TRM61_DEBHA
ID TRM61_DEBHA Reviewed; 369 AA.
AC Q6BX32; B5RSY8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=DEHA2B06380g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAR65457.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382134; CAR65457.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002770087.1; XM_002770041.1.
DR AlphaFoldDB; Q6BX32; -.
DR SMR; Q6BX32; -.
DR STRING; 4959.XP_002770087.1; -.
DR EnsemblFungi; CAR65457; CAR65457; DEHA2B06380g.
DR GeneID; 8998194; -.
DR KEGG; dha:DEHA2B06380g; -.
DR eggNOG; KOG2915; Eukaryota.
DR HOGENOM; CLU_025402_4_0_1; -.
DR InParanoid; Q6BX32; -.
DR OrthoDB; 1032689at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro.
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..369
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit TRM61"
FT /id="PRO_0000256173"
FT BINDING 114..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 135
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 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 163..164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 192
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 369 AA; 41909 MW; B501778492BB2EAD CRC64;
MSFFEYKDII EEGDLVLAFL GRSNIKPITV TKGSQLNTRY GNFEHDRMIG MKYGEQMPGA
KGVGFIHLLY PTPELWTVSL PHRTQIVYTP DSSYIIQRLN VTSGTRVIEA GTGSGSFSHS
FARTIGVEGR LFTYEFHEPR YIEAKKELED HGLLANTVIT HRDVCNDGFE ISNIPEDFKK
DDGICGDVVF LDLPSPWTAI PNLKSVISHQ SRVGICCFSP CIEQVEKTVK ALETEGWSNI
EMVEVAGKRW EARKDMVKDV KDVVKRLKDI QSRKNQGIEH RKQSKIHNVG DKRDIKEVET
ADDSSPEPTK FQNLGKGFNP FGKGLRVREG DEQFQWRNVT KIESEIKSHT SYLTFAYMNP
NVRLNTSVE
