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Q0A7L5 (PIMT_ALHEH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 47. 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:Mlg_1828
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length221 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 – 221221Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090
PRO_0000351811

Sites

Active site701 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A7L5 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: E828CC9C2CBAC15A

FASTA22124,679
        10         20         30         40         50         60 
MDPNRYQGIG MTSRRTRERL VSRLAEEGIR DPRVLQAILE VPRHLFVDEA LASRAYDNTP 

        70         80         90        100        110        120 
LPIGHGQTIS QPWVVARMTE LLIEQSIPER VLELGTGSGY QAAVLAYLGV EVYTIERIKA 

       130        140        150        160        170        180 
LADQARQRMR DLRLHRVHVR YGDGSEGWAQ HAPYQGIIVT AAPEEVPDPL WDQLDEGGRL 

       190        200        210        220 
VAPLGGAGRP QELVLIERVD GELRRRHVAS VSFVPLLGGC R 

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MLHE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000453 Genomic DNA. Translation: ABI57172.1.
RefSeqYP_742662.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0A7L5.
ModBaseSearch...

Protein-protein interaction databases

STRING187272.Mlg_1828.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI57172; ABI57172; Mlg_1828.
GeneID4268183.
KEGGaeh:Mlg_1828.
PATRIC20862913. VBIAlkEhr114327_1827.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2518.
HOGENOMHOG000257189.
KOK00573.
OMAVRARMVQ.
ProtClustDBCLSK727475.

Enzyme and pathway databases

BioCycAEHR187272:GHAX-1884-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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePIMT_ALHEH
AccessionPrimary (citable) accession number: Q0A7L5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 17, 2006
Last modified: May 1, 2013
This is version 47 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