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Protein

Probable protein-L-isoaspartate O-methyltransferase

Gene

pcm2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 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. This enzyme does not act on D-aspartyl residues (By similarity).By similarity

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 – 601By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiR-SPO-5676934. Protein repair.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable protein-L-isoaspartate O-methyltransferase (EC:2.1.1.77)
Short name:
PIMT
Alternative name(s):
L-isoaspartyl protein carboxyl methyltransferase
Protein L-isoaspartyl methyltransferase
Protein-beta-aspartate methyltransferase
Gene namesi
Name:pcm2
ORF Names:SPAC869.08
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC869.08.
PomBaseiSPAC869.08. pcm2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Probable protein-L-isoaspartate O-methyltransferasePRO_0000316247Add
BLAST

Interactioni

Protein-protein interaction databases

BioGridi279805. 10 interactions.
MINTiMINT-4707334.

Structurei

3D structure databases

ProteinModelPortaliQ9URZ1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000257189.
InParanoidiQ9URZ1.
KOiK00573.
OMAiANNEDLI.
OrthoDBiEOG76TB34.
PhylomeDBiQ9URZ1.

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.

Sequencei

Sequence statusi: Complete.

Q9URZ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFWSFNLSSN AALVQHLVES KFLTNQRAIK AMNATSRSFY CPLSPYMDSP
60 70 80 90 100
QSIGYGVTIS APHMHATALQ ELEPVLQPGC SALDIGSGSG YLVAAMARMV
110 120 130 140 150
APNGTVKGIE HIPQLVETSK KNLLKDINHD EVLMEMYKEK RLQINVGDGR
160 170 180 190 200
MGTSEDEKFD AIHVGASASE LPQKLVDQLK SPGKILIPIG TYSQNIYLIE
210 220 230
KNEQGKISKR TLFPVRYVPL TDSPDDSSDY
Length:230
Mass (Da):25,333
Last modified:May 1, 2000 - v1
Checksum:iA38C89901812F792
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB60018.1.
PIRiT39119.
RefSeqiNP_595011.1. NM_001020442.2.

Genome annotation databases

EnsemblFungiiSPAC869.08.1; SPAC869.08.1:pep; SPAC869.08.
GeneIDi2543383.
KEGGispo:SPAC869.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB60018.1.
PIRiT39119.
RefSeqiNP_595011.1. NM_001020442.2.

3D structure databases

ProteinModelPortaliQ9URZ1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279805. 10 interactions.
MINTiMINT-4707334.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC869.08.1; SPAC869.08.1:pep; SPAC869.08.
GeneIDi2543383.
KEGGispo:SPAC869.08.

Organism-specific databases

EuPathDBiFungiDB:SPAC869.08.
PomBaseiSPAC869.08. pcm2.

Phylogenomic databases

HOGENOMiHOG000257189.
InParanoidiQ9URZ1.
KOiK00573.
OMAiANNEDLI.
OrthoDBiEOG76TB34.
PhylomeDBiQ9URZ1.

Enzyme and pathway databases

ReactomeiR-SPO-5676934. Protein repair.

Miscellaneous databases

PROiQ9URZ1.

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.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPIMT_SCHPO
AccessioniPrimary (citable) accession number: Q9URZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.