Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein-L-isoaspartate O-methyltransferase

Gene

pcm

Organism
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei56UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-L-isoaspartate O-methyltransferaseUniRule annotation (EC:2.1.1.77UniRule annotation)
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferaseUniRule annotation
Protein L-isoaspartyl methyltransferaseUniRule annotation
Protein-beta-aspartate methyltransferaseUniRule annotation
Short name:
PIMTUniRule annotation
Gene namesi
Name:pcmUniRule annotation
Ordered Locus Names:Pars_2349
OrganismiPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
Taxonomic identifieri340102 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
Proteomesi
  • UP000001567 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000932671 – 205Protein-L-isoaspartate O-methyltransferaseAdd BLAST205

Structurei

3D structure databases

ProteinModelPortaliA4WNC5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the methyltransferase superfamily. L-isoaspartyl/D-aspartyl protein methyltransferase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000257189.
KOiK00573.
OMAiFAIERHA.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00090. PIMT. 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.

A4WNC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKLVDDLE REGVLKSERV KKALLSVPRE EFVMPEYRMM AYEDRPLPLF
60 70 80 90 100
ADATISAPHM VAMMCELIEP RPGMSILEVG TGSGYHAAVC AEAIERRGKV
110 120 130 140 150
YTVEIVKGLA IYAAQNLERL GYWGVVEVFH SDGKRGLEKF APYDAIIVTA
160 170 180 190 200
AAASIPSALV NQLKDGGIMV IPVEEGFGQV LYKVVRRGEK TEKKAVTYVL

FVPLR
Length:205
Mass (Da):22,689
Last modified:May 29, 2007 - v1
Checksum:i5F8CC2883F2F557C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000660 Genomic DNA. Translation: ABP51892.1.

Genome annotation databases

EnsemblBacteriaiABP51892; ABP51892; Pars_2349.
KEGGipas:Pars_2349.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000660 Genomic DNA. Translation: ABP51892.1.

3D structure databases

ProteinModelPortaliA4WNC5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP51892; ABP51892; Pars_2349.
KEGGipas:Pars_2349.

Phylogenomic databases

HOGENOMiHOG000257189.
KOiK00573.
OMAiFAIERHA.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00090. PIMT. 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_PYRAR
AccessioniPrimary (citable) accession number: A4WNC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 29, 2007
Last modified: November 2, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. 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.