位置:首页 > 蛋白库 > TRM5_EMENI
TRM5_EMENI
ID   TRM5_EMENI              Reviewed;         478 AA.
AC   C8VJ35; Q5B935;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=tRNA (guanine(37)-N1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE            EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_03152};
DE   AltName: Full=tRNA methyltransferase 5 {ECO:0000255|HAMAP-Rule:MF_03152};
GN   Name=trm5; ORFNames=AN10361;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 in
CC       various cytoplasmic and mitochondrial tRNAs. Methylation is not
CC       dependent on the nature of the nucleoside 5' of the target nucleoside.
CC       This is the first step in the biosynthesis of wybutosine (yW), a
CC       modified base adjacent to the anticodon of tRNAs and required for
CC       accurate decoding. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03152};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC       Rule:MF_03152}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm
CC       {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the
CC       mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. TRM5/TYW2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAA63516.1; Type=Erroneous gene model prediction; Note=The predicted gene AN2945 has been split into 4 genes: AN10350, AN10360, AN10361 and AN10362.; Evidence={ECO:0000305};
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; AACD01000051; EAA63516.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001306; CBF83699.1; -; Genomic_DNA.
DR   RefSeq; XP_660549.1; XM_655457.1.
DR   AlphaFoldDB; C8VJ35; -.
DR   STRING; 162425.CADANIAP00010141; -.
DR   EnsemblFungi; CBF83699; CBF83699; ANIA_10361.
DR   EnsemblFungi; EAA63516; EAA63516; AN2945.2.
DR   GeneID; 2873730; -.
DR   KEGG; ani:AN2945.2; -.
DR   VEuPathDB; FungiDB:AN10361; -.
DR   eggNOG; KOG2078; Eukaryota.
DR   HOGENOM; CLU_001933_0_0_1; -.
DR   InParanoid; C8VJ35; -.
DR   OMA; PKKQMFC; -.
DR   OrthoDB; 788980at2759; -.
DR   Proteomes; UP000000560; Chromosome VI.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0070901; P:mitochondrial tRNA methylation; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_03152; TRM5; 1.
DR   InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025792; tRNA_Gua_MeTrfase_euk.
DR   Pfam; PF02475; Met_10; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Mitochondrion; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing.
FT   CHAIN           1..478
FT                   /note="tRNA (guanine(37)-N1)-methyltransferase"
FT                   /id="PRO_0000414160"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         243
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         281..282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         309..310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
FT   BINDING         367
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03152"
SQ   SEQUENCE   478 AA;  55054 MW;  372A093F57CB872A CRC64;
     MAQSTEDNTR RPRPSDLPEM FRPPVNRAMR VLDRSFFKKT VPLSAATIFK NSDISRVRRA
     LEQSKDILAL PRLNTIQDIK QDDVVKKCLL LKETIRHDDT ATWSPTINEL VDNGVVGVGP
     FDLTLDYDYW LHSDIISAVL PEELLEEVPQ GFTQVGHVAQ LNLREQFIPW RHLIAQVLLD
     KNPTLRTVIR KTEDVGSQSE FRTFPYELLA GDSDMNVIQH EQDCEFRFDF SRVYWNSRLH
     TEHQRLVDLF KPGEMVCDVM AGVGPFAIPA GKKKIFVWAN DLNPHGYEVM QDAVKRNKVF
     KFVTPFNQDG RSFIRWSARA LQKYDPVTVT IQPRTKRTRD ASGQVKETQP PLEVYTRPKV
     FHHYVMNLPG NALEFLDAFI GVYAGCEELF EPHTKEQLPM VHVYCFSGHS ENEVDDHIDI
     CKRMSERLEY PITVEDRVGG AGNTELELSI HNVRLVSPNK QMFCASFRLP RAVAFRKK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024