TRM82_SCLS1
ID TRM82_SCLS1 Reviewed; 517 AA.
AC A7F9K1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit trm82 {ECO:0000255|HAMAP-Rule:MF_03056};
DE AltName: Full=Transfer RNA methyltransferase 82 {ECO:0000255|HAMAP-Rule:MF_03056};
GN Name=trm82; ORFNames=SS1G_14282;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- FUNCTION: Required for the formation of N(7)-methylguanine at position
CC 46 (m7G46) in tRNA. In the complex, it is required to stabilize and
CC induce conformational changes of the catalytic subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03056}.
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03056}.
CC -!- SUBUNIT: Forms a heterodimer with the catalytic subunit trm8.
CC {ECO:0000255|HAMAP-Rule:MF_03056}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03056}.
CC -!- SIMILARITY: Belongs to the WD repeat TRM82 family. {ECO:0000255|HAMAP-
CC Rule:MF_03056}.
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DR EMBL; CH476651; EDO00412.1; -; Genomic_DNA.
DR RefSeq; XP_001584827.1; XM_001584777.1.
DR AlphaFoldDB; A7F9K1; -.
DR SMR; A7F9K1; -.
DR STRING; 665079.A7F9K1; -.
DR EnsemblFungi; EDO00412; EDO00412; SS1G_14282.
DR GeneID; 5480859; -.
DR KEGG; ssl:SS1G_14282; -.
DR VEuPathDB; FungiDB:sscle_04g039750; -.
DR eggNOG; KOG3914; Eukaryota.
DR HOGENOM; CLU_022082_0_0_1; -.
DR InParanoid; A7F9K1; -.
DR OMA; WVFEHDG; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR GO; GO:0106004; P:tRNA (guanine-N7)-methylation; IEA:GOC.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03056; TRM82; 1.
DR InterPro; IPR028884; Trm82.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16288; PTHR16288; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..517
FT /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT subunit trm82"
FT /id="PRO_0000370526"
FT REPEAT 116..158
FT /note="WD 1"
FT REPEAT 260..301
FT /note="WD 2"
FT REPEAT 306..346
FT /note="WD 3"
FT REGION 40..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 56911 MW; 1888F0E25539DC58 CRC64;
MSILRSPYQC LKQCGNYLVA ARGSSIDTFD IKNGSYLSTW KSPVPESMSR SKTTEEETQT
KNEDQNSETA TPEFILESSA PPAKRRKLSI TKESGENTGV VQQSKKKTKN SSPKILEPSP
ITALTITRDL QHVIAVTGED KTIRVLAWED TVEKGLRQIS DRTMPKRPCA LAITDDCNTI
ISADKFGDVY SLPLIPSPLV PSATENASVQ KQAPKMFQPS ASALTVHSAR NLKALEAQKK
QSNKVSEKTG PDFEHKLLLG HVSMLTDILV ATLSGRQYIL TADRDEHIRI SRGIPQAHII
ENFCLGHIEY VSRLCIPPTR PEILISGGGD DDLYTWNWLN GSLLSKTNLK SQVEALDTEK
QSAQEAESKK IAVTGVYHAR DEVSNQDIII ATSEGVPAAF IYFLTASNQL THTQTLALPG
NALSCTFSNP DLSSPFSLII SINNIHEPSS ITTLKDANSS VANPLQFFKY ENEKFVSVQQ
DGFAPQDSEG ILDDQQKNNL CGLLYNVGNL RKMEDEE