GenomeNet

Database: UniProt
Entry: A0A0G4LCK3_9PEZI
LinkDB: A0A0G4LCK3_9PEZI
Original site: A0A0G4LCK3_9PEZI 
ID   A0A0G4LCK3_9PEZI        Unreviewed;       415 AA.
AC   A0A0G4LCK3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   08-NOV-2023, entry version 22.
DE   RecName: Full=Protein phosphatase methylesterase 1 {ECO:0000256|ARBA:ARBA00020672};
DE            EC=3.1.1.89 {ECO:0000256|ARBA:ARBA00013111};
DE   Flags: Fragment;
GN   ORFNames=BN1708_000406 {ECO:0000313|EMBL:CRK19741.1}, HYQ45_013430
GN   {ECO:0000313|EMBL:KAG7125026.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK19741.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK19741.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK19741.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAG7125026.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Vl32 {ECO:0000313|EMBL:KAG7125026.1};
RX   PubMed=33955130;
RA   Harting R., Starke J., Kusch H., Poggeler S., Maurus I., Schluter R.,
RA   Landesfeind M., Bulla I., Nowrousian M., de Jonge R., Stahlhut G.,
RA   Hoff K.J., Asshauer K.P., Thurmer A., Stanke M., Daniel R., Morgenstern B.,
RA   Thomma B.P.H.J., Kronstad J.W., Braus-Stromeyer S.A., Braus G.H.;
RT   "A 20-kb lineage-specific genomic region tames virulence in pathogenic
RT   amphidiploid Verticillium longisporum.";
RL   Mol. Plant Pathol. 0:0-0(2021).
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}.
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; CVQH01011112; CRK19741.1; -; Genomic_DNA.
DR   EMBL; JAEMWZ010000322; KAG7125026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4LCK3; -.
DR   STRING; 100787.A0A0G4LCK3; -.
DR   OrthoDB; 169198at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   Proteomes; UP000689129; 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   Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT   DOMAIN          117..384
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
FT   REGION          1..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        373
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   NON_TER         415
FT                   /evidence="ECO:0000313|EMBL:CRK19741.1"
SQ   SEQUENCE   415 AA;  44594 MW;  C823316361EBC3A6 CRC64;
     MSDLQRAWAK RKVDAIPEPF DELPDDDADE LSELPDHLDD GDSSSASSAS STGTIIPSPS
     QRLFARPGAA LSRPGRSWEP VPWTTYFERE LFLEHDATTT YHAYLTSPSP QGGPLFVAHH
     GAGSSALSFA LVAAEIRRAL PHAGFLSLDA RGHGATVTPD QDRPDLSLPT LTADLAAVIA
     LTARRMAWPA DALPPMVLVG HSLGGAVITS LAADPPPDLA PRLLGHAVLD VVEGSAMDAL
     QSMHAYLSTR PAGFTSIEAA IEWHVRSRTV RNALSARTSV PALLVERVAA AADTEADTGS
     RAQTSARPWR WRTDLAATQP FWEGWFTGLS ARFLAARGGK LLLLAGTDRL DTTLTIGQVQ
     GRYALQVFPE AGHFIHEDLP EKTAVALVDF FRRNDRGALV LPPKVGDLLR QGKRV
//
DBGET integrated database retrieval system