TRM82_SCHPO
ID TRM82_SCHPO Reviewed; 421 AA.
AC O74863;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=SPCC18.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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}.
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; CU329672; CAA21427.1; -; Genomic_DNA.
DR PIR; T41156; T41156.
DR RefSeq; NP_588392.1; NM_001023383.2.
DR AlphaFoldDB; O74863; -.
DR SMR; O74863; -.
DR BioGRID; 275816; 76.
DR STRING; 4896.SPCC18.13.1; -.
DR iPTMnet; O74863; -.
DR MaxQB; O74863; -.
DR PaxDb; O74863; -.
DR PRIDE; O74863; -.
DR EnsemblFungi; SPCC18.13.1; SPCC18.13.1:pep; SPCC18.13.
DR GeneID; 2539246; -.
DR KEGG; spo:SPCC18.13; -.
DR PomBase; SPCC18.13; trm82.
DR VEuPathDB; FungiDB:SPCC18.13; -.
DR eggNOG; KOG3914; Eukaryota.
DR HOGENOM; CLU_667571_0_0_1; -.
DR InParanoid; O74863; -.
DR OMA; IPKRCAD; -.
DR PhylomeDB; O74863; -.
DR UniPathway; UPA00989; -.
DR PRO; PR:O74863; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0106143; C:tRNA (m7G46) methyltransferase complex; IC:PomBase.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR GO; GO:0106004; P:tRNA (guanine-N7)-methylation; ISO:PomBase.
DR Gene3D; 2.130.10.10; -; 2.
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; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16288; PTHR16288; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; tRNA processing;
KW WD repeat.
FT CHAIN 1..421
FT /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT subunit trm82"
FT /id="PRO_0000051294"
FT REPEAT 60..99
FT /note="WD 1"
FT REPEAT 176..222
FT /note="WD 2"
FT REPEAT 224..264
FT /note="WD 3"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 421 AA; 47498 MW; 7B78AF95ABD7FDBA CRC64;
MSEQRVFKHP CQFLTWNSKH NYIVCCSGPY LLGFSCSTGE KIFEHCYRDN INEKHREAAA
YGEAIRQVAF SKDYSRMATV SEDKCLRLWD STQPDKIELL YQKNIPKRCA DLCFAGSNEI
VFGDKFGDVY CVDENWFTTS EVTEEKKSNV VEGKQEPVNN DTLKDSKLQK LEPIMGHVSI
LTQLIVAQNP QNSKEEIIIT SDKDEHIRIS RFPNAFVIEG FCLGHEDFVS RMSLYDNRTL
ISGGGDNHVF VWDLENFKCL DAFDLRSAFS TYLSLNQPMV VSVILPIFKR QLVAFACEGM
AGLIFAKVTP EKRLLFHSAL KLSGPVLDAV LLDTDTDQIL ISLDSSFTFG ACFECVKFDE
GNAAVLTKPD VIKRIESDGL ISTEKPFCPL AQIHTLRKNH SKFIRSVETG TSSPSVESKD
N
