TRM61_KLULA
ID TRM61_KLULA Reviewed; 407 AA.
AC Q6CN53;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61;
DE EC=2.1.1.220;
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM61;
DE Short=tRNA(m1A58)MTase subunit TRM61;
GN Name=TRM61; OrderedLocusNames=KLLA0E15290g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase,
CC which catalyzes the formation of N(1)-methyladenine at position 58
CC (m1A58) in initiator methionyl-tRNA. {ECO:0000250|UniProtKB:P46959}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00952};
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRM6 and two copies
CC of TRM61. {ECO:0000250|UniProtKB:P46959}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46959}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
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DR EMBL; CR382125; CAG99723.1; -; Genomic_DNA.
DR RefSeq; XP_454636.1; XM_454636.1.
DR AlphaFoldDB; Q6CN53; -.
DR SMR; Q6CN53; -.
DR STRING; 28985.XP_454636.1; -.
DR PRIDE; Q6CN53; -.
DR EnsemblFungi; CAG99723; CAG99723; KLLA0_E15225g.
DR GeneID; 2894200; -.
DR KEGG; kla:KLLA0_E15225g; -.
DR eggNOG; KOG2915; Eukaryota.
DR HOGENOM; CLU_025402_4_0_1; -.
DR InParanoid; Q6CN53; -.
DR OMA; VVYPKDA; -.
DR Proteomes; UP000000598; Chromosome E.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:EnsemblFungi.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:EnsemblFungi.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR PANTHER; PTHR12133; PTHR12133; 1.
DR Pfam; PF08704; GCD14; 1.
DR PIRSF; PIRSF017269; GCD14; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51620; SAM_TRM61; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..407
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit TRM61"
FT /id="PRO_0000256174"
FT REGION 284..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119..121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT ECO:0000255|PROSITE-ProRule:PRU00952"
FT BINDING 142
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 167..168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT ECO:0000255|PROSITE-ProRule:PRU00952"
SQ SEQUENCE 407 AA; 46707 MW; 2F41301E574C9C2A CRC64;
MSQFFEYKDT IKEGDLVLAW LSRDNLKPIT VKAGEVFNTR YGAFSHSDMI GKPFGSQIAI
RTKGSNRFGF IHVLQPTPEL WSISLPHRTQ IVYTPDSSYI MQRMECNPRS RVIEAGTGSG
SFSHAFARSA GHLFSYEFHE VRYEQAKQEF KEHGLLEAGN TTITHRDVCK DGFEIKNGDT
TSHEFRGPEE TKVELNADCI FLDLPAPWDA IPNLTSVISK EKKVNLCCFS PCIEQVDKTL
EALEEEGWQD VQTVEIQGRQ YEARRQMVRR LDDAIERLRD VKRRKHEGVE KRQKNVEQTS
NNGSSVEATE SDKDLKHTEK THFNPFGKGS RVKEGDSNFE WTQVSKVELE IKSHTSFLTF
ASKIIDRTRD EEQTKAYLAT FKDEGSKLSK REQRRLKAQA NKDIQKE
