ID A0A0C7N2S1_9SACH Unreviewed; 365 AA.
AC A0A0C7N2S1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=LALA0_S05e02212g {ECO:0000313|EMBL:CEP62290.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP62290.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP62290.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP62290.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. {ECO:0000256|PIRNR:PIRNR022950}.
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 -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC {ECO:0000256|ARBA:ARBA00008645, ECO:0000256|PIRNR:PIRNR022950}.
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DR EMBL; LN736364; CEP62290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7N2S1; -.
DR STRING; 1245769.A0A0C7N2S1; -.
DR HOGENOM; CLU_024818_3_0_1; -.
DR OrthoDB; 169198at2759; -.
DR Proteomes; UP000054304; Unassembled WGS sequence.
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; PF00561; Abhydrolase_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000054304};
KW Serine esterase {ECO:0000256|PIRNR:PIRNR022950}.
FT DOMAIN 82..327
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 199
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 325
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
SQ SEQUENCE 365 AA; 40759 MW; 6F16333F36A7D254 CRC64;
MSDALRRALL AKMEHADTVI QSGTTSESAP KVNPPIDLPS WKDFFDQNET FSIENGDFTF
NSYFTLPTSE SLPKSPASRN IPIFVFHHGA GSSALSFAPL ARSLHEKLGN QCGTFAFDAR
GHGQTKTPDS ASYRLEDFQT DFCQILELFS QRYLARLFTS SNFCLILVGH SLGGSICCSA
FNQFDQFLRQ KIVGVAMLDI VEEAAKKALN TVDTFLAKTP NVFPNYKAAI DWHVQRRLSS
LESSAQICIP SLFTPTESGQ VARITNLTTF RPFWSTWFTG LSSRFVKLPT SKLLILAGDD
NLDRELIIGQ MQGKFQLVVF QDSGHFIEED CPAKTALTLI DFWQRNDVKN VRIKTNWSKK
GSPTP
//
