EC 2.1.1.77
Protein-beta-aspartate methyltransferase 1
PIMT 1
Protein L-isoaspartyl methyltransferase 1
L-isoaspartyl protein carboxyl methyltransferase 1

Gene name

	Name:	pcm1
	Synonyms:	pcm-1
	OrderedLocusNames:	MA_0544

From

Methanosarcina acetivorans

[TaxID: 2214]

[HAMAP proteome]

Taxonomy

Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
DOI=10.1101/gr.223902; PubMed=11932238 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.;
"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.";
Genome Res. 12:532-542(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

AE010299; AAM03988.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_615508.1; -.

3D structure databases

HSSP

Q8TZR3; 1JG1. [HSSP ENTRY / PDB]

ModBase

Q8TT93.

Enzyme and pathway databases

BioCyc

MACE188937:MA0544-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

1472436; -.

GenomeReviews

AE010299_GR; MA_0544.

KEGG

mac:MA0544; -.

NMPDR

fig|188937.1.peg.534; -.

Phylogenomic databases

HOGENOM

Q8TT93; -.

Genome annotation databases

CMR

Q8TT93; MA_0544.

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`	`1 251`	`251`	`Protein-L-isoaspartate O-methyltransferase 1.`	`PRO_0000111914`
`ACT_SITE`	`98 98`		`By similarity.`

Sequence information

Length: 251 AA [This is the length of the unprocessed precursor]

Molecular weight: 27873 Da [This is the MW of the unprocessed precursor]

CRC64: 7B3481CCB7A995E3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPERKEKGQV SVGAAEDRGK KGHSEKKDKR KQEENQEELH QLEEMRERLI RRIGIHGADE 

        70         80         90        100        110        120 
KVLKAMLRVP RHLFVPEYAK KGAYIDTPLE IGFGQTISAP HMVAIMCDLL ELSEGLKVLE 

       130        140        150        160        170        180 
IGAGSGYNAA VMGELVGKSG HVYTVERIEP LVDFARENLK KAGYENVTVL LDDGSMGYSK 

       190        200        210        220        230        240 
CAPYDRIVVT CAAPDIPEPL LEQLKPGGIM IIPVGDYIQE LVRIKKDPEG KIHEEKRGGV 

       250 
VFVPLIGKYG F

Q8TT93 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