PP2A1_NEUCR
ID PP2A1_NEUCR Reviewed; 327 AA.
AC P48580; Q7RVE8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A catalytic subunit;
DE EC=3.1.3.16;
GN Name=pph-1; ORFNames=NCU06630;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=8575020; DOI=10.1007/bf00310816;
RA Yatzkan E., Yarden O.;
RT "Inactivation of a single-2A phosphoprotein phosphatase is lethal in
RT Neurospora crassa.";
RL Curr. Genet. 28:458-466(1995).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Yarden O.;
RL Submitted (APR-2003) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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-2A subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA58573.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X83593; CAA58573.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002239; EAA32582.2; -; Genomic_DNA.
DR PIR; S60471; S60471.
DR RefSeq; XP_961818.2; XM_956725.3.
DR AlphaFoldDB; P48580; -.
DR SMR; P48580; -.
DR STRING; 5141.EFNCRP00000006351; -.
DR EnsemblFungi; EAA32582; EAA32582; NCU06630.
DR GeneID; 3877966; -.
DR KEGG; ncr:NCU06630; -.
DR VEuPathDB; FungiDB:NCU06630; -.
DR HOGENOM; CLU_004962_0_5_1; -.
DR InParanoid; P48580; -.
DR OMA; EGYNWGQ; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0000278; P:mitotic cell cycle; IBA:GO_Central.
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 Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Metal-binding; Methylation; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..327
FT /note="Serine/threonine-protein phosphatase PP2A catalytic
FT subunit"
FT /id="PRO_0000058870"
FT ACT_SITE 136
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 327
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 37291 MW; 335603AEAB32392B CRC64;
MDTNMEDVGR VPAELTSSNF EPTTIPTLDG WIESLMNCKQ LAESDVQRLC EKAREVLQDE
SNVQPVKCPV TVCGDIHGQF HDLMELFKIG GSCPDTNYLF MGDYVDRGYY SVETVTLLVA
LKIRYPNRIT ILRGNHESRQ ITQVYGFYDE CLRKYGNANV WKYFTDLFDY LPLTALIDNQ
IFCLHGGLSP SIDTLDNIRA LDRIQEVPHE GPMCDLLWSD PDDRCGWGIS PRGAGYTFGQ
DISEAFNHNN GLTLIARAHQ LVMEGYNWSQ DRNVVTIFSA PNYCYRCGNQ AAIMEIDEHL
KYTFLQFDPC PRAGEPMVSR RTPDYFL
