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Protein

M-phase inducer phosphatase

Gene

nimT

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-Experimental evidence at transcript leveli

Functioni

This protein functions as a dosage-dependent inducer in mitotic control. It is a tyrosine protein phosphatase required for progression of the cell cycle. It may directly dephosphorylate p34(cdc2) and activate the p34(cdc2) kinase activity.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei421 – 4211By similarity

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: ASPGD

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. G2/M transition of mitotic cell cycle Source: ASPGD
  3. mitotic nuclear division Source: UniProtKB-KW
  4. peptidyl-tyrosine dephosphorylation Source: GOC
  5. positive regulation of mitotic nuclear division Source: ASPGD
  6. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ASPGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase inducer phosphatase (EC:3.1.3.48)
Gene namesi
Name:nimT
ORF Names:AN3941
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome II

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556M-phase inducer phosphatasePRO_0000198660Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00004753.

Structurei

3D structure databases

ProteinModelPortaliP30303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini371 – 474104RhodanesePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the MPI phosphatase family.Curated
Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5105.
HOGENOMiHOG000215320.
InParanoidiP30303.
KOiK02555.
OMAiQRTCERE.
OrthoDBiEOG7VMPGR.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR00716. MPIPHPHTASE.
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEHSSPLAAM QPPSVMLGHC FRSDAPTSYH GFSPLPGLGP GGFNFKDLSM
60 70 80 90 100
KRSNGDYFGT KVVRGSSPTA SLAADLSQNF HIDQSPQVAT PRRSLFSACL
110 120 130 140 150
LGNGNRRGVD DAMTTPPLPS SSPAPAMDIM DMSPLPHKPP FISTPEIELD
160 170 180 190 200
SPTLESSPMD TTMMSTDGLV PDSPTVLPKD GKQERRRPTF LRPSLARSKA
210 220 230 240 250
QSFQVGMTRP APESQGPPFK FQTNGINKTS SGVAASLEDM FGESPQRERP
260 270 280 290 300
MMRINSTSGL NSRLRPPLGS GSHVRGNGSP SAASVRKSAH PNMRPRKQCR
310 320 330 340 350
RSLSMYEHPE DVIADSEVSY TSNAPLQSIS DFEETQALQL PHFIPEEQAD
360 370 380 390 400
NLPRIDKATL VDIKEGKYDN MFDNIMIIDC RFEYEYDGGH IVGAVNYNDK
410 420 430 440 450
ENLAAELFAD PKPRTAIVFH CEYSVHRAPL MAKYIRHRDR AYNVDHYPQL
460 470 480 490 500
SYPDMYILEG GYSGFFAEHR SLCYPQNYVE MSAKEHEFAC ERGLGKVKQR
510 520 530 540 550
SKLSRAQTFA FGQQSPEMED SPTGRCRNNP GDRKLLASPF NDSPGSRFPG

RRMLSY
Length:556
Mass (Da):61,626
Last modified:May 1, 2007 - v2
Checksum:iF558E77944A0BA59
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti353 – 3531P → G in CAA45885 (PubMed:1534750).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64601 mRNA. Translation: CAA45885.1.
AACD01000064 Genomic DNA. Translation: EAA59250.1.
BN001302 Genomic DNA. Translation: CBF75046.1.
PIRiS24395.
RefSeqiXP_661545.1. XM_656453.1.

Genome annotation databases

EnsemblFungiiCADANIAT00004753; CADANIAP00004753; CADANIAG00004753.
GeneIDi2873361.
KEGGiani:AN3941.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64601 mRNA. Translation: CAA45885.1.
AACD01000064 Genomic DNA. Translation: EAA59250.1.
BN001302 Genomic DNA. Translation: CBF75046.1.
PIRiS24395.
RefSeqiXP_661545.1. XM_656453.1.

3D structure databases

ProteinModelPortaliP30303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00004753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00004753; CADANIAP00004753; CADANIAG00004753.
GeneIDi2873361.
KEGGiani:AN3941.2.

Phylogenomic databases

eggNOGiCOG5105.
HOGENOMiHOG000215320.
InParanoidiP30303.
KOiK02555.
OMAiQRTCERE.
OrthoDBiEOG7VMPGR.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR00716. MPIPHPHTASE.
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An extra copy of nimEcyclinB elevates pre-MPF levels and partially suppresses mutation of nimTcdc25 in Aspergillus nidulans."
    O'Connell M.J., Osmani A.H., Morris N.R., Osmani S.A.
    EMBO J. 11:2139-2149(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: GB20.
  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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Entry informationi

Entry nameiMPIP_EMENI
AccessioniPrimary (citable) accession number: P30303
Secondary accession number(s): C8V635, Q5B689
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 1, 2007
Last modified: April 1, 2015
This is version 93 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.