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Q8PW90 (PIMT_METMA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:MM_1706
OrganismMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP]
Taxonomic identifier192952 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

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

Sites

Active site871 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8PW90 [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 11833 / OCM 88.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008384 Genomic DNA. Translation: AAM31402.1.
RefSeqNP_633730.1. NC_003901.1.

3D structure databases

ProteinModelPortalQ8PW90.
SMRQ8PW90. Positions 38-241.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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

HOGENOMHBG699907.
OMAMGAKEDL.
PhylomeDBQ8PW90.
ProtClustDBPRK13942.

Enzyme and pathway databases

BioCycMMAZ192952:MM1706-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_METMA
AccessionPrimary (citable) accession number: Q8PW90
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: December 14, 2011
This is version 66 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