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Q8TZR3 (PIMT_PYRFU) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:PF1922
OrganismPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifier186497 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
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. 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

Subunit structure

Monomer.

Subcellular location

Cytoplasm By similarity HAMAP MF_00090.

Sequence similarities

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

Sequence caution

The sequence AAL82046.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference 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 – 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 [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]"Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
Genetics 152:1299-1305(1999) [PubMed: 10430560] [Abstract]
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

EMBL
GenBank
DDBJ
AE009950 Genomic DNA. Translation: AAL82046.1. Different initiation.
RefSeqNP_579651.1. NC_003413.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JG1X-ray1.20A1-219[»]
1JG2X-ray1.50A1-219[»]
1JG3X-ray2.10A/B1-219[»]
1JG4X-ray1.50A1-219[»]
ProteinModelPortalQ8TZR3.
SMRQ8TZR3. Positions 4-218.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000005126; EBPYRP00000004987; EBPYRG00000005125.
GeneID1469802.
GenomeReviewsGene locus PF1922 in contig AE009950_GR.
KEGGpfu:PF1922.
NMPDRfig|186497.1.peg.1972.

Phylogenomic databases

GeneTreeEBGT00050000023051.
HOGENOMHBG699907.
OMAGYHAAVV.
PhylomeDBQ8TZR3.
ProtClustDBPRK00312.

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_PYRFU
AccessionPrimary (citable) accession number: Q8TZR3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: December 14, 2011
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families