ID S6BND7_POLVA Unreviewed; 276 AA.
AC S6BND7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=PvPimt3 {ECO:0000313|EMBL:BAN67559.1};
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:BAN67559.1};
RN [1] {ECO:0000313|EMBL:BAN67559.1}
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.
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; AB842102; BAN67559.1; -; mRNA.
DR AlphaFoldDB; S6BND7; -.
DR OrthoDB; 303909at2759; -.
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 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:BAN67559.1};
KW Transferase {ECO:0000313|EMBL:BAN67559.1}.
FT REGION 232..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 31202 MW; D306542FB978AE23 CRC64;
MALQLQSDSN TDFIKKLQDF GVIKHKIVAT AMKETDRKYY SNLPSPYVDR LEIIDANAVL
SAPHMHAYAL EKLVDRIRHD SKILDIGSGS GYLTACFARL IQERAFEKLQ IASGFVIAIE
PHERVYKHSI ENILTDNSEL IMSGLIKIFH GDGKKEIEQY EPFDIIHVGA ALSEIPTDLL
MHLNLNGRLI CPVGDKDGEQ QMMQFDKNSA GEVSKKVLTK VIFDPLKATP VEYSHSEESS
LDEQPWTDTT DDESEWSEHN KTPTSDLNEP EFVLKE
//
