NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
PubMed=12125824 [NCBI, ExPASy, EBI, Israel, Japan]
Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G.;
"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea.";
J. Mol. Microbiol. Biotechnol. 4:453-461(2002).

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

AE008384; AAM31402.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_633730.1; -.

3D structure databases

HSSP

Q8TZR3; 1JG1. [HSSP ENTRY / PDB]

ModBase

Q8PW90.

Enzyme and pathway databases

BioCyc

MMAZ192952:MM1706-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

IPR002110; ANK.
IPR000682; PCMT.
Graphical view of domain structure.

PANTHER

PTHR11579; PCMT; 1.

Pfam

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

PR01415; ANKYRIN.

TIGR00080; pimt; 1.

PS01279; PCMT; 1.

Genome annotation databases

GeneID

1480048; -.

GenomeReviews

AE008384_GR; MM_1706.

KEGG

mma:MM_1706; -.

NMPDR

fig|192952.1.peg.1706; -.

Phylogenomic databases

HOGENOM

Q8PW90; -.

Genome annotation databases

CMR

Q8PW90; MM_1706.

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`	`1 243`	`243`	`Protein-L-isoaspartate O-methyltransferase.`	`PRO_0000111918`
`ACT_SITE`	`87 87`		`By similarity.`

Sequence information

Length: 243 AA [This is the length of the unprocessed precursor]

Molecular weight: 27120 Da [This is the MW of the unprocessed precursor]

CRC64: DF83E0D0591A1B1C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPERRGIVLV NAVSEKDLGE DKRKREKEKE CEKLRKLLVE GLEGFVIDEK VLQAMLRVPR 

        70         80         90        100        110        120 
HRFVPEYEQR AAYVDMPLEI GHGQTISAPH MVAMMCEILE LAEGHKVLEI GAGSGYNAAV 

       130        140        150        160        170        180 
MSELVGKTGH IYTVERVEPL ANFAKKNLKE AGYKNVTVLL ENGSMGYPGY APYDRIAVTC 

       190        200        210        220        230        240 
AAPNIPETLL EQLKPGGIMV IPVGSYSQEL IRVKKDSTGK IYRKKKGDVI FVPMIGKHGF 


RRI

Q8PW90 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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