
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 19, 2014
Last sequence update: April 26, 2005
Last modified: May 27, 2015
This is version 71 of the entry and version 1 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.