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Reviewed, UniProtKB/Swiss-Prot Q3YYB9 (PIMT_SHISS)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein-L-isoaspartate O-methyltransferase
    EC=2.1.1.77
Alternative name(s):
    Protein-beta-aspartate methyltransferase
      Short name=PIMT
    Protein L-isoaspartyl methyltransferase
    L-isoaspartyl protein carboxyl methyltransferase
Gene names
Name: pcm
Ordered Locus Names: SSON_2891
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 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 modification process

Inferred from electronic annotation. Source: HAMAP

protein 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 – 208208Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090
PRO_1000004828

Sites

Active site591 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3YYB9-1 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 200A9663746255A8

FASTA20823,272
        10         20         30         40         50         60 
MVSRRVQALL EQLRAQGIQD EQVLNALAAV PREKFVDEAF EQKAWDNIAL PIGQGQTISQ 

        70         80         90        100        110        120 
PYMVARMTEL LELTPQSRVL EIGTGSGYQT AILAHLVQHV CSVERIKGLQ WQARRRLKNL 

       130        140        150        160        170        180 
DLHNVSTRHG DGWQGWQARA PFDAIIVTAA PPEIPTALMT QLDEGGILVL PVGEEHQYLK 

       190        200 
RVRRRGGEFI IDTVEAVRFV PLVKGELA 

« Hide

References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000038 Genomic DNA. Translation: AAZ89493.1.
RefSeqYP_311728.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3667577.
GenomeReviewsGene locus SSON_2891 in contig CP000038_GR.
KEGGssn:SSON_2891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3YYB9.
OMAQ3YYB9. KELNYAN.

Enzyme and pathway databases

BioCycSSON300269:SSO_2891-MON.

Family and domain databases

HAMAPMF_00090.
[Tree]
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_SHISS
AccessionPrimary (citable) accession number: Q3YYB9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 27, 2005
Last modified: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents