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Entry version 39 (11 Dec 2019)
Sequence version 1 (05 May 2009)
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Protein

Tryptophan 2-C-methyltransferase

Gene

tsrM

Organism
Streptomyces laurentii
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Involved in the biosynthetic pathway of the antibiotic thiostrepton A. First, TsrM catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to cobalamin, leading to the formation of methylcobalamin (CH3-cobalamin) and S-adenosyl-L-homocysteine (SAH). Then the methyl group is transferred to the C2 position of tryptophan (Trp) with the concerted action of the radical SAM [4Fe-4S] center, leading to the production of methyltryptophan.3 Publications

Miscellaneous

TsrM has a totally new mechanism among methyltransferases and radical SAM enzymes. TsrM is not able to use methylcobalamin directly but instead coordinates free cobalamin. SAM serves exclusively as a methyl donor and not as a radical source, and the methyl group of SAM is not directly transferred to tryptophan.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi253Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1
Metal bindingi257Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1
Metal bindingi260Iron-sulfur (4Fe-4S-S-AdoMet)1 Publication1

<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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processAntibiotic biosynthesis
Ligand4Fe-4S, Cobalamin, Cobalt, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:MONOMER-19353

<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 subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Tryptophan 2-C-methyltransferaseCurated (EC:2.1.1.1061 Publication)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tsrM1 Publication
Synonyms:trsT
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiStreptomyces laurentii
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri39478 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi253C → A: Loss of methyltransferase activity. 1 Publication1
Mutagenesisi257C → A: Loss of methyltransferase activity. 1 Publication1
Mutagenesisi260C → A: Loss of methyltransferase activity. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004353081 – 599Tryptophan 2-C-methyltransferaseAdd BLAST599

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini4 – 149B12-bindingPROSITE-ProRule annotationAdd BLAST146

Phylogenomic databases

KEGG Orthology (KO)

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KOi
K21551

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.80.30.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR030969 B12_rSAM_trp_MT
IPR006158 Cobalamin-bd
IPR006638 Elp3/MiaB/NifB
IPR007197 rSAM
IPR023404 rSAM_horseshoe

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02310 B12-binding, 1 hit
PF04055 Radical_SAM, 1 hit

Structure-Function Linkage Database

More...
SFLDi
SFLDF00322 tryptophan_2-C-methyltransfera, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00729 Elp3, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR04428 B12_rSAM_trp_MT, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51332 B12_BINDING, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

C0JRZ9-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRKGTVALI NPNQIHPPIA PYALDVLTTA LEASGFEAHV LDLTFHLDDW
60 70 80 90 100
RQTLRDYFRA ERPLLVGVTC RNTDTVYALE QRPFVDGYKA VIDEVRRLTA
110 120 130 140 150
APVVAGGVGF STMPFALVDY FGIEYGVKGP GEKIICDLAR ALAEGRSADR
160 170 180 190 200
IHIPGLLVNR GPGNVTRVAP PALDPRAAPA PSSSPSPSPA PSSSSAPVPV
210 220 230 240 250
PLSFAAVGHH ESRAWQAETE LPYTRRSGEP YKVDNLRYYR EGGLGSILTK
260 270 280 290 300
NGCVYKCSFC VEPDAKGTQF ARRGITAVVD EMEALTAQGI HDLHTTDSEF
310 320 330 340 350
NLSIAHSKNL LREIVRRRDH DATSPLRDLR LWVYCQPSPF DEEFAELLAA
360 370 380 390 400
AGCAGVNIGA DHTRPEMLDG WKVTAKGTRY YDFADTERLV QLCHRNGMLT
410 420 430 440 450
MVEALFGMPG ETLETMRDCV DRMMELDATV TGFSLGLRLL PYMGLAKSLA
460 470 480 490 500
EQCDGVRTVR GLQSNNASGP IVLKQLHQCD GPIEYERQFM FDESGDFRLV
510 520 530 540 550
CYFSPDLPEA PGTADSPDGI WRASVDFLWD RIPKSEQYRV MLPTLSGSSE
560 570 580 590
NDNNYADNPF LTSLNRKGYT GAFWAHWRDR EAIMSGATLP LGELAEAVR
Length:599
Mass (Da):66,061
Last modified:May 5, 2009 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA3829A2EEE2C851A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
FJ652572 Genomic DNA Translation: ACN52303.1
FJ436358 Genomic DNA Translation: ACN80682.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ag:ACN52303

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ652572 Genomic DNA Translation: ACN52303.1
FJ436358 Genomic DNA Translation: ACN80682.1

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Genome annotation databases

KEGGiag:ACN52303

Phylogenomic databases

KOiK21551

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19353

Family and domain databases

Gene3Di3.80.30.20, 1 hit
InterProiView protein in InterPro
IPR030969 B12_rSAM_trp_MT
IPR006158 Cobalamin-bd
IPR006638 Elp3/MiaB/NifB
IPR007197 rSAM
IPR023404 rSAM_horseshoe
PfamiView protein in Pfam
PF02310 B12-binding, 1 hit
PF04055 Radical_SAM, 1 hit
SFLDiSFLDF00322 tryptophan_2-C-methyltransfera, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR04428 B12_rSAM_trp_MT, 1 hit
PROSITEiView protein in PROSITE
PS51332 B12_BINDING, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTSRM_STRLU
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: C0JRZ9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 20, 2016
Last sequence update: May 5, 2009
Last modified: December 11, 2019
This is version 39 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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