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TRM61_YARLI
ID   TRM61_YARLI             Reviewed;         389 AA.
AC   Q6C0P9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=YALI0F22737g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382132; CAG78574.1; -; Genomic_DNA.
DR   RefSeq; XP_505763.1; XM_505763.1.
DR   AlphaFoldDB; Q6C0P9; -.
DR   SMR; Q6C0P9; -.
DR   STRING; 4952.CAG78574; -.
DR   EnsemblFungi; CAG78574; CAG78574; YALI0_F22737g.
DR   GeneID; 2908809; -.
DR   KEGG; yli:YALI0F22737g; -.
DR   VEuPathDB; FungiDB:YALI0_F22737g; -.
DR   HOGENOM; CLU_025402_4_0_1; -.
DR   InParanoid; Q6C0P9; -.
DR   OMA; VVYPKDA; -.
DR   Proteomes; UP000001300; Chromosome F.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
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..389
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT                   subunit TRM61"
FT                   /id="PRO_0000256176"
FT   REGION          278..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         112..114
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         133
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         138
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         160..161
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT   BINDING         181
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   389 AA;  44103 MW;  8EB480F904DCD849 CRC64;
     MFSAYKDTIE DGDLVLGWMT RTAIKPIVVE KKEGLFNTRY GAFPHRNMDK YGAQLGSMSK
     QGFIHLIHPT PELWTLSLPH RTQIVYTTDS SYIVQRLKIR PGSTVIESGT GSGSFTHAIS
     RSAGLAGKVY SYEFHEERYN LAKQEFERHQ LTNVIPTHRD VCNDGFDIEN IDVNATAVFL
     DLPAPWTAIP HLERVIDRSV VSRVCCFSPC FEQVVKAVQA LQEAGWVDIE MVEVAAKRWE
     SRLEMKRSLD EAITRLRDVK ARRETGLAKR NARIKVETET GVEEEESDER DAKRSKTESG
     HRGYNPWGKG QKIKEGDESF EWTEVSKCEQ EIKSHTSYLL FASRLPKLGE EVFDKDMCVR
     PYSERCPETS TEGAEASTEA TEAPARTEA
 
 
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