ID   LCMT1_NEUCR             Reviewed;         431 AA.
AC   Q7SAP7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Leucine carboxyl methyltransferase 1;
DE            EC=2.1.1.233;
DE   AltName: Full=Protein phosphatase methyltransferase 1;
DE   AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1;
GN   Name=ppm-1; ORFNames=NCU07993;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Methylates the carboxyl group of the C-terminal leucine
CC       residue of protein phosphatase 2A catalytic subunits to form alpha-
CC       leucine ester residues. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-
CC         methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl
CC         ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48544, Rhea:RHEA-
CC         COMP:12134, Rhea:RHEA-COMP:12135, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:90516, ChEBI:CHEBI:90517;
CC         EC=2.1.1.233;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC       {ECO:0000305}.
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DR   EMBL; CM002239; EAA33427.2; -; Genomic_DNA.
DR   RefSeq; XP_962663.2; XM_957570.3.
DR   AlphaFoldDB; Q7SAP7; -.
DR   SMR; Q7SAP7; -.
DR   STRING; 5141.EFNCRP00000008272; -.
DR   EnsemblFungi; EAA33427; EAA33427; NCU07993.
DR   GeneID; 3878802; -.
DR   KEGG; ncr:NCU07993; -.
DR   VEuPathDB; FungiDB:NCU07993; -.
DR   HOGENOM; CLU_031312_1_1_1; -.
DR   InParanoid; Q7SAP7; -.
DR   OMA; IIYEPIR; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0018423; F:protein C-terminal leucine carboxyl O-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006481; P:C-terminal protein methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR016651; PPM1.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR13600; PTHR13600; 1.
DR   Pfam; PF04072; LCM; 1.
DR   PIRSF; PIRSF016305; LCM_mtfrase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..431
FT                   /note="Leucine carboxyl methyltransferase 1"
FT                   /id="PRO_0000226131"
FT   REGION          228..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         103
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         131
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..220
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   431 AA;  46747 MW;  4B9C073E34F0B489 CRC64;
     MSGSAPSIPN LLTLRGRIGG GGVTRGRYRG VIHRGGRGHG PGAPSASAAH DATIQGTDTD
     AAVSRLSAVQ IGYIDDPYAE LFAQSGPGAA RRLPIINRGT YARTTAIDKL VDKFLDDTES
     SPEGRQIVSL GAGTDTRSLR LFSPSAPTPR KRVIYHEIDF PAMCEKKQRI VCSAPQLRSI
     LSDPDSVEEL SQHGGGNSWH SKAVAEKHKG SELWVHGLDL RAIAASQQPQ QPLPPGVPIG
     SRGLHASPFT PGSTTQHEEQ TEETSLPQQR EPLTLTSLNP NLPTLIISEC CLCYLPPSTA
     SSIVSFFTTT IQSSLSIVIY EPIKPDDAFG KMMVSNLAAR EIRMPTLEVY KEAEDQERRL
     REAGFSGGEG KGIGGARSKT IEQIWEEWTS QEEKERVDAL EGLDEVEEWK LLAGHYIVVW
     GWRGVGVDLE I