Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q1QU77 (PIMT_CHRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein-L-isoaspartate O-methyltransferase

EC=2.1.1.77
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl methyltransferase
Protein-beta-aspartate methyltransferase
Short name=PIMT
Gene names
Name:pcm
Ordered Locus Names:Csal_2634
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

Protein attributes

Sequence length229 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00090

Catalytic activity

S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. HAMAP-Rule MF_00090

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein repair

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 229229Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090
PRO_0000351847

Sites

Active site781 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QU77 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 0F780E9BFB82B32B

FASTA22925,661
        10         20         30         40         50         60 
MHCRIPDTQD THRLGGIGMT SQRTRNRLIR RLQANGIRDT RVLETMAREP RHLFVDEALA 

        70         80         90        100        110        120 
HRAYEDTALP LGHGQTLSQP WIVARMTELV LTARPRRVLE VGTGSGYQTL ILARLVEAVW 

       130        140        150        160        170        180 
SIERIGALHQ RAAARLAMLG ADNVRLRHED GGHGWPQAAP YDVILLTACA SVLPPELLAQ 

       190        200        210        220 
LADGGELIAP LEDDAGRQWL TRVRRCGITF ERTRLERVRF VPLLEGVIQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000285 Genomic DNA. Translation: ABE59981.1.
RefSeqYP_574680.1. NC_007963.1.

3D structure databases

ProteinModelPortalQ1QU77.
ModBaseSearch...

Protein-protein interaction databases

STRING290398.Csal_2634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE59981; ABE59981; Csal_2634.
GeneID4028162.
KEGGcsa:Csal_2634.
PATRIC21449124. VBIChrSal113723_2649.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2518.
HOGENOMHOG000257189.
KOK00573.
OMAVRARMVQ.

Family and domain databases

HAMAPMF_00090. PIMT.
InterProIPR000682. PCMT.
[Graphical view]
PANTHERPTHR11579. PTHR11579. 1 hit.
PfamPF01135. PCMT. 1 hit.
[Graphical view]
TIGRFAMsTIGR00080. pimt. 1 hit.
PROSITEPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePIMT_CHRSD
AccessionPrimary (citable) accession number: Q1QU77
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: May 16, 2006
Last modified: May 1, 2013
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families