TR141_SCHPO
ID TR141_SCHPO Reviewed; 248 AA.
AC O74386;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase trm141 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305|PubMed:27354703};
GN Name=trm141 {ECO:0000303|PubMed:27354703, ECO:0000312|PomBase:SPBC3H7.11};
GN ORFNames=SPBC3H7.11 {ECO:0000312|PomBase:SPBC3H7.11};
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=27354703; DOI=10.1261/rna.056259.116;
RA Arimbasseri A.G., Iben J., Wei F.Y., Rijal K., Tomizawa K., Hafner M.,
RA Maraia R.J.;
RT "Evolving specificity of tRNA 3-methyl-cytidine-32 (m3C32) modification: a
RT subset of tRNAsSer requires N6-isopentenylation of A37.";
RL RNA 22:1400-1410(2016).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC mediates N(3)-methylcytidine modification of residue 32 of the tRNA
CC anticodon loop of tRNA(Ser) (PubMed:27354703). N(3)-methylcytidine
CC methylation by trm141 requires the formation of N(6)-
CC dimethylallyladenosine(37) (i6A37) by tit1 as prerequisite
CC (PubMed:27354703). Does not catalyze N(3)-methylcytidine modification
CC of tRNA(Thr) (PubMed:27354703). {ECO:0000269|PubMed:27354703}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) +
CC N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50956, Rhea:RHEA-COMP:12849, Rhea:RHEA-COMP:12851,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74894, ChEBI:CHEBI:82748;
CC Evidence={ECO:0000305|PubMed:27354703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50957;
CC Evidence={ECO:0000269|PubMed:27354703};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking trm141 show abolished N(3)-
CC methylcytidine modification in tRNA(Ser) (PubMed:27354703). Cells
CC lacking trm140 and trm141 show abolished N(3)-methylcytidine
CC modification in tRNAs (tRNA(Ser) and tRNA(Thr)) (PubMed:27354703).
CC {ECO:0000269|PubMed:27354703}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. METL family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA20307.1; -; Genomic_DNA.
DR PIR; T40404; T40404.
DR RefSeq; NP_595764.1; NM_001021665.2.
DR AlphaFoldDB; O74386; -.
DR SMR; O74386; -.
DR BioGRID; 277547; 8.
DR STRING; 4896.SPBC3H7.11.1; -.
DR MaxQB; O74386; -.
DR PaxDb; O74386; -.
DR EnsemblFungi; SPBC3H7.11.1; SPBC3H7.11.1:pep; SPBC3H7.11.
DR GeneID; 2541032; -.
DR KEGG; spo:SPBC3H7.11; -.
DR PomBase; SPBC3H7.11; trm141.
DR VEuPathDB; FungiDB:SPBC3H7.11; -.
DR eggNOG; KOG2361; Eukaryota.
DR HOGENOM; CLU_029724_2_0_1; -.
DR InParanoid; O74386; -.
DR OMA; PEFKANK; -.
DR PhylomeDB; O74386; -.
DR PRO; PR:O74386; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0052735; F:tRNA (cytosine-3-)-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0106217; P:tRNA C3-cytosine methylation; IMP:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR026113; MeTrfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR22809; PTHR22809; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR PIRSF; PIRSF037755; Mettl2_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome; Transferase;
KW tRNA processing.
FT CHAIN 1..248
FT /note="tRNA N(3)-methylcytidine methyltransferase trm141"
FT /id="PRO_0000339157"
FT BINDING 23
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 27
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 63
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
SQ SEQUENCE 248 AA; 28877 MW; 770C85D958B39795 CRC64;
MSGISKLSDF WVEKYKKESK KSWDKFYKRN ETRFFKDRHW LDREFDCYFG LPDKLPLTIL
EVGCGVGNLV YPLLEVQPNL KIYCCDFSPR AIDFVKKHSC YNENRVFPFV NDITEDSLLE
VLGSACIDTL TAIFVLSAIP REKQLRSIKN LASVIKPGGH LVFRDYCDGD FAQEKFMTSG
DPSMIDEQTF VRQDGTLSLF FREEDIAEWM KSAGFGLVTL DRVNRTVDNR KRNLNMKRTF
LQGVWKKL
