ID D2VR44_NAEGR Unreviewed; 433 AA.
AC D2VR44;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Protein phosphatase methylesterase 1 {ECO:0000256|PIRNR:PIRNR022950};
DE Short=PME-1 {ECO:0000256|PIRNR:PIRNR022950};
DE EC=3.1.1.- {ECO:0000256|PIRNR:PIRNR022950};
GN ORFNames=NAEGRDRAFT_71456 {ECO:0000313|EMBL:EFC40742.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC40742.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC40742.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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; GG738890; EFC40742.1; -; Genomic_DNA.
DR RefSeq; XP_002673486.1; XM_002673440.1.
DR AlphaFoldDB; D2VR44; -.
DR STRING; 5762.D2VR44; -.
DR ESTHER; naegr-d2vr44; PPase_methylesterase_euk.
DR EnsemblProtists; EFC40742; EFC40742; NAEGRDRAFT_71456.
DR GeneID; 8864576; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_71456; -.
DR eggNOG; KOG2564; Eukaryota.
DR InParanoid; D2VR44; -.
DR OrthoDB; 169198at2759; -.
DR Proteomes; UP000006671; 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; PF12697; Abhydrolase_6; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR022950};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Serine esterase {ECO:0000256|PIRNR:PIRNR022950}.
FT DOMAIN 127..418
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF12697"
FT REGION 1..49
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 242
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 283
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
SQ SEQUENCE 433 AA; 48734 MW; F41776829FD4BD3E CRC64;
MERNLFKRKV TENQSSSSSP SSPPTMSPPS RPTSFIPKHT SSSFSDNRIS SSIQQQNDEA
FKPEVDYASH GLEQHDVAVE GRGVFRMYTM NHLHHQNTNN EQSNTNTTTT TSLPAHLIKT
RKCESVLVFI HGAGLSSLSW TLCMQNLRQL VIRSGNTNNV NINFMRSPPT PIEMGMGQPK
SASEAFNVDD YEYCAMDLRG HGASHTEKDS ELSIDTLVDD IIALLQQVYR GKKRNFILIG
HSLGGSIAVR CAHKMDIIEE QETKSGTVQS HELMTVKGVV VIDMVEGSAL TSLPNTKKFI
ESRPNKFKNM ESAIKWSIQH GVVNNISSAV ISIPSQLMHV EEGNYYTWRT NLTDSEEYWT
AWFTDMSQIF LEVKGLKLLM ITSTDILDKE LTIAQMQGKF QMKVLNRSGH CIQEDDPAHC
SEVIFSFLHR FRL
//
