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UniProtKB - Q8TMG0 (ICMT_METAC)

>sp|Q8TMG0|ICMT_METAC Protein-S-isoprenylcysteine O-methyltransferase OS=Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) OX=188937 GN=MA_2698 PE=1 SV=1
MNENLWKICFIVMFIIWVFVRKVYGTRAMKNKSKKKVRPNFEKSLVFLNFIGMVFLPLTA
VFSSYLDSFNINLPDSIRLFALIVTFLNIGLFTKIHKDLGNNWSAILEIKDGHKLVKEGI
YKNIRHPMYAHLWLWVITQGIILSNWVVLIFGIVAWAILYFIRVPKEEELLIEEFGDEYI
EYMGKTGRLFPKVV

Entry version 93 (25 May 2022)
Sequence version 1 (01 Jun 2002)
Previous versions | rss

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Protein

Protein-S-isoprenylcysteine O-methyltransferase

Gene

MA_2698

Organism

Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Carboxyl methyltransferase with activity toward prenyl lipids. In vitro, displays activity toward N-acetyl-S-farnesyl-L-cysteine (AFC) and S-farnesylthioacetic acid (FTA), an analog of AFC.

1 Publication

Catalytic activityⁱ

[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
S-adenosyl-L-methionine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
S-adenosyl-L-homocysteine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.2
  "Mechanism of isoprenylcysteine carboxyl methylation from the crystal structure of the integral membrane methyltransferase ICMT."
  Yang J., Kulkarni K., Manolaridis I., Zhang Z., Dodd R.B., Mas-Droux C., Barford D.
  Mol. Cell 44:997-1004(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF HIS-113; HIS-126; ARG-163 AND GLU-167.
EC:
2.1.1.100
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
1 Publication
Manual assertion inferred by curator fromⁱ
- Ref.2
  "Mechanism of isoprenylcysteine carboxyl methylation from the crystal structure of the integral membrane methyltransferase ICMT."
  Yang J., Kulkarni K., Manolaridis I., Zhang Z., Dodd R.B., Mas-Droux C., Barford D.
  Mol. Cell 44:997-1004(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF HIS-113; HIS-126; ARG-163 AND GLU-167.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine
C-terminal S-[(2E,6E)-farnesyl]-L-cysteine residue
zoom
+
S-adenosyl-L-methionine
zoom
=
[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester
C-terminal S-[(2E,6E)-farnesyl]-L-cysteine methyl ester residue
zoom
+
S-adenosyl-L-homocysteine
zoom

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	108	S-adenosyl-L-methionine; via carbonyl oxygen1 Publication	1
Binding siteⁱ	121	S-adenosyl-L-methionine1 Publication	1
Binding siteⁱ	163	SubstrateBy similarity	1
Binding siteⁱ	167	S-adenosyl-L-methionine1 Publication	1

GO - Molecular functionⁱ

protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity Source: UniProtKB-EC

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Methyltransferase, Transferase
Ligand	S-adenosyl-L-methionine

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Protein-S-isoprenylcysteine O-methyltransferaseCurated (EC:2.1.1.1001 Publication) Alternative name(s): Isoprenylcysteine carboxyl methyltransferase1 Publication Short name: ICMT1 Publication
Gene namesⁱ	Ordered Locus Names:MA_2698Imported
Organismⁱ	Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifierⁱ	188937 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Archaea › Euryarchaeota › Stenosarchaea group › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina › Methanosarcina acetivorans
Proteomesⁱ	UP000002487 Componentⁱ: Chromosome

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1	Extracellular1 Publication	1
Transmembraneⁱ	2 – 28	Helical1 PublicationAdd BLAST	27
Topological domainⁱ	29 – 37	Cytoplasmic1 Publication	9
Transmembraneⁱ	38 – 62	Helical1 PublicationAdd BLAST	25
Topological domainⁱ	63 – 73	Extracellular1 PublicationAdd BLAST	11
Transmembraneⁱ	74 – 98	Helical1 PublicationAdd BLAST	25
Topological domainⁱ	99 – 125	Cytoplasmic1 PublicationAdd BLAST	27
Transmembraneⁱ	126 – 144	Helical1 PublicationAdd BLAST	19
Topological domainⁱ	145	Extracellular1 Publication	1
Transmembraneⁱ	146 – 166	Helical1 PublicationAdd BLAST	21
Topological domainⁱ	167 – 194	Cytoplasmic1 PublicationAdd BLAST	28

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	113	H → A: Abolishes FTA methylation. 1 Publication	1
Mutagenesisⁱ	126	H → A: Abolishes FTA methylation. 1 Publication	1
Mutagenesisⁱ	163	R → A: Abolishes FTA methylation. 1 Publication	1
Mutagenesisⁱ	167	E → A: Abolishes FTA methylation. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000449360	1 – 194	Protein-S-isoprenylcysteine O-methyltransferaseAdd BLAST		194

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	3 – 28	Combined sources	26
Beta strandⁱ	29 – 31	Combined sources	3
Beta strandⁱ	33 – 35	Combined sources	3
Helixⁱ	39 – 53	Combined sources	15
Helixⁱ	55 – 61	Combined sources	7
Helixⁱ	65 – 69	Combined sources	5
Helixⁱ	75 – 99	Combined sources	25
Helixⁱ	100 – 102	Combined sources	3
Turnⁱ	120 – 123	Combined sources	4
Beta strandⁱ	124 – 126	Combined sources	3
Helixⁱ	127 – 143	Combined sources	17
Helixⁱ	146 – 175	Combined sources	30
Helixⁱ	177 – 185	Combined sources	9
Beta strandⁱ	187 – 190	Combined sources	4

Show more details

3D structure databases

AlphaFoldDBⁱ	Q8TMG0
SMRⁱ	Q8TMG0
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	113 – 116	S-adenosyl-L-methionine binding1 Publication		4
Regionⁱ	126 – 129	S-adenosyl-L-methionine binding1 Publication		4

Sequence similaritiesⁱ

Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family.Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMⁱ	CLU_065200_1_1_2
InParanoidⁱ	Q8TMG0
OMAⁱ	FSLWLFR
Database of Orthologous Groups More...OrthoDBⁱ	94584at2157
PhylomeDBⁱ	Q8TMG0

Family and domain databases

InterProⁱ	View protein in InterPro IPR007269, ICMT_MeTrfase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF04140, ICMT, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q8TMG0-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MNENLWKICF IVMFIIWVFV RKVYGTRAMK NKSKKKVRPN FEKSLVFLNF 
        60         70         80         90        100
IGMVFLPLTA VFSSYLDSFN INLPDSIRLF ALIVTFLNIG LFTKIHKDLG 
       110        120        130        140        150
NNWSAILEIK DGHKLVKEGI YKNIRHPMYA HLWLWVITQG IILSNWVVLI 
       160        170        180        190 
FGIVAWAILY FIRVPKEEEL LIEEFGDEYI EYMGKTGRLF PKVV

Length:194

Mass (Da):22,811

Last modified:June 1, 2002 - v1

Checksum:ⁱ11A8176F4E8B4EA9

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE010299 Genomic DNA Translation: AAM06077.1
NCBI Reference Sequences More...RefSeqⁱ	WP_011022658.1, NC_003552.1

Genome annotation databases

EnsemblBacteriaⁱ	AAM06077; AAM06077; MA_2698
GeneIDⁱ	1474591
KEGGⁱ	mac:MA_2698

Similar proteinsⁱ

50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q8TMG0	Isoprenylcysteine carboxylmethyltransferase family protein		Methanomicrobiales archaeon		193	UniRef50_Q8TMG0
Isoprenylcysteine carboxylmethyltransferase family protein		Methanospirillum stamsii		194
Isoprenylcysteine carboxyl methyltransferase		METP4		193
Isoprenylcysteine carboxylmethyltransferase family protein		Methanoregula sp.		194
+1

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AE010299 Genomic DNA Translation: AAM06077.1
RefSeqⁱ	WP_011022658.1, NC_003552.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4A2N	X-ray	3.40	B	1-194	[»]
AlphaFoldDBⁱ	Q8TMG0
SMRⁱ	Q8TMG0
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAM06077; AAM06077; MA_2698
GeneIDⁱ	1474591
KEGGⁱ	mac:MA_2698

Phylogenomic databases

HOGENOMⁱ	CLU_065200_1_1_2
InParanoidⁱ	Q8TMG0
OMAⁱ	FSLWLFR
OrthoDBⁱ	94584at2157
PhylomeDBⁱ	Q8TMG0

Family and domain databases

InterProⁱ	View protein in InterPro IPR007269, ICMT_MeTrfase
Pfamⁱ	View protein in Pfam PF04140, ICMT, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ICMT_METAC
Accessionⁱ	Q8TMG0Primary (citable) accession number: Q8TMG0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 22, 2020
	Last sequence update:	June 1, 2002
	Last modified:	May 25, 2022
	This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - Q8TMG0 (ICMT_METAC)

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Protein-S-isoprenylcysteine O-methyltransferase

MA_2698

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Plasma Membrane

Other locations

Topology

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ