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O42898

- COMT1_SCHPO

UniProt

O42898 - COMT1_SCHPO

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Protein

Probable catechol O-methyltransferase 1

Gene

SPBC119.03

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei78 – 781S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei86 – 861S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei106 – 1061S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei107 – 1071S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Binding sitei135 – 1351S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi162 – 1621MagnesiumBy similarity
Binding sitei162 – 1621S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei165 – 1651SubstrateBy similarity
Metal bindingi190 – 1901MagnesiumBy similarity
Metal bindingi191 – 1911MagnesiumBy similarity
Binding sitei191 – 1911SubstrateBy similarity

GO - Molecular functioni

  1. catechol O-methyltransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. catecholamine metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Catecholamine metabolism

Keywords - Ligandi

Magnesium, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_232591. Enzymatic degradation of dopamine by COMT.
REACT_246604. Enzymatic degradation of Dopamine by monoamine oxidase.
REACT_261472. Methylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable catechol O-methyltransferase 1 (EC:2.1.1.6)
Gene namesi
ORF Names:SPBC119.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC119.03.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 266266Probable catechol O-methyltransferase 1PRO_0000318148Add
BLAST

Proteomic databases

MaxQBiO42898.
PaxDbiO42898.

Interactioni

Protein-protein interaction databases

BioGridi276612. 1 interaction.
MINTiMINT-4673835.
STRINGi4896.SPBC119.03-1.

Structurei

3D structure databases

ProteinModelPortaliO42898.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG4122.
HOGENOMiHOG000171638.
InParanoidiO42898.
OMAiFIDHYKP.
OrthoDBiEOG7KM644.
PhylomeDBiO42898.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR002935. O-MeTrfase_3.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10509. PTHR10509. 1 hit.
PfamiPF01596. Methyltransf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51682. SAM_OMT_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O42898-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPHMEDNGSE KEQLFLQHIQ NLPQERLDAI RGHPELVLKE IDEFTYPDGS 
        60         70         80         90        100
GVRMCIGDVK GGFIVGKIRE RKPKIMVELG GYLGYSAILF GNEISKIPGG 
       110        120        130        140        150
RYYSLEVNED YAKIAYELVK LAGLDEIVTI MIGKACDSLV ELQQKLLHKD 
       160        170        180        190        200
LGFQALDMVF IDHWKDLYVP DLRVIESLNM IAPGTLLVAD NIITPGAPEY 
       210        220        230        240        250
HKYVNMSPEE RRGYQAKVRN VNGFDFIGRW DLIYKTETKE FEGVIRNKHR 
       260 
KDAVDVTECV GYAKKD
Length:266
Mass (Da):30,267
Last modified:June 1, 1998 - v1
Checksum:i99316BCF4FAED5EA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA17918.1.
PIRiT39301.
RefSeqiNP_595284.1. NM_001021191.2.

Genome annotation databases

EnsemblFungiiSPBC119.03.1; SPBC119.03.1:pep; SPBC119.03.
GeneIDi2540074.
KEGGispo:SPBC119.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 CU329671 Genomic DNA. Translation: CAA17918.1 .
PIRi T39301.
RefSeqi NP_595284.1. NM_001021191.2.

3D structure databases

ProteinModelPortali O42898.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 276612. 1 interaction.
MINTi MINT-4673835.
STRINGi 4896.SPBC119.03-1.

Proteomic databases

MaxQBi O42898.
PaxDbi O42898.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC119.03.1 ; SPBC119.03.1:pep ; SPBC119.03 .
GeneIDi 2540074.
KEGGi spo:SPBC119.03.

Organism-specific databases

PomBasei SPBC119.03.

Phylogenomic databases

eggNOGi COG4122.
HOGENOMi HOG000171638.
InParanoidi O42898.
OMAi FIDHYKP.
OrthoDBi EOG7KM644.
PhylomeDBi O42898.

Enzyme and pathway databases

Reactomei REACT_232591. Enzymatic degradation of dopamine by COMT.
REACT_246604. Enzymatic degradation of Dopamine by monoamine oxidase.
REACT_261472. Methylation.

Miscellaneous databases

NextBioi 20801211.
PROi O42898.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR002935. O-MeTrfase_3.
IPR029063. SAM-dependent_MTases.
[Graphical view ]
PANTHERi PTHR10509. PTHR10509. 1 hit.
Pfami PF01596. Methyltransf_3. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51682. SAM_OMT_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Entry informationi

Entry nameiCOMT1_SCHPO
AccessioniPrimary (citable) accession number: O42898
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 1998
Last modified: January 7, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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