ID A0A178EHI0_9PLEO Unreviewed; 222 AA.
AC A0A178EHI0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase {ECO:0000256|RuleBase:RU003802};
DE EC=2.1.1.77 {ECO:0000256|RuleBase:RU003802};
GN ORFNames=IQ07DRAFT_584039 {ECO:0000313|EMBL:OAL54881.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL54881.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL54881.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL54881.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KV441638; OAL54881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178EHI0; -.
DR STRING; 765867.A0A178EHI0; -.
DR InParanoid; A0A178EHI0; -.
DR OrthoDB; 303909at2759; -.
DR Proteomes; UP000077535; 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:OAL54881.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU003802};
KW Transferase {ECO:0000256|RuleBase:RU003802, ECO:0000313|EMBL:OAL54881.1}.
SQ SEQUENCE 222 AA; 23791 MW; FEA67F58138802D5 CRC64;
MAWRSSGDSN EALINNLARN GLIKSDRVKE AMLKVDREHY APRRPYEDCP QPIGHRATIS
APHMHANACE SLLTYLQPGA SVLDIGSGSG YLTAVLANLV APGGTVIGID HIQPLVDLAD
ANMGKSEAGR AMLEGGQVRF VAGDGRKGWA EGAPYDAIHV GAAAAEHHQE LTEQLKAPGR
LFVPVEEGNA QYIFVVDKKA DGSVERKKLY GVQYVPLTDA PE
//
