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Q2L008 (PIMT_BORA1) 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:BAV1980
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length264 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 – 264264Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090
PRO_0000351818

Sites

Active site1121 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2L008 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 935EED7C0CB3BC3F

FASTA26428,283
        10         20         30         40         50         60 
MRKPVGSKDG SGVYSRQGLD GYTPANSNTR ISTATLPRPE PLRPAASSAN LGLNSDRLRL 

        70         80         90        100        110        120 
AMVQRLRQMG ITDDRVLDAM AAVPRHTFVD EALASRAYED AALPIGHSQT ISQPWVVARM 

       130        140        150        160        170        180 
IAAVCEARAP SRVLEVGAGC GYQAAVLAQF VREVHSIERI RGLYELARAN LRALRLSTRV 

       190        200        210        220        230        240 
RLIYGDGTQG VPGVAPFDAI VVAAAGLAIP QALLNQLAPG GRLIAPEGST SQRLVLIERT 

       250        260 
GTASWKRMEL EAVRFVPLKA GIQS 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ49589.1.
RefSeqYP_786496.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2L008.
ModBaseSearch...

Protein-protein interaction databases

STRING360910.BAV1980.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6265723.
KEGGbav:BAV1980.
PATRIC21130154. VBIBorAvi43433_1999.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2518.
HOGENOMHOG000257189.
KOK00573.
OMAVRARMVQ.
ProtClustDBCLSK920464.

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_BORA1
AccessionPrimary (citable) accession number: Q2L008
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: March 7, 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