TR140_SCHPO
ID TR140_SCHPO Reviewed; 307 AA.
AC Q9P7L6;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=tRNA N(3)-methylcytidine methyltransferase trm140 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305|PubMed:27354703};
GN Name=trm140 {ECO:0000303|PubMed:27354703,
GN ECO:0000312|PomBase:SPBC21C3.07c};
GN ORFNames=SPBC21C3.07c {ECO:0000312|PomBase:SPBC21C3.07c};
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 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(Thr) (PubMed:27354703). Does not catalyze N(3)-
CC methylcytidine modification of tRNA(Ser) (PubMed:27354703).
CC {ECO:0000269|PubMed:27354703}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) +
CC N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:50960, Rhea:RHEA-COMP:12850, Rhea:RHEA-COMP:12852,
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:50961;
CC Evidence={ECO:0000305|PubMed:27354703};
CC -!- DISRUPTION PHENOTYPE: Cells lacking trm140 show abolished N(3)-
CC methylcytidine modification in tRNA(Thr) (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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB76043.2; -; Genomic_DNA.
DR PIR; T50351; T50351.
DR RefSeq; NP_596587.2; NM_001022507.3.
DR AlphaFoldDB; Q9P7L6; -.
DR SMR; Q9P7L6; -.
DR BioGRID; 276851; 2.
DR STRING; 4896.SPBC21C3.07c.1; -.
DR MaxQB; Q9P7L6; -.
DR PaxDb; Q9P7L6; -.
DR PRIDE; Q9P7L6; -.
DR EnsemblFungi; SPBC21C3.07c.1; SPBC21C3.07c.1:pep; SPBC21C3.07c.
DR GeneID; 2540321; -.
DR KEGG; spo:SPBC21C3.07c; -.
DR PomBase; SPBC21C3.07c; trm140.
DR VEuPathDB; FungiDB:SPBC21C3.07c; -.
DR eggNOG; KOG2361; Eukaryota.
DR HOGENOM; CLU_029724_1_1_1; -.
DR InParanoid; Q9P7L6; -.
DR OMA; PAKWWNL; -.
DR PhylomeDB; Q9P7L6; -.
DR PRO; PR:Q9P7L6; -.
DR Proteomes; UP000002485; Chromosome II.
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 Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..307
FT /note="tRNA N(3)-methylcytidine methyltransferase trm140"
FT /id="PRO_0000204457"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 176
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8TCB7"
SQ SEQUENCE 307 AA; 35836 MW; 6796182A8D2104EC CRC64;
MDTTPDNSEK KKTSSVREAT FSINESFGGR LLTEEEDVFE QNAWDHVEWD DEHLALAKKC
IEEQKLYPVT EKDAYMTHPE RYWDQFYGKN EGKFFMNRRW IAQEFPELLD LLKEDAGEKS
ILEIGCGAGN TIWPILKENK NSNLKIFAVD YSEKAIDVVK QNPLYDAKFC SASVWDLAGS
DLLRSIEEAS IDAITLIFCF SALSPDQWQQ AIENLYRLLK PGGLILFRDY GRLDLTQLRA
KKNRILSENF YIRGDGTRVY YMTNEELVDV FGKNFKIIQN GVDKRLIVNR KKRVKMYRCW
LQAKFQK
