ID   TRM6_CRYNB              Reviewed;         560 AA.
AC   P0CS07; Q55VE7; Q5KKT9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 38.
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=CNBC5380;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(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; AAEY01000015; EAL21837.1; -; Genomic_DNA.
DR   RefSeq; XP_776484.1; XM_771391.1.
DR   AlphaFoldDB; P0CS07; -.
DR   SMR; P0CS07; -.
DR   EnsemblFungi; AAW42248; AAW42248; CNC01870.
DR   EnsemblFungi; EAL21837; EAL21837; CNBC5380.
DR   GeneID; 4935203; -.
DR   KEGG; cnb:CNBC5380; -.
DR   VEuPathDB; FungiDB:CNBC5380; -.
DR   HOGENOM; CLU_010916_1_0_1; -.
DR   Proteomes; UP000001435; Chromosome 3.
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; RNA-binding; tRNA processing.
FT   CHAIN           1..560
FT                   /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT                   catalytic subunit TRM6"
FT                   /id="PRO_0000410315"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        148..163
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        546..560
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  62193 MW;  9BD25DC23AE3B652 CRC64;
     MTEKQQNSQQ PSQLDSTASI SALPPQLQQP AAGITGAPGN AEATTSEPPS TKRPRKAIES
     SEPLTEVILR RLTTIKEGDT VLLRLPSDLV KSVVVQGDNL VQLGKYGAFP ASQLIGLHYD
     ITYEIVSSSG SGASTPQPQS LDFSTEETQS KKGNKKNKNK GKDTAAVSKN NPGWNNILRP
     LKRQLVVDAV IDDIVETNEF IEDLSETEKT TLSHDEIAEL RAQGCTPEEI IQAQIARHEK
     FGLKTDFSKE KWRRRKEKKF YQTVQPLAPS IPNVLYHYNL RSPQSILHLR DDTLSQLLTM
     ANVRPGGRYL VVDDTGGLIT AAVLERMGSE GSILLFNESD SPPAWGILQT MNFSDRELEP
     IKWLNWLEAE EEYQKPAPPV QAEPPTNPIK AAAKQRKYAA QVAELNNTRN ELHLGGWDGL
     ILATTLNPIS VVARLTPYLL GSAPIVVYSP YYQVLAELLS WSKKDPNYLN DTLTESWERT
     YQVLPGRTHP MMTTSATGGY LWNATRVHPS QFQPESHQRF KRRKTGKAPG KEQLSSVAKD
     EEAVNESLEI DPEELANEGE