ID   TRM6_ASPOR              Reviewed;         578 AA.
AC   Q2UJ66;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
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; ORFNames=AO090003001339;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007155; BAE58399.1; -; Genomic_DNA.
DR   RefSeq; XP_001820401.1; XM_001820349.2.
DR   AlphaFoldDB; Q2UJ66; -.
DR   STRING; 510516.Q2UJ66; -.
DR   EnsemblFungi; BAE58399; BAE58399; AO090003001339.
DR   GeneID; 5992384; -.
DR   KEGG; aor:AO090003001339; -.
DR   VEuPathDB; FungiDB:AO090003001339; -.
DR   HOGENOM; CLU_010916_2_0_1; -.
DR   OMA; PFYLTFE; -.
DR   Proteomes; UP000006564; Chromosome 2.
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.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; RNA-binding; tRNA processing.
FT   CHAIN           1..578
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT                   catalytic subunit trm6"
FT                   /id="PRO_0000256159"
FT   REGION          253..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..284
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        459..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   578 AA;  64585 MW;  B8B4D3C24E6B4A42 CRC64;
     MHSYVRPNQF VALRLPSEFT KIQKIEPDST VFLGKFGSFP ANQIIGRPFY LTFEILDDAD
     EKDGSCLRII PAAELHAETL IAEGEGDGEE LDTNEDGTPM RTNREIVDDA STQKLTWEEI
     EALKKESGGA GREIISKLLE SHQTLDQKTS FSLAKYMLRK RRKYMKRFTV LPLDVSILTN
     HMMEDQGAAR IMELRDEMVG LLGCWGNVHH GGDASLDEAI AAKPNGRYLV VDDTGGLVVA
     AMAERMGILY PHDGDEYEEQ GSSDEPKKNE AEQAHDDEQP PTESSTHRPA RPAHMSASGN
     SITVLHPNKQ PNLSLLKYFG YSQDNPDETH PLHKHLKTIS WLQLLDPNAD PIYSEEPEII
     PESELYTMKS NKRGAYYRKR NRWTRVQSVV NEARAGEFDG LIVATVMDPS SVLKYAVPLL
     AGSAHVAVYS PSIEPLTELS DLYSTAKKTA FINRRQQLRE QKLQQSSDQP DANETELQDS
     DLSELMAEFY LDPTLLLAPT LQNSRVRPWQ VLPGRTHPLM SMRGGAEGYI FHAVRVIPTQ
     QTIQAAGNLS RKKRKVVTQE TPTTAVDSGS GVDVEMKS