ID   TRM6_YARLI              Reviewed;         487 AA.
AC   Q6CF35;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=YALI0B10582g;
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: 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}.
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DR   EMBL; CR382128; CAG82972.1; -; Genomic_DNA.
DR   RefSeq; XP_500727.1; XM_500727.1.
DR   AlphaFoldDB; Q6CF35; -.
DR   SMR; Q6CF35; -.
DR   STRING; 4952.CAG82972; -.
DR   EnsemblFungi; CAG82972; CAG82972; YALI0_B10582g.
DR   GeneID; 2907608; -.
DR   KEGG; yli:YALI0B10582g; -.
DR   VEuPathDB; FungiDB:YALI0_B10582g; -.
DR   HOGENOM; CLU_010916_2_0_1; -.
DR   InParanoid; Q6CF35; -.
DR   OMA; TFHNRTE; -.
DR   Proteomes; UP000001300; Chromosome B.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:EnsemblFungi.
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..487
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT                   catalytic subunit TRM6"
FT                   /id="PRO_0000256166"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..487
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  55432 MW;  32E0D912BFD40324 CRC64;
     MKDAAQQQEP VSARQTQVHR KSSKPESPPF IFDNPRIQPN TYCMVKLPSE NFRVVKLIPN
     QTISIGKFGS FQVNDILGLP YGYTFEIQED KRLRIIQEGV DDHDYVVGAK GALLEPEETN
     QTLIDTSESQ TLSMAEIEEM KKQKTLSGKD IIDHVIKGHN EFHKKTAFSK EKYLRRKEQK
     YLRRFTPQPM CSSLLLDFYL EKDYKKVLDM SQEMLALLLS MANVRPGGKY LVVDETTGVL
     TAALMERMAG EGLIVVAHEN EHPNLDALKY LSMPTELQDR MIKSINWLQF FEPEGEEEVP
     EKTPEQIASM KPRNRGAYFR KRNRWLELQN VNDLVANQGF DGLIVASTLH PASIVDRTLH
     AIGGSRPVVV YSEYKEVVTE VSQLMLKDLR VLAPSIWESR VRKYQTILGR MHPSMTSRGG
     GGYLVHGTRV FPNEEVNATQ VRNRKRKRED GDKTKSSETE GKSEESVEPD TEQSAEPEAK
     LETDADA