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Reviewed, UniProtKB/Swiss-Prot Q9P804 (TRM1_SCHPO)

Last modified June 16, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    N(2),N(2)-dimethylguanosine tRNA methyltransferase
    EC=2.1.1.32
Alternative name(s):
    tRNA(guanine-26,N(2)-N(2)) methyltransferase
    tRNA 2,2-dimethylguanosine-26 methyltransferase
    tRNA(m(2,2)G26)dimethyltransferase
Gene names
Name: trm1
ORF Names: SPBC25D12.05
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Catalytic activity

S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing N(2)-methylguanine.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: Nuclear/cytoplasmic compartments By similarity.

Sequence similarities

Belongs to the TRM1 family.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
Nucleus
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: GeneDB_SPombe

nucleus

Inferred from direct assay. Source: GeneDB_SPombe

   Molecular functionRNA binding

Inferred from electronic annotation. Source: InterPro

tRNA (guanine-N2-)-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 548548N(2),N(2)-dimethylguanosine tRNA methyltransferase
PRO_0000147677

Experimental info

Sequence conflict3221S → T in CAA11801. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9P804-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E0DD19178A6B4959

FASTA54860,297
        10         20         30         40         50         60 
MYEANMLRLS QRISNAVNHF STAMMSGASA SLTEGSAIIP FSNPNEVFYN PVQQFNRDLS 

        70         80         90        100        110        120 
VTAIRAWSET RSKKIVAKSH HRHQLLDQNS ELSQENLTKC DTTHDFEKNC SEKTDSTSAD 

       130        140        150        160        170        180 
NIAGFTILEA LSATGLRSIR YAKELPNVKR ILANDLLENA VKTIEKNVNY NNVSDIVIPN 

       190        200        210        220        230        240 
KGDANAVMHM NKFHYDVIDL DPYGSAAPFL DAAVQSVSKD GLLCITCTDS AVLAGNAYPE 

       250        260        270        280        290        300 
KCFSNYGGSS LRSNFCHEQA VRHLLYAIAA SAAKYGRAIK PLLSLSIDFY FRVFVQIKAK 

       310        320        330        340        350        360 
PVLVKNLQSQ SLLIYHCSGC GSFAEQPLGK TSPGRLPGTT KFSNASGPPV SANCEHCGYV 

       370        380        390        400        410        420 
HHVGGPLWGG PLHDAEFLKK MRAIAEDLDP EVYGTKRRIL GMLALADEEL PDVPFYFVLS 

       430        440        450        460        470        480 
QICSVLRSQS PPQNIFVSAL LNAGYRVSGS HAKSNAIKTN APWSFVWDVL RSWIKDHPVK 

       490        500        510        520        530        540 
LENISKTSAG AAILEKTPTA EVDFTFRPDS EFASKKEGYT RYQMNPTENW GPKSKPGKRT 


IAEVDSKS 

« Hide

References

« Hide 'large scale' references
[1]"The tRNA N2,N2-dimethylguanosine-26 methyltransferase encoded by gene trm1 increases efficiency of suppression of an ochre codon in Schizosaccharomyces pombe."
Niederberger C., Graub R., Costa A., Desgres J., Schweingruber M.E.
FEBS Lett. 464:67-70(1999) [PubMed: 10611485] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

Cross-references

Sequence databases

AJ224000 Genomic DNA. Translation: CAA11801.1.
CU329671 Genomic DNA. Translation: CAA20101.2.
PIRT39993.
T46565.
RefSeqNP_596547.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2540604.
KEGGspo:SPBC25D12.05.
NMPDRfig|4896.1.peg.2413.

Organism-specific databases

GeneDB_SpombeSPBC25D12.05.

Phylogenomic databases

OMAQ9P804. AAMENGT.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-004543-MON.
BRENDA2.1.1.32. 653.

Gene expression databases

ArrayExpressQ9P804.

Family and domain databases

InterProIPR002905. TRM_MeTrfase.
[Graphical view]
PANTHERPTHR10631. TRM_mtfrase. 1 hit.
PfamPF02005. TRM. 1 hit.
[Graphical view]
TIGRFAMsTIGR00308. TRM1. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTRM1_SCHPO
AccessionPrimary (citable) accession number: Q9P804
Secondary accession number(s): O74566
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents