ID M2TE06_COCSN Unreviewed; 376 AA.
AC M2TE06;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 08-NOV-2023, entry version 44.
DE RecName: Full=Protein phosphatase methylesterase 1 {ECO:0000256|ARBA:ARBA00020672, ECO:0000256|PIRNR:PIRNR022950};
DE Short=PME-1 {ECO:0000256|PIRNR:PIRNR022950};
DE EC=3.1.1.- {ECO:0000256|PIRNR:PIRNR022950};
GN ORFNames=COCSADRAFT_82308 {ECO:0000313|EMBL:EMD66977.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD66977.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD66977.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit.
CC {ECO:0000256|ARBA:ARBA00024741}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine methyl ester +
CC H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) +
CC methanol; Xref=Rhea:RHEA:48548, Rhea:RHEA-COMP:12134, Rhea:RHEA-
CC COMP:12135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=3.1.1.89;
CC Evidence={ECO:0000256|ARBA:ARBA00000906};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AKT2 hydrolase
CC family. {ECO:0000256|ARBA:ARBA00005668}.
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DR EMBL; KB445639; EMD66977.1; -; Genomic_DNA.
DR RefSeq; XP_007696752.1; XM_007698562.1.
DR AlphaFoldDB; M2TE06; -.
DR STRING; 665912.M2TE06; -.
DR GeneID; 19140885; -.
DR KEGG; bsc:COCSADRAFT_82308; -.
DR eggNOG; KOG2564; Eukaryota.
DR HOGENOM; CLU_024818_3_0_1; -.
DR OMA; EAHHTSM; -.
DR OrthoDB; 169198at2759; -.
DR Proteomes; UP000016934; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0051723; F:protein methylesterase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR PANTHER; PTHR14189:SF0; PROTEIN PHOSPHATASE METHYLESTERASE 1; 1.
DR PANTHER; PTHR14189; PROTEIN PHOSPHATASE METHYLESTERASE-1 RELATED; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR022950};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000016934};
KW Serine esterase {ECO:0000256|PIRNR:PIRNR022950}.
FT DOMAIN 96..346
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 208
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 334
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
SQ SEQUENCE 376 AA; 41159 MW; 5DDF9912C8BD18B8 CRC64;
MSSLAREFAK TKLSSLPPPE PLQEEPPEYE DDSSSASSMS STGTVRPSNT LRPAPAIHWS
DYFAQEFYLE QDRKSAGHAK FHVYLTPPAS PKAPLIVLHH GAGSSAMTFA LATKEIRKAM
PDIGILAVEA RDHGSVVWDA SGQVDTDLSI AQLSQDLLDM ILLTQAKMGW RDLPTVVLIG
HSLGGAVVTD AANRGLLGNK LMGFGVLDVV EGSAMETLGH MHTYLASRPK SFPSLPAAIE
WHIRSRTLRN PQSARASVPS LLLQTPDGRW AWRTEISSTE PYWENWFTGM SGKFLSGKGA
KLLLLAGTDR LDKELMIGQM QGKFQLQVFP AAGHFLHEDL PEKTAEVIVE FVKRNDRSTL
VLPPKVSDML AQGKRV
//
