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Q3YYB9 (PIMT_SHISS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:SSON_2891
OrganismShigella sonnei (strain Ss046) [Complete proteome] [HAMAP]
Taxonomic identifier300269 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length208 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 MF_00090

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 HAMAP MF_00090.

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)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity

Inferred from electronic annotation. Source: EC

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 [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].
Strain: Ss046.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000038 Genomic DNA. Translation: AAZ89493.1.
RefSeqYP_311728.1. NC_007384.1.

3D structure databases

ProteinModelPortalQ3YYB9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3YYB9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000098879; EBESCP00000094908; EBESCG00000097923.
GeneID3667577.
GenomeReviewsGene locus SSON_2891 in contig CP000038_GR.
KEGGssn:SSON_2891.
PATRIC18740278. VBIShiSon107113_3448.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2518.
GeneTreeEBGT00050000011550.
HOGENOMHBG699907.
OMAYMVARMS.
PhylomeDBQ3YYB9.
ProtClustDBPRK00312.

Enzyme and pathway databases

BioCycSSON300269:SSO_2891-MONOMER.

Family and domain databases

HAMAPMF_00090. PIMT.
[Tree]
InterProIPR000682. PCMT.
[Graphical view]
KOK00573.
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: January 25, 2012
This is version 44 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