Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q8TYL4 (PIMT_METKA)

Last modified June 16, 2009. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein-L-isoaspartate O-methyltransferase
    EC=2.1.1.77
Alternative name(s):
    Protein-beta-aspartate methyltransferase
      Short name=PIMT
    Protein L-isoaspartyl methyltransferase
    L-isoaspartyl protein carboxyl methyltransferase
Gene names
Name: pcm
Ordered Locus Names: MK0282
OrganismMethanopyrus kandleri [Complete proteome] [HAMAP]
Taxonomic identifier2320 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester. HAMAP MF_00090

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the 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 modification process

Inferred from electronic annotation. Source: HAMAP

protein 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 – 226226Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090
PRO_0000111917

Sites

Active site661 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TYL4-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 1BCD87E3265E61B4

FASTA22625,207
        10         20         30         40         50         60 
MAEDDKVFRR ARERLVERLK SLGYIRSNRV AEAMLKVPRH EFVPEDLRDR AYVDSPLPIG 

        70         80         90        100        110        120 
RGQTISAPHM VAIMTELLDP RPGHKVLEVG AGSGYHAAVV AELVKPDGRV ITVERIPELA 

       130        140        150        160        170        180 
DFARNNLKKT GYDRFVKVLV GDGTKGYPPE APYDRILVTA GAPDVPESLL EQLKPGGKMV 

       190        200        210        220 
IPVGDRHMQE LWLVEKTEDG EIRRRRHGGC AFVPLIGEEG FQEPES 

« Hide

References

[1]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

AE010326 Genomic DNA. Translation: AAM01499.1.
RefSeqNP_613569.1.

3D structure databases

HSSPHSSP built from PDB template 1JG1 based on UniProtKB Q8TZR3.
ModBaseSearch...

Genome annotation databases

GeneID1477585.
GenomeReviewsGene locus MK0282 in contig AE009439_GR.
KEGGmka:MK0282.
NMPDRfig|190192.1.peg.282.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8TYL4.
OMAQ8TYL4. APYDRIY.

Enzyme and pathway databases

BioCycMKAN190192:MK0282-MON.
BRENDA2.1.1.77. 7577.

Family and domain databases

HAMAPMF_00090.
[Tree]
InterProIPR000682. PCMT.
[Graphical view]
PANTHERPTHR11579. PCMT. 1 hit.
PfamPF01135. PCMT. 1 hit.
[Graphical view]
TIGRFAMsTIGR00080. pimt. 1 hit.
PROSITEPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePIMT_METKA
AccessionPrimary (citable) accession number: Q8TYL4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2002
Last modified: June 16, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents