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Reviewed, UniProtKB/Swiss-Prot Q8TZR3 (PIMT_PYRFU)

Last modified June 16, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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: PF1922
OrganismPyrococcus furiosus [Complete proteome] [HAMAP]
Taxonomic identifier2261 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein 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 By similarity.

Catalytic activity

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

Subunit structure

Monomer. 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 term3D-structure
Complete 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 – 219219Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090
PRO_0000111923

Sites

Active site651 By similarity

Secondary structure

......................................... 219
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8TZR3-1 [UniParc].

Last modified October 10, 2002. Version 2.
Checksum: A239F32E24C3445D

FASTA21924,617
        10         20         30         40         50         60 
MMDEKELYEK WMRTVEMLKA EGIIRSKEVE RAFLKYPRYL FVEDKYKKYA HIDEPLPIPA 

        70         80         90        100        110        120 
GQTVSAPHMV AIMLEIANLK PGMNILEVGT GSGWNAALIS EIVKTDVYTI ERIPELVEFA 

       130        140        150        160        170        180 
KRNLERAGVK NVHVILGDGS KGFPPKAPYD VIIVTAGAPK IPEPLIEQLK IGGKLIIPVG 

       190        200        210 
SYHLWQELLE VRKTKDGIKI KNHGGVAFVP LIGEYGWKE 

« Hide

References

« Hide 'large scale' references
[1]"The complete sequence of the Pyrococcus furiosus genome."
Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]"Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate."
Griffith S.C., Sawaya M.R., Boutz D.R., Thapar N., Katz J.E., Clarke S., Yeates T.O.
J. Mol. Biol. 313:1103-1116(2001) [PubMed: 11700066] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).

Cross-references

Sequence databases

AE010286 Genomic DNA. Translation: AAL82046.1. Different initiation.
RefSeqNP_579651.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JG1X-ray1.20A1-219[»]
1JG2X-ray1.50A1-219[»]
1JG3X-ray2.10A/B1-219[»]
1JG4X-ray1.50A1-219[»]
ModBaseSearch...

Genome annotation databases

GeneID1469802.
GenomeReviewsGene locus PF1922 in contig AE009950_GR.
KEGGpfu:PF1922.
NMPDRfig|186497.1.peg.1972.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8TZR3.
OMAQ8TZR3. APYDRIY.

Enzyme and pathway databases

BRENDA2.1.1.77. 321.

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_PYRFU
AccessionPrimary (citable) accession number: Q8TZR3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: June 16, 2009
This is version 42 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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