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Q96WV1 (TRMB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
tRNA (guanine-N(7)-)-methyltransferase

EC=2.1.1.33
Alternative name(s):
Transfer RNA methyltransferase 8
tRNA (guanine(46)-N(7))-methyltransferase
tRNA(m7G46)-methyltransferase
Gene names
Name:trm8
ORF Names:SPCPB16A4.04c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length273 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA By similarity. HAMAP-Rule MF_03055

Catalytic activity

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_03055

Pathway

tRNA modification; N(7)-methylguanine-tRNA biosynthesis. HAMAP-Rule MF_03055

Subunit structure

Forms a complex with trm82 By similarity. HAMAP-Rule MF_03055

Subcellular location

Nucleus By similarity HAMAP-Rule MF_03055.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. TrmB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 273273tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_03055
PRO_0000171436

Regions

Region111 – 1122S-adenosyl-L-methionine binding By similarity
Region150 – 1512S-adenosyl-L-methionine binding By similarity
Region248 – 2503S-adenosyl-L-methionine binding By similarity

Sites

Active site1731 By similarity
Binding site881S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1701S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q96WV1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: CD9814860E37855E

FASTA27331,622
        10         20         30         40         50         60 
MSATAKKSAA QLQREEEEAR KKLKRLSKQG GVEGRLPMKR LFRQRAHANV LSDHELEYPR 

        70         80         90        100        110        120 
SPSEMDWSPY YPDFDVESNK KVEIVDIGCG YGGLTVALGP QFPDTLVLGM EIRMQVSDYL 

       130        140        150        160        170        180 
KEKIQALRYR ADHEEPVPGG YKNISVLRMN CQKFLPNFFE KGQLSKMFFC FPDPHFKARK 

       190        200        210        220        230        240 
HKNRIITSTL ASEYAYFIRP HGTLYTITDV EELHVWMAQH LDAHPLFRRF TKEEEENDIC 

       250        260        270 
VTLMTNETEE GKKVARNGGK KFVACYERIP NPK 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329672 Genomic DNA. Translation: CAC39323.1.
RefSeqNP_588028.1. NM_001023019.2.

3D structure databases

ProteinModelPortalQ96WV1.
SMRQ96WV1. Positions 56-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276134. 16 interactions.
MINTMINT-4701684.
STRING4896.SPCPB16A4.04c-1.

Proteomic databases

MaxQBQ96WV1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCPB16A4.04c.1; SPCPB16A4.04c.1:pep; SPCPB16A4.04c.
GeneID2539574.
KEGGspo:SPCPB16A4.04c.

Organism-specific databases

PomBaseSPCPB16A4.04c.

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000260965.
KOK03439.
OMARAHSNPI.
OrthoDBEOG708W9T.
PhylomeDBQ96WV1.

Enzyme and pathway databases

UniPathwayUPA00989.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_03055. tRNA_methyltr_TrmB_euk.
InterProIPR029063. SAM-dependent_MTases-like.
IPR025763. Trm8_euk.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00091. TIGR00091. 1 hit.
PROSITEPS51625. SAM_MT_TRMB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800733.
PROQ96WV1.

Entry information

Entry nameTRMB_SCHPO
AccessionPrimary (citable) accession number: Q96WV1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways