(data stored in ACNUC7421 zone)

SWISSPROT: TRM82_ASHGO

ID   TRM82_ASHGO             Reviewed;         450 AA.
AC   Q750U8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 109.
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}; OrderedLocusNames=AGL159W;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
DR   EMBL; AE016820; AAS54332.1; -; Genomic_DNA.
DR   RefSeq; NP_986508.1; NM_211570.1.
DR   STRING; 33169.AAS54332; -.
DR   EnsemblFungi; AAS54332; AAS54332; AGOS_AGL159W.
DR   GeneID; 4622801; -.
DR   KEGG; ago:AGOS_AGL159W; -.
DR   HOGENOM; HOG000111149; -.
DR   InParanoid; Q750U8; -.
DR   KO; K15443; -.
DR   OMA; RISNYPK; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0106143; C:tRNA (m7G46) methyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:EnsemblFungi.
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; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR16288; PTHR16288; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750U8.
DR   SWISS-2DPAGE; Q750U8.
KW   Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT   CHAIN           1..450
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT                   subunit TRM82"
FT                   /id="PRO_0000370511"
FT   REPEAT          108..147
FT                   /note="WD 1"
FT   REPEAT          200..241
FT                   /note="WD 2"
FT   REPEAT          245..285
FT                   /note="WD 3"
SQ   SEQUENCE   450 AA;  50564 MW;  9FE5836AA50E63F4 CRC64;
     MIHPIQFTLT NHDGTLLFCV IKNTIFAYKT NGEDGHLDLA GEWVDDYDSA ELIKAKVEKE
     QQRRLAENAA KKLKTNEGEA IERPGNQRRV PLPGKDPKVP VPGPGAPPVY QYIRCLQLSH
     DEKMLVACTD SDKAAVFFRI ELHKDNCLTL FKRQPFPKRP NAVTFADDDA KLLLADKFGD
     VYAVDSVGEP EKKDPEPILG HVSMLTDIAL VTDTKKSYVI TADRDEHIKI SHYPQSFVID
     KWLFGHKEFV SSLCVPEWQS SMLFSAGGDS FIATWDWQKG LLMSSFDYST IVEPHLTDAH
     LPPARFLAND GSDRREASIS KLLTFKDLPY LVAVPEMTKI VLLLQWDATS GELILSQTLA
     LPLNVVSATV TSANHKLILS LDNREQPGKN FVKIFTLENG KFEEEQAASS SVDEAIVRNL
     SERPEVQTTV DDIYPLYHVS QLRKRGEHYS
//

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