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A1WWY5 (PIMT_HALHL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 45. 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:Hhal_1430
OrganismHalorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) [Complete proteome] [HAMAP]
Taxonomic identifier349124 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeHalorhodospira

Protein attributes

Sequence length220 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 – 220220Protein-L-isoaspartate O-methyltransferase HAMAP-Rule MF_00090
PRO_0000351866

Sites

Active site701 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WWY5 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 4FBDAFBD219EDA9E

FASTA22024,274
        10         20         30         40         50         60 
MRERNAAGIG MTSQRTRDRL VDALAAQGIQ DERVLSAMRE VPRHLFVDEA LESRAYENTP 

        70         80         90        100        110        120 
LPIGEGQTIS QPWVVARMTE LLLEPGVPER VLEVGTGSGY QAAVLARLVP RVYSIERIGS 

       130        140        150        160        170        180 
LLRRARERLQ AVRLFNCQLR HGDGYEGWPE YAPYDGIIVT AAPDALPEAL LEQLADGGRL 

       190        200        210        220 
VAPIGGAGYQ ELLVVDRRGD AYEQRRVAGV SFVPMLEGRV 

« Hide

References

[1]"Complete sequence of Halorhodospira halophila SL1."
US DOE Joint Genome Institute
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., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 244 / SL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000544 Genomic DNA. Translation: ABM62197.1.
RefSeqYP_001002999.1. NC_008789.1.

3D structure databases

ProteinModelPortalA1WWY5.
ModBaseSearch...

Protein-protein interaction databases

STRING349124.Hhal_1430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM62197; ABM62197; Hhal_1430.
GeneID4710549.
KEGGhha:Hhal_1430.
PATRIC22097161. VBIHalHal112047_1417.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2518.
HOGENOMHOG000257189.
KOK00573.
OMAVRARMVQ.
ProtClustDBCLSK727475.

Enzyme and pathway databases

BioCycHHAL349124:GI3I-1484-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_HALHL
AccessionPrimary (citable) accession number: A1WWY5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: February 6, 2007
Last modified: May 1, 2013
This is version 45 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