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Database: UniProt
Entry: S6CDF7_POLVA
LinkDB: S6CDF7_POLVA
Original site: S6CDF7_POLVA 
ID   S6CDF7_POLVA            Unreviewed;       231 AA.
AC   S6CDF7;
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=PvPimt2 {ECO:0000313|EMBL:BAN67565.1};
GN   ORFNames=PVAND_016352 {ECO:0000313|EMBL:KAG5668412.1};
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:BAN67565.1};
RN   [1] {ECO:0000313|EMBL:BAN67565.1}
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:KAG5668412.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIAS01 {ECO:0000313|EMBL:KAG5668412.1};
RC   TISSUE=Whole body or cell culture {ECO:0000313|EMBL:KAG5668412.1};
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; AB842108; BAN67565.1; -; mRNA.
DR   EMBL; JADBJN010000004; KAG5668412.1; -; Genomic_DNA.
DR   OrthoDB; 303909at2759; -.
DR   Proteomes; UP001107558; Chromosome 4.
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:BAN67565.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP001107558};
KW   Transferase {ECO:0000313|EMBL:BAN67565.1}.
SQ   SEQUENCE   231 AA;  25318 MW;  8DF779276CCAB360 CRC64;
     MASRLRSESN AGLVQQLQDS GVIKKPIVAE VMKQTDRKHY CRVANPYVDQ PESIGCFATI
     SAPHMHAFAL ENLSEVINAD SKILDIGAGS GYLTACFARL IEAKAKEKNT EPTGIVIAIE
     HQPDLVKFAN ENIKNDDYKL ISDERLKIIQ GDGRIGCIEY GPYDVIHVGA AASETPLELL
     LQLKTGGRML CPVGPQDGEQ NMEQYDKKNS GEVVKDTLTS VMYVPLTDLK V
//
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