ID S6BNE1_POLVA Unreviewed; 229 AA.
AC S6BNE1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=protein-L-isoaspartate(D-aspartate) O-methyltransferase {ECO:0000256|ARBA:ARBA00011890};
DE EC=2.1.1.77 {ECO:0000256|ARBA:ARBA00011890};
GN Name=PvPimt1 {ECO:0000313|EMBL:BAN67564.1};
GN ORFNames=PVAND_006694 {ECO:0000313|EMBL:KAG5676890.1};
OS Polypedilum vanderplanki (Sleeping chironomid midge).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Chironominae; Polypedilum; Polypedilum.
OX NCBI_TaxID=319348 {ECO:0000313|EMBL:BAN67564.1};
RN [1] {ECO:0000313|EMBL:BAN67564.1}
RP NUCLEOTIDE SEQUENCE.
RA Gusev O., Suetsugu Y., Cornette R., Kawashima T., Logacheva M.,
RA Kondrashev A., Penin A., Hatanaka R., Kikuta S., Shimura S., Katayose Y.,
RA Matsumoto T., Shagimardanova E., Alexeev D., Govorun V., Wisecaver J.,
RA Mikheyev A., Koyanagi R., Nishiyama T., Shigenobu S., Shibata T.F.,
RA Hasebe M., Okuda T., Satoh N., Kikawada T.;
RT "Functional and evolutionary insights for the origin and mechanisms of
RT complete desiccation tolerance from genome of the sleeping chironomid
RT Polypedilum vanderplanki.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAG5676890.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIAS01 {ECO:0000313|EMBL:KAG5676890.1};
RC TISSUE=Whole body or cell culture {ECO:0000313|EMBL:KAG5676890.1};
RA Yoshida Y., Kikawada T., Gusev O.;
RT "Chromosome level genome of the anhydrobiotic midge Polypedilum
RT vanderplanki.";
RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00005369}.
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DR EMBL; AB842107; BAN67564.1; -; mRNA.
DR EMBL; JADBJN010000002; KAG5676890.1; -; Genomic_DNA.
DR OrthoDB; 303909at2759; -.
DR Proteomes; UP001107558; Chromosome 2.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
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.
PE 2: Evidence at transcript level;
KW Methyltransferase {ECO:0000313|EMBL:BAN67564.1};
KW Reference proteome {ECO:0000313|Proteomes:UP001107558};
KW Transferase {ECO:0000313|EMBL:BAN67564.1}.
SQ SEQUENCE 229 AA; 25237 MW; DCA6A7E76FB6953F CRC64;
MAWRSQSDSN EGLIQQLKEN GIIKNEMVAN AMKMTDRKLY CRVAYPYVDR PHSIGFSATI
SAPHMHAFAL ENLFDFIKPG CRILDVGSGS GFLTACFSRL IDAKSVNSNE KSLVIGIEHH
PKLVEFSIGN LNSDDIKFIE EGKIKIIQGD GRLGCKEFAP YDCIHVGAAA ADIPSELLNQ
LKPNGRLLCP VGLAGETQQM EQYDKTASGE IMKKTLMSVV YVPLTDLNE
//
