Reviewed, UniProtKB/Swiss-Prot Q42539 (PIMT_ARATH)

Names and origin

Protein names

Recommended name:
    Protein-L-isoaspartate O-methyltransferase
      Short name=PIMT
    EC=2.1.1.77
Alternative name(s):
    Protein-beta-aspartate methyltransferase
    Protein L-isoaspartyl methyltransferase
    L-isoaspartyl protein carboxyl methyltransferase

Gene names

Name:	PCM
Ordered Locus Names:	At3g48330
ORF Names:	T29H11_150

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	230 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. This enzyme does not act on D-aspartyl residues By similarity.
Catalytic activity	S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Tissue specificity	Highest contents in seeds. Ref.1
Sequence similarities	Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein modification process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 230	230	Protein-L-isoaspartate O-methyltransferase		PRO_0000111882
Sites
	Active site	65	1	By similarity
Experimental info
	Sequence conflict	140	1	G → R in CAB41165. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q42539-1 [UniParc]. Last modified February 5, 2008. Version 3. Checksum: AC7E505605A48B13	FASTA	230	24,614
	10 20 30 40 50 60 MKQFWSPSSI NKNKAMVENL QNHGIVTSDE VAKAMEAVDR GVFVTDRSSA YVDSPMSIGY 70 80 90 100 110 120 NVTISAPHMH AMCLQLLEKH LKPGMRVLDV GSGTGYLTAC FAVMVGTEGR AIGVEHIPEL 130 140 150 160 170 180 VASSVKNIEA SAASPFLKEG SLAVHVGDGR QGWAEFAPYD AIHVGAAAPE IPEALIDQLK 190 200 210 220 230 PGGRLVIPVG NIFQDLQVVD KNSDGSVSIK DETSVRYVPL TSREAQLRGD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A distinctly regulated protein repair L-isoaspartylmethyltransferase from Arabidopsis thaliana." Mudgett M.B., Clarke S. Plant Mol. Biol. 30:723-737(1996) [PubMed: 8624405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Arabidopsis ORF clones." Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U31288 Genomic DNA. Translation: AAC49279.1. AL049659 Genomic DNA. Translation: CAB41165.1. BT029372 mRNA. Translation: ABK32186.1.
IPI	IPI00518020.
PIR	T06709.
RefSeq	NP_680112.2. NP_851013.2.
UniGene	At.3161
3D structure databases
HSSP	HSSP built from PDB template 1KR5 based on UniProtKB P22061.
ModBase	Search...
Proteomic databases
PRIDE	Q42539.
Genome annotation databases
GeneID	823991.
GenomeReviews	Gene locus AT3G48330 in contig BA000014_GR.
KEGG	ath:AT3G48330.
NMPDR	fig|3702.1.peg.16070.
Organism-specific databases
TAIR	At3g48330.
Enzyme and pathway databases
BRENDA	2.1.1.77. 302.
Family and domain databases
InterPro	IPR000682. PCMT. [Graphical view]
PANTHER	PTHR11579. PCMT. 1 hit.
Pfam	PF01135. PCMT. 1 hit. [Graphical view]
TIGRFAMs	TIGR00080. pimt. 1 hit.
PROSITE	PS01279. PCMT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PIMT_ARATH

Accession

Primary (citable) accession number: Q42539
Secondary accession number(s): A0JQ02, Q9STL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 5, 2008
Last modified:	June 16, 2009
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)