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Q42539 (PIMT_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Protein-L-isoaspartate O-methyltransferase
Short name=PIMT
EC=2.1.1.77
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl methyltransferase
Protein-beta-aspartate methyltransferase
Gene names
Name:PCM
Ordered Locus Names:At3g48330
ORF Names:T29H11_150
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceEvidence 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 methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Protein-L-isoaspartate O-methyltransferase
PRO_0000111882

Sites

Active site651 By similarity

Experimental info

Sequence conflict1401G → R in CAB41165. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q42539 [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: AC7E505605A48B13

FASTA23024,614
        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

« Hide

References

« Hide '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. expand/collapse author list , 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]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U31288 Genomic DNA. Translation: AAC49279.1.
AL049659 Genomic DNA. Translation: CAB41165.1.
CP002686 Genomic DNA. Translation: AEE78401.1.
CP002686 Genomic DNA. Translation: AEE78402.1.
BT029372 mRNA. Translation: ABK32186.1.
IPIIPI00518020.
PIRT06709.
RefSeqNP_680112.2. NM_148859.4.
NP_851013.2. NM_180682.3.
UniGeneAt.3161.
At.70492.

3D structure databases

ProteinModelPortalQ42539.
SMRQ42539. Positions 5-228.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ42539.

Proteomic databases

PRIDEQ42539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G48330.1; AT3G48330.1; AT3G48330.
AT3G48330.2; AT3G48330.2; AT3G48330.
GeneID823991.
GenomeReviewsGene locus AT3G48330 in contig BA000014_GR.
KEGGath:AT3G48330.
NMPDRfig|3702.1.peg.16070.

Organism-specific databases

TAIRAt3g48330.

Phylogenomic databases

eggNOGKOG1661.
GeneTreeEPGT00050000011986.
HOGENOMHBG699907.
InParanoidQ42539.
PhylomeDBQ42539.
ProtClustDBCLSN2708507.

Gene expression databases

GenevestigatorQ42539.

Family and domain databases

InterProIPR000682. PCMT.
[Graphical view]
PANTHERPTHR11579. PCMT. 1 hit.
PfamPF01135. PCMT. 1 hit.
[Graphical view]
TIGRFAMsTIGR00080. Pimt. 1 hit.
PROSITEPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePIMT_ARATH
AccessionPrimary (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: December 14, 2011
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents