ID   PIMT_ARATH              Reviewed;         230 AA.
AC   Q42539; A0JQ02; Q9STL3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 3.
DT   16-JUN-2009, entry version 73.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE            Short=PIMT;
DE            EC=2.1.1.77;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
GN   Name=PCM; OrderedLocusNames=At3g48330; ORFNames=T29H11_150;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   MEDLINE=96194456; PubMed=8624405; DOI=10.1007/BF00019007;
RA   Mudgett M.B., Clarke S.;
RT   "A distinctly regulated protein repair L-isoaspartylmethyltransferase
RT   from Arabidopsis thaliana.";
RL   Plant Mol. Biol. 30:723-737(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl
CC       residues in peptides and proteins that result from spontaneous
CC       decomposition of normal L-aspartyl and L-asparaginyl residues. It
CC       plays a role in the repair and/or degradation of damaged proteins.
CC       This enzyme does not act on D-aspartyl residues (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-
CC       isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate
CC       alpha-methyl ester.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highest contents in seeds.
CC   -!- SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein
CC       methyltransferase family.
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DR   EMBL; U31288; AAC49279.1; -; Genomic_DNA.
DR   EMBL; AL049659; CAB41165.1; -; Genomic_DNA.
DR   EMBL; BT029372; ABK32186.1; -; mRNA.
DR   IPI; IPI00518020; -.
DR   PIR; T06709; T06709.
DR   RefSeq; NP_680112.2; -.
DR   RefSeq; NP_851013.2; -.
DR   UniGene; At.3161; -.
DR   HSSP; P22061; 1KR5.
DR   PRIDE; Q42539; -.
DR   GeneID; 823991; -.
DR   GenomeReviews; BA000014_GR; AT3G48330.
DR   KEGG; ath:AT3G48330; -.
DR   NMPDR; fig|3702.1.peg.16070; -.
DR   TAIR; At3g48330; -.
DR   BRENDA; 2.1.1.77; 302.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-meth...; IEA:EC.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000682; PCMT.
DR   PANTHER; PTHR11579; PCMT; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   TIGRFAMs; TIGR00080; pimt; 1.
DR   PROSITE; PS01279; PCMT; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    230       Protein-L-isoaspartate O-
FT                                methyltransferase.
FT                                /FTId=PRO_0000111882.
FT   ACT_SITE     65     65       By similarity.
FT   CONFLICT    140    140       G -> R (in Ref. 2; CAB41165).
SQ   SEQUENCE   230 AA;  24614 MW;  AC7E505605A48B13 CRC64;
     MKQFWSPSSI NKNKAMVENL QNHGIVTSDE VAKAMEAVDR GVFVTDRSSA YVDSPMSIGY
     NVTISAPHMH AMCLQLLEKH LKPGMRVLDV GSGTGYLTAC FAVMVGTEGR AIGVEHIPEL
     VASSVKNIEA SAASPFLKEG SLAVHVGDGR QGWAEFAPYD AIHVGAAAPE IPEALIDQLK
     PGGRLVIPVG NIFQDLQVVD KNSDGSVSIK DETSVRYVPL TSREAQLRGD
//