TRM82_YEAS6
ID TRM82_YEAS6 Reviewed; 444 AA.
AC B5VG60;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 25-MAY-2022, entry version 51.
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=AWRI1631_43860;
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631;
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
CC -!- FUNCTION: Required for the formation of N(7)-methylguanine at position
CC 46 (m7G46) in tRNA, a modification required to maintain stability of
CC tRNAs; its absence resulting in tRNA decay. In the complex, it is
CC required to stabilize and induce conformational changes of the
CC catalytic subunit. {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; ABSV01000467; EDZ73085.1; -; Genomic_DNA.
DR AlphaFoldDB; B5VG60; -.
DR SMR; B5VG60; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000008988; 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.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Nucleus; Phosphoprotein; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..444
FT /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT subunit TRM82"
FT /id="PRO_0000370530"
FT REPEAT 1..47
FT /note="WD 1"
FT REPEAT 48..99
FT /note="WD 2"
FT REPEAT 100..147
FT /note="WD 3"
FT REPEAT 148..192
FT /note="WD 4"
FT REPEAT 193..237
FT /note="WD 5"
FT REPEAT 238..279
FT /note="WD 6"
FT REPEAT 308..354
FT /note="WD 7"
FT REGION 55..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03774"
SQ SEQUENCE 444 AA; 50461 MW; 68FB0E5C9901CE67 CRC64;
MSVIHPLQNL LTSRDGSLVF AIIKNCILSF KYQSPNHWEF AGKWSDDFDK IQESRNTTAK
EQQGQSSENE NENKKLKSNK GDSIKRTAAK VPSPGLGAPP IYSYIRNLRL TSDESRLIAC
ADSDKSLLVF DVDKTSKNVL KLRKRFCFSK RPNAISIAED DTTVIIADKF GDVYSIDINS
IPEEKFTQEP ILGHVSMLTD VHLIKDSDGH QFIITSDRDE HIKISHYPQC FIVDKWLFGH
KHFVSSICCG KDYLLLSAGG DDKIFAWDWK TGKNLSTFDY SSLIKPYLND QHLAPPRFQN
ENNDIIEFAV SKIIKSKNLP FVAFFVEATK CIIILEMSEK QKGDLALKQI ITFPYNVISL
SAHNDEFQVT LDNKESSGVQ KNFAKFIEYN LNENSFVVNN EKSNEFDSAI IQSVQGDSNL
VTKKEEIYPL YNVSSLRKHG EHYS
