ID A0A1V9ZT15_9STRA Unreviewed; 507 AA.
AC A0A1V9ZT15;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=[phosphatase 2A protein]-leucine-carboxy methyltransferase {ECO:0000256|ARBA:ARBA00012834};
DE EC=2.1.1.233 {ECO:0000256|ARBA:ARBA00012834};
DE AltName: Full=[Phosphatase 2A protein]-leucine-carboxy methyltransferase 1 {ECO:0000256|ARBA:ARBA00032526};
GN ORFNames=ACHHYP_01753 {ECO:0000313|EMBL:OQS01147.1};
OS Achlya hypogyna.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Achlya.
OX NCBI_TaxID=1202772 {ECO:0000313|EMBL:OQS01147.1, ECO:0000313|Proteomes:UP000243579};
RN [1] {ECO:0000313|EMBL:OQS01147.1, ECO:0000313|Proteomes:UP000243579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 48635 {ECO:0000313|EMBL:OQS01147.1,
RC ECO:0000313|Proteomes:UP000243579};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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; Evidence={ECO:0000256|ARBA:ARBA00000724};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. LCMT family.
CC {ECO:0000256|ARBA:ARBA00010703}.
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:OQS01147.1}.
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DR EMBL; JNBR01000013; OQS01147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9ZT15; -.
DR STRING; 1202772.A0A1V9ZT15; -.
DR OrthoDB; 5472060at2759; -.
DR Proteomes; UP000243579; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:InterPro.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR016651; PPM1.
DR InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR13600; LEUCINE CARBOXYL METHYLTRANSFERASE; 1.
DR PANTHER; PTHR13600:SF21; LEUCINE CARBOXYL METHYLTRANSFERASE 1; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF04072; LCM; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000243579}.
FT DOMAIN 347..505
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 507 AA; 55863 MW; 0591588D3B9DA97A CRC64;
MAEFAQTSDH GVAETAFDAI HCKISAVKQG YFHDDFVALF GRKPTRRIPL IHRGYYLRHK
AVEAAVSSFL AERATPTTPV QILSFGAGFD TLFFRLRQQH AAHVSMYEID CDAIVDQKIT
VLTQHFDQLF GGSFEQSTPW PHAYKAASAT ATYAVTGCDL GDTAALAKQL AQLGLDPTRP
TLVLAECVLA YLAPSARSSL LQWTASHLSD ALFVGYDPIG LATSFGEQMQ SYFAAKGCDL
RSAKALPSVH DQDAHFRAHG WGSVRLWNMN ATLRLLVADN ERRRMEGLEP FDEYDDWITC
NHHYGFTMAS NNAVDGASVG AAVLREWRLP TLALDEAVIT DTYADGVTVR LFQPTDAPAV
RHIFESTLDE YNHKSVRKLV AHQLATELSD LVASYMSQPS ACFWVAERGS DFLGCVGVKP
FKGAATAELL RLRVAGSGRR LGVATRLVDA LEGYCRRVGY ETVYLETLSV MEAAQAFYAK
RGYTHVGSTR VGKPPADFGL EQFQLRL
//
