Reviewed, UniProtKB/Swiss-Prot Q8TZR3 (PIMT_PYRFU)

Names and origin

Protein names

Recommended name:
    Protein-L-isoaspartate O-methyltransferase
    EC=2.1.1.77
Alternative name(s):
    Protein-beta-aspartate methyltransferase
      Short name=PIMT
    Protein L-isoaspartyl methyltransferase
    L-isoaspartyl protein carboxyl methyltransferase

Gene names

Name:	pcm
Ordered Locus Names:	PF1922

Organism

Pyrococcus furiosus [Complete proteome] [HAMAP]

Taxonomic identifier

2261 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (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. HAMAP MF_00090
Subunit structure	Monomer. HAMAP MF_00090
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein modification process Inferred from electronic annotation. Source: HAMAP protein repair Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein-L-isoaspartate (D-aspartate) O-methyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 219

219

Protein-L-isoaspartate O-methyltransferase HAMAP MF_00090

PRO_0000111923

Sites

Active site

65

1

By similarity

Secondary structure

1

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219

Helix Strand Turn

Details...

Helix

5 – 20

16

Helix

27 – 35

9

Helix

38 – 41

4

Helix

44 – 49

6

Beta strand

52 – 54

3

Helix

67 – 77

11

Beta strand

85 – 88

4

Helix

94 – 103

10

Beta strand

107 – 112

6

Helix

114 – 126

13

Beta strand

131 – 137

7

Helix

139 – 141

3

Helix

144 – 146

3

Beta strand

149 – 154

6

Beta strand

156 – 160

5

Helix

163 – 167

5

Beta strand

169 – 179

11

Beta strand

181 – 184

4

Beta strand

186 – 194

9

Beta strand

197 – 206

10

Sequences

	Sequence		Length	Mass (Da)
	Q8TZR3-1 [UniParc]. Last modified October 10, 2002. Version 2. Checksum: A239F32E24C3445D	FASTA	219	24,617
	10 20 30 40 50 60 MMDEKELYEK WMRTVEMLKA EGIIRSKEVE RAFLKYPRYL FVEDKYKKYA HIDEPLPIPA 70 80 90 100 110 120 GQTVSAPHMV AIMLEIANLK PGMNILEVGT GSGWNAALIS EIVKTDVYTI ERIPELVEFA 130 140 150 160 170 180 KRNLERAGVK NVHVILGDGS KGFPPKAPYD VIIVTAGAPK IPEPLIEQLK IGGKLIIPVG 190 200 210 SYHLWQELLE VRKTKDGIKI KNHGGVAFVP LIGEYGWKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequence of the Pyrococcus furiosus genome." Weiss R.B., Dunn D.M., Robb F.T., Brown J.R. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
[2]	"Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate." Griffith S.C., Sawaya M.R., Boutz D.R., Thapar N., Katz J.E., Clarke S., Yeates T.O. J. Mol. Biol. 313:1103-1116(2001) [PubMed: 11700066] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

AE010286 Genomic DNA. Translation: AAL82046.1. Different initiation.

RefSeq

NP_579651.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JG1	X-ray	1.20	A	1-219	[»]
1JG2	X-ray	1.50	A	1-219	[»]
1JG3	X-ray	2.10	A/B	1-219	[»]
1JG4	X-ray	1.50	A	1-219	[»]

ModBase

Search...

Genome annotation databases

GeneID

1469802.

GenomeReviews

Gene locus PF1922 in contig AE009950_GR.

KEGG

pfu:PF1922.

NMPDR

fig|186497.1.peg.1972.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q8TZR3.

OMA

Q8TZR3. APYDRIY.

Enzyme and pathway databases

BRENDA

2.1.1.77. 321.

Family and domain databases

HAMAP

MF_00090.
[Tree]

InterPro

IPR000682. PCMT.
[Graphical view]

PANTHER

PTHR11579. PCMT. 1 hit.

Pfam

PF01135. PCMT. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00080. pimt. 1 hit.

PROSITE

PS01279. PCMT. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PIMT_PYRFU

Accession

Primary (citable) accession number: Q8TZR3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	October 10, 2002
Last modified:	June 16, 2009
This is version 42 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)