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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei60 – 6011 Publication

GO - Molecular functioni

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

GO - Biological processi

  • cellular protein modification process Source: FlyBase
  • defense response to bacterium Source: FlyBase
  • protein methylation Source: GOC
  • protein repair 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601S → A: Reduces catalytic efficiency. 1 Publication
Mutagenesisi60 – 601S → Q: Loss of catalytic activity. 1 Publication
Mutagenesisi60 – 601S → T: Reduces catalytic efficiency. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226Protein-L-isoaspartate(D-aspartate) O-methyltransferasePRO_0000111881Add
BLAST

Proteomic databases

PaxDbiQ27869.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiQ27869.
ExpressionAtlasiQ27869. differential.
GenevisibleiQ27869. DM.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi7227.FBpp0078405.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 1910Combined sources
Helixi26 – 338Combined sources
Helixi37 – 393Combined sources
Beta strandi47 – 493Combined sources
Beta strandi51 – 544Combined sources
Beta strandi57 – 593Combined sources
Helixi62 – 7110Combined sources
Turni72 – 754Combined sources
Beta strandi81 – 866Combined sources
Helixi91 – 10212Combined sources
Beta strandi110 – 1167Combined sources
Helixi118 – 13215Combined sources
Helixi134 – 1374Combined sources
Beta strandi140 – 1467Combined sources
Helixi148 – 1503Combined sources
Helixi153 – 1553Combined sources
Beta strandi157 – 1637Combined sources
Beta strandi167 – 1693Combined sources
Helixi172 – 1765Combined sources
Beta strandi178 – 18912Combined sources
Beta strandi191 – 1933Combined sources
Beta strandi195 – 2028Combined sources
Beta strandi208 – 2169Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ27869.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1661. Eukaryota.
COG2518. LUCA.
GeneTreeiENSGT00510000046974.
HOGENOMiHOG000242538.
InParanoidiQ27869.
OMAiANNEDLI.
OrthoDBiEOG78WKSS.
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.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1R18X-ray2.20A1-221[»]
ProteinModelPortaliQ27869.
SMRiQ27869. Positions 1-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0078405.

Proteomic databases

PaxDbiQ27869.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0078758; FBpp0078405; FBgn0086768.
GeneIDi40668.

Organism-specific databases

CTDi30751.
FlyBaseiFBgn0086768. Pcmt.

Phylogenomic databases

eggNOGiKOG1661. Eukaryota.
COG2518. LUCA.
GeneTreeiENSGT00510000046974.
HOGENOMiHOG000242538.
InParanoidiQ27869.
OMAiANNEDLI.
OrthoDBiEOG78WKSS.
PhylomeDBiQ27869.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPcmt. fly.
EvolutionaryTraceiQ27869.
GenomeRNAii40668.
NextBioi819937.
PROiQ27869.

Gene expression databases

BgeeiQ27869.
ExpressionAtlasiQ27869. differential.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Structural organization and developmental expression of the protein isoaspartyl methyltransferase gene from Drosophila melanogaster."
    O'Connor M.B., Galus A., Hartenstine M., Magee M., Jackson F.R., O'Connor C.M.
    Insect Biochem. Mol. Biol. 27:49-54(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
  2. O'Connor C.M.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 124.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis."
    Bennett E.J., Bjerregaard J., Knapp J.E., Chavous D.A., Friedman A.M., Royer W.E. Jr., O'Connor C.M.
    Biochemistry 42:12844-12853(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-221, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-60.

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: May 11, 2016
This is version 123 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.