GenomeNet

Database: UniProt
Entry: G1XB58_ARTOA
LinkDB: G1XB58_ARTOA
Original site: G1XB58_ARTOA 
ID   G1XB58_ARTOA            Unreviewed;       429 AA.
AC   G1XB58;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=AOL_s00078g155 {ECO:0000313|EMBL:EGX49666.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Orbilia; Orbilia oligospora.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX49666.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX49666.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L., Luo Y.,
RA   Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L., Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008645, ECO:0000256|PIRNR:PIRNR022950}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGX49666.1}.
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; ADOT01000133; EGX49666.1; -; Genomic_DNA.
DR   RefSeq; XP_011121720.1; XM_011123418.1.
DR   AlphaFoldDB; G1XB58; -.
DR   STRING; 756982.G1XB58; -.
DR   GeneID; 22892613; -.
DR   eggNOG; KOG2564; Eukaryota.
DR   HOGENOM; CLU_024818_3_0_1; -.
DR   InParanoid; G1XB58; -.
DR   OMA; EAHHTSM; -.
DR   OrthoDB; 169198at2759; -.
DR   Proteomes; UP000008784; 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; 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:UP000008784};
KW   Serine esterase {ECO:0000256|PIRNR:PIRNR022950}.
FT   DOMAIN          134..405
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
FT   REGION          15..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..52
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..81
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        215
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
SQ   SEQUENCE   429 AA;  46727 MW;  5C6383795D4ECAF4 CRC64;
     MSALGRDFFK AKLAKLPAMP PPPLGALPEE LEELEELDIE DEDEDDFPDG YGENDEYHEG
     VLDDSSSASS ASSTSTIIAP PSRPELTARR RNNLEPIPWN HHFSENLQLT PSSNPTSHFN
     AYYTPNTGSG PLFVTHHGAG SSGLSFAALA SEIRKINPEA GIFSFDARGH GGTSTSNDQD
     FSLSTLSTDL YEALLAAQEQ LRWESLPPII LVGHSLGGAV ITDLAKRGLL GDRLLAYAVL
     DVVEGSAMDA LHSMQSYLLS RPTGFTSLNQ GIEWHVRSRT IRNGRSARVS VPALLYDYSN
     SGGSGDVSSS SSTATANSGA AAVGSNSRPW RWRTDLATTQ PFWQDWFVGL SRKFLEAKGG
     KLLILAGTDR LDKELIIGQM QGKYQLLVLP EVGHFLHEDA PEKTAIALVE FYKRNDRSAL
     VLPKKVWEM
//
DBGET integrated database retrieval system