LCMT1_ASPFU
ID LCMT1_ASPFU Reviewed; 398 AA.
AC Q4WS57; Q6MYA1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=ppm1; ORFNames=AfA19D12.070, AFUA_1G13930;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA Pain A., Woodward J.R., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA Fosker N., Fraser A., Harris D.E., Larke N., Murphy L.D., Humphray S.,
RA O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M.A.,
RA Salzberg S.L., Saunders D., Seeger K., Sharp S., Warren T., Denning D.W.,
RA Barrell B.G., Hall N.;
RT "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT region encompassing the nitrate assimilation gene cluster.";
RL Fungal Genet. Biol. 41:443-453(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF32102.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; BX649607; CAF32102.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AAHF01000004; EAL90725.1; -; Genomic_DNA.
DR RefSeq; XP_752763.1; XM_747670.1.
DR AlphaFoldDB; Q4WS57; -.
DR SMR; Q4WS57; -.
DR STRING; 746128.CADAFUBP00001320; -.
DR EnsemblFungi; EAL90725; EAL90725; AFUA_1G13930.
DR GeneID; 3510304; -.
DR KEGG; afm:AFUA_1G13930; -.
DR VEuPathDB; FungiDB:Afu1g13930; -.
DR eggNOG; KOG2918; Eukaryota.
DR HOGENOM; CLU_031312_1_1_1; -.
DR InParanoid; Q4WS57; -.
DR OMA; IIYEPIR; -.
DR OrthoDB; 1094856at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
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..398
FT /note="Leucine carboxyl methyltransferase 1"
FT /id="PRO_0000226123"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 201..202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 398 AA; 43370 MW; 62D3009AA70B2F1F CRC64;
MSASQIPNLN TLRRGGGRGR LRGRGGFETG APSEDRHGSR GLAAQDRVVQ GTDNDASVSR
LSAVEIGYLE DPFAKVLTPP GSGTRRLPII NRGTYVRTTA IDRLVARFLE GPSQTKKQII
SLGAGSDTRV FRLLSSRSSA SSSDLIYHEI DFSANTAAKI KFIRAAPLLQ RTLGLGSAQN
VAIPDSGDAL HSPTYHLHPV DLRTLAASGS ATTSRSPSSP NPAEKDQPPC PLQGVDPTLP
TLLISECCLV YLSPREAADV VDYFTKTLFP ASVPLGLIIY EPIRPDDAFG RTMVANLATR
GIQLQTLHEY ASLEAQRRRL REHGLHSGQA AADIDFIWER WVSEAEKERV ARLEMLDEVE
EWQLLARHYC VAWGWTSGAG EDTTVFDGWK EIDGQTGD
