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.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE008833; AAL21806.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_461847.1; -.

3D structure databases

HSSP

Q8TZR3; 1JG1. [HSSP ENTRY / PDB]

ModBase

Q8ZMF9.

Enzyme and pathway databases

BioCyc

STYP99287:STM2926-MON; -.

Organism-specific databases

StyGene

SG?????; pcm.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004719;	Molecular function: protein-L-isoaspartate (D-aspartate) O-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006464;	Biological process: protein modification process (inferred from electronic annotation from HAMAP).
GO:0030091;	Biological process: protein repair (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00090; -; 1.
PBIL [Tree]

InterPro

IPR000682; PCMT.
Graphical view of domain structure.

PANTHER

PTHR11579; PCMT; 1.

Pfam

PF01135; PCMT; 1.
Pfam graphical view of domain structure.

TIGR00080; pimt; 1.

PS01279; PCMT; 1.

Genome annotation databases

GeneID

1254449; -.

GenomeReviews

AE006468_GR; STM2926.

KEGG

stm:STM2926; -.

Phylogenomic databases

HOGENOM

Q8ZMF9; -.

Genome annotation databases

CMR

Q8ZMF9; STM2926.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 208`	`208`	`Protein-L-isoaspartate O-methyltransferase.`	`PRO_0000111903`
`ACT_SITE`	`59 59`		`By similarity.`

Sequence information

Length: 208 AA [This is the length of the unprocessed precursor]

Molecular weight: 23192 Da [This is the MW of the unprocessed precursor]

CRC64: 4CC10D557A37FAB7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVSGRVQALL EQLRAQGIRD EQVLNALAAV PREKFIDEAF EHKAWENIAL PIGQGQTISQ 

        70         80         90        100        110        120 
PYMVARMTEL LELTPQSRVL EIGTGSGYQT AILAHLVHHV CSVERIKGLQ WQARRRLKQL 

       130        140        150        160        170        180 
DLHNVSTRHG DGWQGWQARA PFDAIIVTAA PPEIPTALMA QLDEGGILVL PVGDEQQFLK 

       190        200 
RVRRRGGEFI IDTVEAVRFV PLVKGELA

Q8ZMF9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools