TRM6_DEBHA
ID TRM6_DEBHA Reviewed; 473 AA.
AC Q6BKK7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6;
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6;
DE Short=tRNA(m1A58)MTase subunit TRM6;
GN Name=TRM6; OrderedLocusNames=DEHA2F21032g;
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: Substrate-binding subunit of tRNA (adenine-N(1)-)-
CC methyltransferase, which catalyzes the formation of N(1)-methyladenine
CC at position 58 (m1A58) in initiator methionyl-tRNA.
CC {ECO:0000250|UniProtKB:P41814}.
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRM6 and two copies
CC of TRM61. {ECO:0000250|UniProtKB:P41814}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41814}.
CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG89653.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382138; CAG89653.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_461264.2; XM_461264.2.
DR AlphaFoldDB; Q6BKK7; -.
DR SMR; Q6BKK7; -.
DR STRING; 4959.XP_461264.2; -.
DR EnsemblFungi; CAG89653; CAG89653; DEHA2F21032g.
DR GeneID; 2903972; -.
DR KEGG; dha:DEHA2F21032g; -.
DR eggNOG; KOG1416; Eukaryota.
DR HOGENOM; CLU_010916_2_0_1; -.
DR InParanoid; Q6BKK7; -.
DR OrthoDB; 543764at2759; -.
DR Proteomes; UP000000599; Chromosome F.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IEA:InterPro.
DR InterPro; IPR017423; TRM6.
DR PANTHER; PTHR12945; PTHR12945; 1.
DR Pfam; PF04189; Gcd10p; 1.
DR PIRSF; PIRSF038170; tRNA_m1A_mtfrase; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; RNA-binding; tRNA processing.
FT CHAIN 1..473
FT /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT catalytic subunit TRM6"
FT /id="PRO_0000256163"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 473 AA; 53611 MW; 7FF03E3E9D15CB12 CRC64;
MASVIEDKMN LDREPEVDSL PQREKSTTII SPNQHALIRL PSEGLKIIDL KPGGIISLGK
FGTFAVDGIL GYPFGQTFEI LEELKVKPIK SMTMQADETS VDNENEELTK DDLTKMLSNS
SDNNQNIINI GSKIQKLTSE DVDKLKESGA TSDIGQRIIE QMIAGHEGFD KKTLFSQQKY
LKRKQQKFLR RFTVEYLGSS QLLQYYIEKD TQRVLDMSEE TLGLLLNYAN VRPGGKYLLI
DETGGIILYA MMERMNGQGT IVSAHDNEHP NHIALRYSDY PEEMQNRMVK SINWLQFLEP
ENEKVEFETA TEEEIEEMKH AKRAQYYRRE QRAKNINSVI DMVMEGNFDG FISVSTLNMP
TLLPEIIPTI GGSRPVVIYS QFKEALLETQ HHMSTDKRVL APSIMETRVR PHQTIPGRMH
PVMCMRGFGG YILWGTRVFP RESGITAVGK GSGKSKKEKP EQIPEAVSQQ ASV