MPIP_EMENI
ID MPIP_EMENI Reviewed; 556 AA.
AC P30303; C8V635; Q5B689;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=M-phase inducer phosphatase;
DE EC=3.1.3.48 {ECO:0000269|PubMed:1534750};
GN Name=nimT; ORFNames=AN3941;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=GB20;
RX PubMed=1534750; DOI=10.1002/j.1460-2075.1992.tb05273.x;
RA O'Connell M.J., Osmani A.H., Morris N.R., Osmani S.A.;
RT "An extra copy of nimEcyclinB elevates pre-MPF levels and partially
RT suppresses mutation of nimTcdc25 in Aspergillus nidulans.";
RL EMBO J. 11:2139-2149(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
CC -!- FUNCTION: This protein functions as a dosage-dependent inducer in
CC mitotic control. It is a tyrosine protein phosphatase required for
CC progression of the cell cycle. It may directly dephosphorylate
CC p34(cdc2) and activate the p34(cdc2) kinase activity.
CC {ECO:0000305|PubMed:1534750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000269|PubMed:1534750};
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR EMBL; X64601; CAA45885.1; -; mRNA.
DR EMBL; AACD01000064; EAA59250.1; -; Genomic_DNA.
DR EMBL; BN001302; CBF75046.1; -; Genomic_DNA.
DR PIR; S24395; S24395.
DR RefSeq; XP_661545.1; XM_656453.1.
DR AlphaFoldDB; P30303; -.
DR SMR; P30303; -.
DR STRING; 162425.CADANIAP00004753; -.
DR EnsemblFungi; CBF75046; CBF75046; ANIA_03941.
DR EnsemblFungi; EAA59250; EAA59250; AN3941.2.
DR GeneID; 2873361; -.
DR KEGG; ani:AN3941.2; -.
DR VEuPathDB; FungiDB:AN3941; -.
DR eggNOG; KOG3772; Eukaryota.
DR HOGENOM; CLU_017900_0_0_1; -.
DR InParanoid; P30303; -.
DR OMA; PEMYILD; -.
DR OrthoDB; 1423329at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:AspGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:AspGD.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0110032; P:positive regulation of G2/MI transition of meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:AspGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:AspGD.
DR CDD; cd01530; Cdc25; 1.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR000751; MPI_Phosphatase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00716; MPIPHPHTASE.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Hydrolase; Mitosis; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..556
FT /note="M-phase inducer phosphatase"
FT /id="PRO_0000198660"
FT DOMAIN 371..474
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT REGION 164..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /evidence="ECO:0000250"
FT CONFLICT 353
FT /note="P -> G (in Ref. 1; CAA45885)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 61626 MW; F558E77944A0BA59 CRC64;
MEHSSPLAAM QPPSVMLGHC FRSDAPTSYH GFSPLPGLGP GGFNFKDLSM KRSNGDYFGT
KVVRGSSPTA SLAADLSQNF HIDQSPQVAT PRRSLFSACL LGNGNRRGVD DAMTTPPLPS
SSPAPAMDIM DMSPLPHKPP FISTPEIELD SPTLESSPMD TTMMSTDGLV PDSPTVLPKD
GKQERRRPTF LRPSLARSKA QSFQVGMTRP APESQGPPFK FQTNGINKTS SGVAASLEDM
FGESPQRERP MMRINSTSGL NSRLRPPLGS GSHVRGNGSP SAASVRKSAH PNMRPRKQCR
RSLSMYEHPE DVIADSEVSY TSNAPLQSIS DFEETQALQL PHFIPEEQAD NLPRIDKATL
VDIKEGKYDN MFDNIMIIDC RFEYEYDGGH IVGAVNYNDK ENLAAELFAD PKPRTAIVFH
CEYSVHRAPL MAKYIRHRDR AYNVDHYPQL SYPDMYILEG GYSGFFAEHR SLCYPQNYVE
MSAKEHEFAC ERGLGKVKQR SKLSRAQTFA FGQQSPEMED SPTGRCRNNP GDRKLLASPF
NDSPGSRFPG RRMLSY
