PP1_EMENI
ID PP1_EMENI Reviewed; 323 AA.
AC P20654; C8VTH6; Q5BGC0;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Serine/threonine-protein phosphatase PP1;
DE EC=3.1.3.16;
GN Name=bimG; ORFNames=AN0410;
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].
RX PubMed=2544297; DOI=10.1016/0092-8674(89)90337-1;
RA Doonan J.H., Morris N.R.;
RT "The bimG gene of Aspergillus nidulans, required for completion of
RT anaphase, encodes a homolog of mammalian phosphoprotein phosphatase 1.";
RL Cell 57:987-996(1989).
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: Plays an important role in the control of mitosis by
CC reversing the action of the nimA kinase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; M27067; AAA33299.1; -; mRNA.
DR EMBL; AACD01000007; EAA66509.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF89542.1; -; Genomic_DNA.
DR PIR; A32549; A32549.
DR RefSeq; XP_658014.1; XM_652922.1.
DR AlphaFoldDB; P20654; -.
DR SMR; P20654; -.
DR STRING; 162425.CADANIAP00002289; -.
DR EnsemblFungi; CBF89542; CBF89542; ANIA_00410.
DR EnsemblFungi; EAA66509; EAA66509; AN0410.2.
DR GeneID; 2876189; -.
DR KEGG; ani:AN0410.2; -.
DR VEuPathDB; FungiDB:AN0410; -.
DR eggNOG; KOG0374; Eukaryota.
DR HOGENOM; CLU_004962_0_0_1; -.
DR InParanoid; P20654; -.
DR OMA; EEHEIRY; -.
DR OrthoDB; 766640at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0030428; C:cell septum; IDA:AspGD.
DR GO; GO:0032174; C:cellular bud neck septin collar; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0000776; C:kinetochore; IEA:EnsemblFungi.
DR GO; GO:0001400; C:mating projection base; IEA:EnsemblFungi.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IDA:AspGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:EnsemblFungi.
DR GO; GO:0005816; C:spindle pole body; IDA:AspGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0051211; P:anisotropic cell growth; IMP:AspGD.
DR GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR GO; GO:0006873; P:cellular ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0007059; P:chromosome segregation; IMP:AspGD.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:AspGD.
DR GO; GO:0034221; P:fungal-type cell wall chitin biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0000022; P:mitotic spindle elongation; IMP:AspGD.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:EnsemblFungi.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IEA:EnsemblFungi.
DR GO; GO:1903501; P:positive regulation of mitotic actomyosin contractile ring assembly; IEA:EnsemblFungi.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IEA:EnsemblFungi.
DR GO; GO:0034501; P:protein localization to kinetochore; IEA:EnsemblFungi.
DR GO; GO:0007116; P:regulation of cell budding; IEA:EnsemblFungi.
DR GO; GO:0008360; P:regulation of cell shape; IEA:EnsemblFungi.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; IEA:EnsemblFungi.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:1901901; P:regulation of protein localization to cell division site involved in cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0031297; P:replication fork processing; IEA:EnsemblFungi.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblFungi.
DR GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR GO; GO:0000723; P:telomere maintenance; IEA:EnsemblFungi.
DR GO; GO:0061587; P:transfer RNA gene-mediated silencing; IEA:EnsemblFungi.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Hydrolase; Manganese; Metal-binding; Mitosis;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..323
FT /note="Serine/threonine-protein phosphatase PP1"
FT /id="PRO_0000058816"
FT ACT_SITE 124
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 323 AA; 37176 MW; 9CED43E15C5AA5BA CRC64;
MADQDVDLDS IIDRLLEVRG SRPGKQVQLL ESEIRYLCTK AREIFISQPI LLELEAPIKI
CGDIHGQYYD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFVL
RGNHECASIN RIYGFYDECK RRYNIKLWKT FTDCFNCLPI AAIIDEKIFT MHGGLSPDLN
SMEQIRRVMR PTDIPDCGLL CDLLWSDPDK DITGWSENDR GVSFTFGPDV VSRFLQKHDM
DLICRAHQVV EDGYEFFSKR QLVTLFSAPN YCGEFDNAGA MMSVDESLLC SFQILKPAEK
KQKYVYGAMS SGRPITPPRK QKK
