NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PCC 7421;
DOI=10.1093/dnares/10.4.137; PubMed=14621292 [NCBI, ExPASy, EBI, Israel, Japan]
Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T., Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of Gloeobacter violaceus PCC 7421, a cyanobacterium that lacks thylakoids.";
DNA Res. 10:137-145(2003).

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.
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

BA000045; BAC89640.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_924645.1; -.

3D structure databases

ModBase

Q7NJY2.

Enzyme and pathway databases

BioCyc

GVIO251221:GLR1699-MON; -.

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

2598479; -.

GenomeReviews

BA000045_GR; glr1699.

KEGG

gvi:glr1699; -.

NMPDR

fig|251221.1.peg.1699; -.

Phylogenomic databases

HOGENOM

Q7NJY2; -.

Genome annotation databases

CMR

Q7NJY2; glr1699.

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`	`1 205`	`205`	`Protein-L-isoaspartate O-methyltransferase.`	`PRO_0000111891`
`ACT_SITE`	`52 52`		`By similarity.`

Sequence information

Length: 205 AA [This is the length of the unprocessed precursor]

Molecular weight: 22643 Da [This is the MW of the unprocessed precursor]

CRC64: 9BD86ACFDF33FCF7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVDEQLRPRG VEAQAVLAAM AKVPRHRFVP PPYTRLAYED RPLPIGHSQT ISQPFIVAYM 

        70         80         90        100        110        120 
SEAARITPGA KVLEIGTGSG YQAAVLAEMG AEVYTVEIVP ELAKRAERTL EELGYRSVRV 

       130        140        150        160        170        180 
RSGDGYQGWP QHAPFDAIVV TAAPERIPQP LIDQLAVNGR LIVPVGTQTE DQRMTVLTRT 

       190        200 
PGGIVEQKTF PVRFVPLTRE KPQEH

Q7NJY2 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