TRM82_LODEL
ID TRM82_LODEL Reviewed; 389 AA.
AC A5E654;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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 {ECO:0000255|HAMAP-Rule:MF_03056}; ORFNames=LELG_05093;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981531; EDK46912.1; -; Genomic_DNA.
DR RefSeq; XP_001523677.1; XM_001523627.1.
DR AlphaFoldDB; A5E654; -.
DR SMR; A5E654; -.
DR STRING; 379508.A5E654; -.
DR EnsemblFungi; EDK46912; EDK46912; LELG_05093.
DR GeneID; 5230847; -.
DR KEGG; lel:LELG_05093; -.
DR VEuPathDB; FungiDB:LELG_05093; -.
DR eggNOG; KOG3914; Eukaryota.
DR HOGENOM; CLU_022082_0_0_1; -.
DR InParanoid; A5E654; -.
DR OMA; PPIYNYI; -.
DR OrthoDB; 937275at2759; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0036265; P:RNA (guanine-N7)-methylation; IEA:InterPro.
DR GO; GO:0030488; P:tRNA methylation; IEA:UniProtKB-UniRule.
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; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16288; PTHR16288; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..389
FT /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT subunit TRM82"
FT /id="PRO_0000370522"
FT REPEAT 44..86
FT /note="WD 1"
FT REPEAT 134..179
FT /note="WD 2"
FT REPEAT 184..222
FT /note="WD 3"
SQ SEQUENCE 389 AA; 43900 MW; F4F4818CDE2A7B0E CRC64;
MKHPFQILTS STDGKLLIAS ASSPSKESSL LLLLPELGDV LCQQNVPQPI YINYLETGPD
KVLITADVDK NITIYKLENN ELHQLKQQQM PKRLSGISTL NNDAIVCDSL GDVYQITIDT
QPAVKKEDLK PLLGHTSPLT AVVAAQYKNP PKSFLITSDR DEHIRVSNYP KSYVIKGFLY
GHTQFVSQIH LFEICKESRL VSGGGEGKLF FWDWFREVLI TEFDLMPYVE EYLHEFHIKK
SSKTKEEQDV QKEQEVENIQ PKYEIGVQKI DSIEGEDGVF IVTLVENTSC LVVVHFTDEA
KHAQTIQLAA PAVTFAIVGN KLFVSLDAEN DNILTIYKFV DGQFVNDDEA QSSIAERIIL
ANPINVEDKS KFAPFYSINQ LRKRGNNYS