Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q7NJY2 (PIMT_GLOVI)

Last modified June 16, 2009. Version 33. 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: glr1699
OrganismGloeobacter violaceus [Complete proteome] [HAMAP]
Taxonomic identifier33072 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaGloeobacteriaGloeobacteralesGloeobacter

Protein attributes

Sequence length205 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 – 205205Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090
PRO_0000111891

Sites

Active site521 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NJY2-1 [UniParc].

Last modified November 9, 2004. Version 2.
Checksum: 9BD86ACFDF33FCF7

FASTA20522,643
        10         20         30         40         50         60 
MVDEQLRPRG VEAQAVLAAM AKVPRHRFVP PPYTRLAYED RPLPIGHSQT ISQPFIVAYM 

        70         80         90        100        110        120 
SEAARITPGA KVLEIGTGSG YQAAVLAEMG AEVYTVEIVP ELAKRAERTL EELGYRSVRV 

       130        140        150        160        170        180 
RSGDGYQGWP QHAPFDAIVV TAAPERIPQP LIDQLAVNGR LIVPVGTQTE DQRMTVLTRT 

       190        200 
PGGIVEQKTF PVRFVPLTRE KPQEH 

« Hide

References

[1]"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids."
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.
DNA Res. 10:137-145(2003) [PubMed: 14621292] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7421.

Cross-references

Sequence databases

BA000045 Genomic DNA. Translation: BAC89640.1. Different initiation.
RefSeqNP_924645.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2598479.
GenomeReviewsGene locus glr1699 in contig BA000045_GR.
KEGGgvi:glr1699.
NMPDRfig|251221.1.peg.1699.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7NJY2.

Enzyme and pathway databases

BioCycGVIO251221:GLR1699-MON.
BRENDA2.1.1.77. 276183.

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_GLOVI
AccessionPrimary (citable) accession number: Q7NJY2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 9, 2004
Last sequence update: November 9, 2004
Last modified: June 16, 2009
This is version 33 of the entry and version 2 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