PP2A2_BLUHO
ID PP2A2_BLUHO Reviewed; 328 AA.
AC Q8X178;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-2 catalytic subunit;
DE EC=3.1.3.16;
GN Name=PP2A-2;
OS Blumeria hordei (Barley powdery mildew) (Blumeria graminis f. sp. hordei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=2867405;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhang Z., Scott P., Gurr S.J.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF462042; AAL69898.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8X178; -.
DR SMR; Q8X178; -.
DR PRIDE; Q8X178; -.
DR EnsemblFungi; BLGH_03799-mRNA-1; BLGH_03799-mRNA-1; BLGH_03799.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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.
FT CHAIN 1..328
FT /note="Serine/threonine-protein phosphatase PP2A-2
FT catalytic subunit"
FT /id="PRO_0000058869"
FT ACT_SITE 137
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 328
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250"
SQ SEQUENCE 328 AA; 37486 MW; C5339E5D238618AE CRC64;
MDTKMEDVGK TPEPIRFQTT TEPASISTLD GWIENLMACK QLPEVDVLRL CEKAREVLHS
ESNVQPVKCP VTVCGDIHGQ FHDLMELFRI GGPNPDTNYL FMGDYVDRGY YSVETVTLLV
ALKIRYPQRI TILRGNHESR QITQVYGFYD ECLRKYGNAN VWKYFTNLFD FLPLTALIEN
QIFCLHGGLS PSIDTLDNIK SLDRIQEVPH EGPMCDLLWS DPDDRCGWGI SPRGAGYTFG
QDISEAFNHN NGLTLVARAH QLVMEGYNWS QDRNVVTIFS APNYCYRCGN QAAIMEIDEH
LKYTFLQFDP CPRAGEPMVT RRTPDYFL
