ID A0A0A2J5E1_PENEN Unreviewed; 257 AA.
AC A0A0A2J5E1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|RuleBase:RU003802};
DE EC=2.1.1.77 {ECO:0000256|RuleBase:RU003802};
GN ORFNames=PEX2_037530 {ECO:0000313|EMBL:KGO50602.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO50602.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO50602.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO50602.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine =
CC [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-
CC COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596,
CC ChEBI:CHEBI:90598; EC=2.1.1.77;
CC Evidence={ECO:0000256|RuleBase:RU003802};
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369, ECO:0000256|RuleBase:RU003802}.
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:KGO50602.1}.
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; JQFZ01000329; KGO50602.1; -; Genomic_DNA.
DR RefSeq; XP_016593789.1; XM_016741028.1.
DR AlphaFoldDB; A0A0A2J5E1; -.
DR STRING; 27334.A0A0A2J5E1; -.
DR GeneID; 27676447; -.
DR HOGENOM; CLU_055432_0_0_1; -.
DR OrthoDB; 303909at2759; -.
DR PhylomeDB; A0A0A2J5E1; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00080; pimt; 1.
DR PANTHER; PTHR11579; PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11579:SF0; PROTEIN-L-ISOASPARTATE(D-ASPARTATE) O-METHYLTRANSFERASE; 1.
DR Pfam; PF01135; PCMT; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|RuleBase:RU003802,
KW ECO:0000313|EMBL:KGO50602.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW Transferase {ECO:0000256|RuleBase:RU003802, ECO:0000313|EMBL:KGO50602.1}.
SQ SEQUENCE 257 AA; 27928 MW; BA0A372880AEFE6E CRC64;
MLNLRIKPKF SLSKATQATM AWYCSGSTNT ELIENLFKAG LIHNERVKDA MIGVDRAHYA
PSRPYSDSPQ PIGYGATISA PHMHGHACEY LIDYLKPGAR VLDIGSGSGY LTHVLANLVT
SSSSNAQGQV IGIDHIPELT DLARTNMDKS KQGSELQTST TVKFITGDGR LGWKEGAPYD
AIHVGAAADK LHPTLVDQLR APGRLFIPVE SEDDESAMDS LSGGQYIWVV DKKEDGSIRK
EKVFQVSYVP LTDAPRG
//
