ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8TU01


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name MTRC_METAC
Primary accession number Q8TU01
Secondary accession numbers None
Integrated into Swiss-Prot on November 28, 2003
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 39)
Name and origin of the protein
Protein name Tetrahydromethanopterin S-methyltransferase subunit C
Synonyms EC 2.1.1.86
N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit C
Gene name
Name: mtrC
OrderedLocusNames: MA_0274
From
Methanosarcina acetivorans [TaxID: 2214] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; Methanosarcinaceae; Methanosarcina.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
DOI=10.1101/gr.223902; PubMed=11932238 [NCBI, ExPASy, EBI, Israel, Japan]
Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E., Metcalf W.W., Birren B.;
"The genome of Methanosarcina acetivorans reveals extensive metabolic and physiological diversity.";
Genome Res. 12:532-542(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE010299; AAM03727.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_615247.1; -.
3D structure databases
ModBase Q8TU01.
Enzyme and pathway databases
BioCyc MACE188937:MA0274-MON; -.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005886; Cellular component: plasma membrane (inferred from electronic annotation from HAMAP).
GO:0030269; Molecular function: tetrahydromethanopterin S-methyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0015948; Biological process: methanogenesis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_01096; -; 1.
PBIL [Tree]
InterPro IPR005865; THM_MeTrfase_su_C.
Graphical view of domain structure.
Pfam PF04211; MtrC; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF006530; MtrC; 1.
TIGRFAMs TIGR01148; mtrC; 1.
ProtoNet Q8TU01.
Genome annotation databases
GeneID 1472166; -.
GenomeReviews AE010299_GR; MA_0274.
KEGG mac:MA0274; -.
NMPDR fig|188937.1.peg.273; -.
Phylogenomic databases
HOGENOM Q8TU01; -.
Genome annotation databases
CMR Q8TU01; MA_0274.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; Membrane; Methanogenesis; Methyltransferase; One-carbon metabolism; Transferase; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   267  267     Tetrahydromethanopterin S-methyltransferase subunit C. PRO_0000147520
TRANSMEM   19    39  21     Potential. 
TRANSMEM   40    60  21     Potential. 
TRANSMEM   75    95  21     Potential. 
TRANSMEM   96   116  21     Potential. 
TRANSMEM   131   151  21     Potential. 
TRANSMEM   162   182  21     Potential. 
TRANSMEM   221   241  21     Potential. 
Sequence information
Length: 267 AA [This is the length of the unprocessed precursor] Molecular weight: 26950 Da [This is the MW of the unprocessed precursor] CRC64: FD258F13BE4D92ED [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAGGAGGEA KGGFPPQTIM AIGAIGGLAG IYLGNFMPAQ FSFFGGLGAI CAMVWGADAV 

        70         80         90        100        110        120 
RRVASYGLGT GVPSIGMISL GMGIVAALFG LSVGGIAGPI VSFIAAAIIG AVIGVLANKV 

       130        140        150        160        170        180 
IGMGIPIMEQ AMVEIAGAGT LVIIGLSVVI AGTFDYAEVV EYVVANGYIA LIFIIGGMGI 

       190        200        210        220        230        240 
LHPFNANLGP DEKQDRTLSV AVEKAAIALI ITGFASSLHE GLMAAGLNIA VGVIIWAWAF 

       250        260 
MKYYGYVKRD SYAVVGTGLL PSAEELE 

Q8TU01 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!