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Reviewed, UniProtKB/Swiss-Prot Q8PW90 (PIMT_METMA)

Last modified June 16, 2009. Version 49. 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: MM_1706
OrganismMethanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier2209 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length243 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 – 243243Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090
PRO_0000111918

Sites

Active site871 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PW90-1 [UniParc].

Last modified October 10, 2002. Version 1.
Checksum: DF83E0D0591A1B1C

FASTA24327,120
        10         20         30         40         50         60 
MPERRGIVLV NAVSEKDLGE DKRKREKEKE CEKLRKLLVE GLEGFVIDEK VLQAMLRVPR 

        70         80         90        100        110        120 
HRFVPEYEQR AAYVDMPLEI GHGQTISAPH MVAMMCEILE LAEGHKVLEI GAGSGYNAAV 

       130        140        150        160        170        180 
MSELVGKTGH IYTVERVEPL ANFAKKNLKE AGYKNVTVLL ENGSMGYPGY APYDRIAVTC 

       190        200        210        220        230        240 
AAPNIPETLL EQLKPGGIMV IPVGSYSQEL IRVKKDSTGK IYRKKKGDVI FVPMIGKHGF 


RRI 

« Hide

References

[1]"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea."
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. expand/collapse author list , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases

AE008384 Genomic DNA. Translation: AAM31402.1.
RefSeqNP_633730.1.

3D structure databases

HSSPHSSP built from PDB template 1JG1 based on UniProtKB Q8TZR3.
ModBaseSearch...

Genome annotation databases

GeneID1480048.
GenomeReviewsGene locus MM_1706 in contig AE008384_GR.
KEGGmma:MM_1706.
NMPDRfig|192952.1.peg.1706.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8PW90.
OMAQ8PW90. RERFAPP.

Enzyme and pathway databases

BioCycMMAZ192952:MM1706-MON.
BRENDA2.1.1.77. 261165.

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_METMA
AccessionPrimary (citable) accession number: Q8PW90
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: June 16, 2009
This is version 49 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