SPBPB21E7.04c

Functionⁱ

Catalytic activityⁱ

S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol.

Cofactorⁱ

Mg²⁺By similarityNote: Binds 1 Mg²⁺ ion per subunit.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	78	S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation	1
Binding siteⁱ	100	S-adenosyl-L-methioninePROSITE-ProRule annotation	1
Binding siteⁱ	108	S-adenosyl-L-methioninePROSITE-ProRule annotation	1
Binding siteⁱ	127	S-adenosyl-L-methioninePROSITE-ProRule annotation	1
Binding siteⁱ	128	S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation	1
Binding siteⁱ	156	S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation	1
Metal bindingⁱ	183	MagnesiumBy similarity	1
Binding siteⁱ	183	S-adenosyl-L-methioninePROSITE-ProRule annotation	1
Binding siteⁱ	186	SubstrateBy similarity	1
Metal bindingⁱ	211	MagnesiumBy similarity	1
Metal bindingⁱ	212	MagnesiumBy similarity	1
Binding siteⁱ	212	SubstrateBy similarity	1

GO - Molecular functionⁱ

metal ion binding Source: UniProtKB-KW
O-methyltransferase activity Source: PomBase

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

catecholamine metabolic process Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Methyltransferase, Transferase
Biological process	Catecholamine metabolism
Ligand	Magnesium, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

Reactomeⁱ	R-SPO-156581. Methylation. R-SPO-379397. Enzymatic degradation of dopamine by COMT. R-SPO-379398. Enzymatic degradation of Dopamine by monoamine oxidase.

Reactomeⁱ

R-SPO-156581. Methylation.
R-SPO-379397. Enzymatic degradation of dopamine by COMT.
R-SPO-379398. Enzymatic degradation of Dopamine by monoamine oxidase.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Probable catechol O-methyltransferase 2 (EC:2.1.1.6)
Gene namesⁱ	ORF Names:SPBPB21E7.04c
Organismⁱ	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifierⁱ	284812 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe
Proteomesⁱ	UP000002485 Componentⁱ: Chromosome II

Organism-specific databases

EuPathDBⁱ	FungiDB:SPBPB21E7.04c.
PomBaseⁱ	SPBPB21E7.04c.

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Vacuole

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000318149	1 – 281	Probable catechol O-methyltransferase 2Add BLAST		281

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q8NKC1.
PaxDbⁱ	Q8NKC1.
PRIDEⁱ	Q8NKC1.

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	280254. 2 interactors.
STRINGⁱ	4896.SPBPB21E7.04c.1.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q8NKC1.
SMRⁱ	Q8NKC1.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMⁱ	HOG000171638.
InParanoidⁱ	Q8NKC1.
KEGG Orthology (KO) More...KOⁱ	K00545.
OMAⁱ	SRFECTH.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C4KCD.
PhylomeDBⁱ	Q8NKC1.

Family and domain databases

InterProⁱ	View protein in InterPro IPR002935. O-MeTrfase_3. IPR029063. SAM-dependent_MTases.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01596. Methyltransf_3. 1 hit.
SUPFAMⁱ	SSF53335. SSF53335. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51682. SAM_OMT_I. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Q8NKC1-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MFAQALHWLT TSKLRYALAL PFLFFILYTK TKKSKEQELE NYIFSLPREK 
        60         70         80         90        100
LDQIRGKPDE VINVIDEYVE QGHFLMNIGK LKGKIISEKI QQVKPKVMIE 
       110        120        130        140        150
LGGYVGYSAI LFGKQLTDPS AHYYSLEVNP KFAKIASKII DLAGLSNKVT 
       160        170        180        190        200
IIVGKATDSL VELRRSLPNV IPSFEYLDFV FIDHWKDLYV PDLRVMETLD 
       210        220        230        240        250
LIGQGSIIAA DNILRPGVPE YVKYVQGSLD YRKEYDSTVS NVNGPQFIGK 
       260        270        280 
WNIIYKSKTI KVDDGKREKD AVEITEYIEA K

Length:281

Mass (Da):32,123

Last modified:October 1, 2002 - v1

Checksum:ⁱ24022103FE9993B1

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CU329671 Genomic DNA. Translation: CAD31744.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001018770.1. NM_001020945.2.

Genome annotation databases

EnsemblFungiⁱ	SPBPB21E7.04c.1; SPBPB21E7.04c.1:pep; SPBPB21E7.04c.
GeneIDⁱ	3361178.
KEGGⁱ	spo:SPBPB21E7.04c.

Similar proteinsⁱ

50% Identity

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
Q8NKC1	O42898 G3AVK8 B9WJY7 G8BKS4 H8XA70 Q6BVD9 A0A0V1PRF6 S9PR61 M3JZ05 S9X5M1 +8	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1) Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841) (Yeast) Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis) Candida orthopsilosis (strain 90-125) (Yeast) Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) Debaryomyces fabryi Schizosaccharomyces octosporus (strain yFS286) (Fission yeast) (Octosporomyces octosporus) Candida maltosa (strain Xu316) (Yeast) Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691) (Fission yeast) And more	266	UniRef50_O42898	Cluster: Probable catechol O-methyltransferase 1	19

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	CU329671 Genomic DNA. Translation: CAD31744.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001018770.1. NM_001020945.2.

3D structure databases

ProteinModelPortalⁱ	Q8NKC1.
SMRⁱ	Q8NKC1.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	280254. 2 interactors.
STRINGⁱ	4896.SPBPB21E7.04c.1.

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q8NKC1.
PaxDbⁱ	Q8NKC1.
PRIDEⁱ	Q8NKC1.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	SPBPB21E7.04c.1; SPBPB21E7.04c.1:pep; SPBPB21E7.04c.
GeneIDⁱ	3361178.
KEGGⁱ	spo:SPBPB21E7.04c.

Organism-specific databases

EuPathDBⁱ	FungiDB:SPBPB21E7.04c.
PomBaseⁱ	SPBPB21E7.04c.

Phylogenomic databases

HOGENOMⁱ	HOG000171638.
InParanoidⁱ	Q8NKC1.
KEGG Orthology (KO) More...KOⁱ	K00545.
OMAⁱ	SRFECTH.
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C4KCD.
PhylomeDBⁱ	Q8NKC1.

Enzyme and pathway databases

Reactomeⁱ	R-SPO-156581. Methylation. R-SPO-379397. Enzymatic degradation of dopamine by COMT. R-SPO-379398. Enzymatic degradation of Dopamine by monoamine oxidase.

Reactomeⁱ

R-SPO-156581. Methylation.
R-SPO-379397. Enzymatic degradation of dopamine by COMT.
R-SPO-379398. Enzymatic degradation of Dopamine by monoamine oxidase.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q8NKC1.

PROⁱ

PR:Q8NKC1.

Family and domain databases

InterProⁱ	View protein in InterPro IPR002935. O-MeTrfase_3. IPR029063. SAM-dependent_MTases.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01596. Methyltransf_3. 1 hit.
SUPFAMⁱ	SSF53335. SSF53335. 1 hit.
PROSITEⁱ	View protein in PROSITE PS51682. SAM_OMT_I. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	COMT2_SCHPO
Accessionⁱ	Q8NKC1Primary (citable) accession number: Q8NKC1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
	Last sequence update:	October 1, 2002
	Last modified:	March 28, 2018
	This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q8NKC1 (COMT2_SCHPO)

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Probable catechol O-methyltransferase 2

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<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

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>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 - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

Vacuole

Mitochondrion

Vacuole

<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

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<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

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

<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

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

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ