Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0B9U1 (PIMT_METTP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. 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:Mthe_1699
OrganismMethanosaeta thermophila (strain DSM 6194 / PT) (Methanothrix thermophila (strain DSM 6194 / PT)) [Complete proteome] [HAMAP]
Taxonomic identifier349307 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosaetaceaeMethanosaeta

Protein attributes

Sequence length210 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-Rule MF_00090

Catalytic activity

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

Subcellular location

Cytoplasm By similarity.

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)
   Biological_processprotein 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 – 210210Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090
PRO_0000351971

Sites

Active site541 By similarity

Sequences

Sequence LengthMass (Da)Tools
A0B9U1 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: EE2612274DE1F2F4

FASTA21023,568
        10         20         30         40         50         60 
MRKERLIESL RNYVSERVVE AMSRVPRELF VPEELRPMAY EDRPLPIGHG QTISAPHMVA 

        70         80         90        100        110        120 
MMCDLLDLRE GMKVLEVGGG CGYHAAVMAE LVGPSGHVYS VERIPELVEM ARRNLERARY 

       130        140        150        160        170        180 
RNVSMILGDG TLGYSEQAPY DRISVAASAP DIPEPLKEQL RPGGRMVIPV GSYSQDLLVV 

       190        200        210 
TKNHDIRVER AMGVIFVPLI GKYGFKDSFW 

« Hide

References

[1]"Complete sequence of Methanosaeta thermophila PT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Smith K.S., Ingram-Smith C., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6194 / PT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000477 Genomic DNA. Translation: ABK15465.1.
RefSeqYP_844105.1. NC_008553.1.

3D structure databases

ProteinModelPortalA0B9U1.
SMRA0B9U1. Positions 4-206.
ModBaseSearch...

Protein-protein interaction databases

STRING349307.Mthe_1699.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK15465; ABK15465; Mthe_1699.
GeneID4463451.
KEGGmtp:Mthe_1699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2518.
HOGENOMHOG000257189.
KOK00573.
OMARILFSAC.

Enzyme and pathway databases

BioCycMMET349307:GHKI-1748-MONOMER.

Family and domain databases

HAMAPMF_00090. PIMT.
InterProIPR000682. PCMT.
[Graphical view]
PANTHERPTHR11579. PTHR11579. 1 hit.
PfamPF01135. PCMT. 1 hit.
[Graphical view]
TIGRFAMsTIGR00080. pimt. 1 hit.
PROSITEPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePIMT_METTP
AccessionPrimary (citable) accession number: A0B9U1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: November 28, 2006
Last modified: May 1, 2013
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