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Protein

Protein-L-isoaspartate(D-aspartate) O-methyltransferase

Gene

Pcmt

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei601 Publication1

GO - Molecular functioni

  • protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Source: FlyBase

GO - Biological processi

  • defense response to bacterium Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.77. 1994.
ReactomeiR-DME-5676934. Protein repair.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (EC:2.1.1.77)
Short name:
PIMT
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl/D-aspartyl methyltransferase
Protein-beta-aspartate methyltransferase
dPIMT
Gene namesi
Name:Pcmt
Synonyms:PIAM
ORF Names:CG2152
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0086768. Pcmt.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi60S → A: Reduces catalytic efficiency. 1 Publication1
Mutagenesisi60S → Q: Loss of catalytic activity. 1 Publication1
Mutagenesisi60S → T: Reduces catalytic efficiency. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001118811 – 226Protein-L-isoaspartate(D-aspartate) O-methyltransferaseAdd BLAST226

Proteomic databases

PaxDbiQ27869.
PRIDEiQ27869.

Expressioni

Developmental stagei

Expressed throughout development, lowest in larvae and highest in adults.1 Publication

Gene expression databases

BgeeiFBgn0086768.
ExpressionAtlasiQ27869. baseline.
GenevisibleiQ27869. DM.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi7227.FBpp0078405.

Structurei

Secondary structure

1226
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 19Combined sources10
Helixi26 – 33Combined sources8
Helixi37 – 39Combined sources3
Beta strandi47 – 49Combined sources3
Beta strandi51 – 54Combined sources4
Beta strandi57 – 59Combined sources3
Helixi62 – 71Combined sources10
Turni72 – 75Combined sources4
Beta strandi81 – 86Combined sources6
Helixi91 – 102Combined sources12
Beta strandi110 – 116Combined sources7
Helixi118 – 132Combined sources15
Helixi134 – 137Combined sources4
Beta strandi140 – 146Combined sources7
Helixi148 – 150Combined sources3
Helixi153 – 155Combined sources3
Beta strandi157 – 163Combined sources7
Beta strandi167 – 169Combined sources3
Helixi172 – 176Combined sources5
Beta strandi178 – 189Combined sources12
Beta strandi191 – 193Combined sources3
Beta strandi195 – 202Combined sources8
Beta strandi208 – 216Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R18X-ray2.20A1-221[»]
ProteinModelPortaliQ27869.
SMRiQ27869.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ27869.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1661. Eukaryota.
COG2518. LUCA.
GeneTreeiENSGT00510000046974.
HOGENOMiHOG000242538.
InParanoidiQ27869.
KOiK00573.
OMAiANNEDLI.
OrthoDBiEOG091G0OTG.
PhylomeDBiQ27869.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR000682. PCMT.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11579. PTHR11579. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00080. pimt. 1 hit.
PROSITEiPS01279. PCMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q27869-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWRSVGANN EDLIRQLKDH GVIASDAVAQ AMKETDRKHY SPRNPYMDAP
60 70 80 90 100
QPIGGGVTIS APHMHAFALE YLRDHLKPGA RILDVGSGSG YLTACFYRYI
110 120 130 140 150
KAKGVDADTR IVGIEHQAEL VRRSKANLNT DDRSMLDSGQ LLIVEGDGRK
160 170 180 190 200
GYPPNAPYNA IHVGAAAPDT PTELINQLAS GGRLIVPVGP DGGSQYMQQY
210 220
DKDANGKVEM TRLMGVMYVP LTDLRS
Length:226
Mass (Da):24,590
Last modified:June 1, 2001 - v2
Checksum:iAA56803256DBD567
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43737 Genomic DNA. Translation: AAA86272.2.
U37432 mRNA. Translation: AAA80540.2.
AE014297 Genomic DNA. Translation: AAF52012.1.
AY070630 mRNA. Translation: AAL48101.1.
AY075527 mRNA. Translation: AAL68334.1.
RefSeqiNP_536756.1. NM_080508.4.
UniGeneiDm.4629.

Genome annotation databases

EnsemblMetazoaiFBtr0078758; FBpp0078405; FBgn0086768.
GeneIDi40668.
KEGGidme:Dmel_CG2152.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U43737 Genomic DNA. Translation: AAA86272.2.
U37432 mRNA. Translation: AAA80540.2.
AE014297 Genomic DNA. Translation: AAF52012.1.
AY070630 mRNA. Translation: AAL48101.1.
AY075527 mRNA. Translation: AAL68334.1.
RefSeqiNP_536756.1. NM_080508.4.
UniGeneiDm.4629.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1R18X-ray2.20A1-221[»]
ProteinModelPortaliQ27869.
SMRiQ27869.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0078405.

Proteomic databases

PaxDbiQ27869.
PRIDEiQ27869.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078758; FBpp0078405; FBgn0086768.
GeneIDi40668.
KEGGidme:Dmel_CG2152.

Organism-specific databases

CTDi30751.
FlyBaseiFBgn0086768. Pcmt.

Phylogenomic databases

eggNOGiKOG1661. Eukaryota.
COG2518. LUCA.
GeneTreeiENSGT00510000046974.
HOGENOMiHOG000242538.
InParanoidiQ27869.
KOiK00573.
OMAiANNEDLI.
OrthoDBiEOG091G0OTG.
PhylomeDBiQ27869.

Enzyme and pathway databases

BRENDAi2.1.1.77. 1994.
ReactomeiR-DME-5676934. Protein repair.

Miscellaneous databases

ChiTaRSiPcmt. fly.
EvolutionaryTraceiQ27869.
GenomeRNAii40668.
PROiQ27869.

Gene expression databases

BgeeiFBgn0086768.
ExpressionAtlasiQ27869. baseline.
GenevisibleiQ27869. DM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR000682. PCMT.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR11579. PTHR11579. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00080. pimt. 1 hit.
PROSITEiPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPIMT_DROME
AccessioniPrimary (citable) accession number: Q27869
Secondary accession number(s): Q9VND1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 1, 2001
Last modified: November 30, 2016
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.