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Q92047 (PIMT_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. 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(D-aspartate) O-methyltransferase

Short name=PIMT
EC=2.1.1.77
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl/D-aspartyl methyltransferase
Protein-beta-aspartate methyltransferase
Gene names
Name:pcmt
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length228 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl 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.

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
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 228227Protein-L-isoaspartate(D-aspartate) O-methyltransferase
PRO_0000111879

Sites

Active site601 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92047 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 0266456304972562

FASTA22824,725
        10         20         30         40         50         60 
MAWKSGGASH AELVNNLRKN GIIKSDRVYE VMLATDRSHF SRCNPYMDSP QSIGYQATIS 

        70         80         90        100        110        120 
APHMHAYALE LLHDHLYEGA KALDVGSGSG ILSVCFSRMV GPTGKVIGID HIKELVEDSI 

       130        140        150        160        170        180 
ANVKKDDPSL ITSGRIKLIV GDGRMGFTEE APYDAIHVGA AAPTVPQALL DQLKPGGRLI 

       190        200        210        220 
LPVGPAGGNQ MLEQYDKLED GSTKMKPLMG VIYVPLTDKD KQWSRDEL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular phylogenetics of a protein repair methyltransferase."
Kagan R.M., McFadden H.J., McFadden P.N., O'Connor C., Clarke S.
Comp. Biochem. Physiol. 117B:379-385(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U37434 mRNA. Translation: AAA96020.1.
BC075735 mRNA. Translation: AAH75735.1.
RefSeqNP_571540.1. NM_131465.2.
UniGeneDr.372.

3D structure databases

ProteinModelPortalQ92047.
SMRQ92047. Positions 3-225.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ92047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000092718; ENSDARP00000087150; ENSDARG00000015201.
GeneID30751.
KEGGdre:30751.

Organism-specific databases

CTD30751.
ZFINZDB-GENE-990415-134. pcmt.

Phylogenomic databases

eggNOGCOG2518.
GeneTreeENSGT00510000046974.
HOVERGENHBG004483.
InParanoidQ92047.
KOK00573.

Gene expression databases

BgeeQ92047.

Family and domain databases

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...

Other

NextBio20807097.
PROQ92047.

Entry information

Entry namePIMT_DANRE
AccessionPrimary (citable) accession number: Q92047
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families