TRM9_SCHPO
ID TRM9_SCHPO Reviewed; 228 AA.
AC Q10224;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=tRNA (carboxymethyluridine(34)-5-O)-methyltransferase;
DE EC=2.1.1.229;
DE AltName: Full=tRNA (uracil-5-)-methyltransferase trm9;
DE AltName: Full=tRNA [Um34] methyltransferase;
DE AltName: Full=tRNA methylase 9;
GN Name=trm9; ORFNames=SPAC13D6.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Required for the methylation of the wobble bases at position
CC 34 in tRNA. Appears to have a role in stress-response (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carboxymethyluridine(34) in tRNA + S-adenosyl-L-methionine =
CC 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:43208, Rhea:RHEA-COMP:10407, Rhea:RHEA-
CC COMP:10408, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74851,
CC ChEBI:CHEBI:74882; EC=2.1.1.229;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAA93543.1; -; Genomic_DNA.
DR PIR; T37623; T37623.
DR RefSeq; NP_593681.1; NM_001019113.2.
DR AlphaFoldDB; Q10224; -.
DR SMR; Q10224; -.
DR BioGRID; 279350; 6.
DR STRING; 4896.SPAC13D6.03c.1; -.
DR MaxQB; Q10224; -.
DR PaxDb; Q10224; -.
DR EnsemblFungi; SPAC13D6.03c.1; SPAC13D6.03c.1:pep; SPAC13D6.03c.
DR GeneID; 2542906; -.
DR KEGG; spo:SPAC13D6.03c; -.
DR PomBase; SPAC13D6.03c; trm9.
DR VEuPathDB; FungiDB:SPAC13D6.03c; -.
DR eggNOG; KOG1331; Eukaryota.
DR HOGENOM; CLU_029501_2_0_1; -.
DR InParanoid; Q10224; -.
DR OMA; TREYAWP; -.
DR PhylomeDB; Q10224; -.
DR PRO; PR:Q10224; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0106335; F:tRNA (carboxymethyluridine(34)-5-O)-methyltransferase activity; ISS:PomBase.
DR GO; GO:0016300; F:tRNA (uracil) methyltransferase activity; ISO:PomBase.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; ISO:PomBase.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR032873; Trm9.
DR PANTHER; PTHR13069:SF21; PTHR13069:SF21; 2.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..228
FT /note="tRNA (carboxymethyluridine(34)-5-O)-
FT methyltransferase"
FT /id="PRO_0000116489"
SQ SEQUENCE 228 AA; 26277 MW; 05CC5AD1A53B8C9A CRC64;
MEIEYENEYV HQVYDKIATH FSDTRYKPWP VVEKFLKSLP LGSVGVDIGC GNGKYQKVNP
NVYMIGSDRC VKLVKIASNL GPMVISDGLH VPHPSNRFDF ALSIAVIHHF SNENRRLQAV
QEVLRPLVKG GKALFFVWAL EQKNSRRGFS EDGPQDVYVP WILKRQYEYP NAKPEELKGH
DPAENIAYQR YYHLFRKGEL NELVETAGGS ILEHGYDRDN WWVIAEKN
