TRM10_EMENI
ID TRM10_EMENI Reviewed; 415 AA.
AC Q5B8X0; C8VIW3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=tRNA (guanine(9)-N1)-methyltransferase {ECO:0000250|UniProtKB:Q12400};
DE EC=2.1.1.221 {ECO:0000250|UniProtKB:Q12400};
DE AltName: Full=tRNA methyltransferase 10 {ECO:0000250|UniProtKB:Q12400};
DE AltName: Full=tRNA(m1G9)-methyltransferase {ECO:0000250|UniProtKB:Q12400};
DE Short=tRNA(m1G9)MTase {ECO:0000250|UniProtKB:Q12400};
GN Name=trm10 {ECO:0000250|UniProtKB:Q12400}; ORFNames=AN3010;
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: S-adenosyl-L-methionine-dependent guanine N(1)-
CC methyltransferase that catalyzes the formation of N(1)-methylguanine at
CC position 9 (m1G9) in cytoplasmic tRNA. {ECO:0000250|UniProtKB:Q12400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221;
CC Evidence={ECO:0000250|UniProtKB:Q12400};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O14214}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q12400}. Nucleus
CC {ECO:0000250|UniProtKB:Q12400}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. TRM10 family. {ECO:0000255|PROSITE-ProRule:PRU01012}.
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DR EMBL; AACD01000051; EAA63581.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF83571.1; -; Genomic_DNA.
DR RefSeq; XP_660614.1; XM_655522.1.
DR AlphaFoldDB; Q5B8X0; -.
DR SMR; Q5B8X0; -.
DR STRING; 162425.CADANIAP00010069; -.
DR PRIDE; Q5B8X0; -.
DR EnsemblFungi; CBF83571; CBF83571; ANIA_03010.
DR EnsemblFungi; EAA63581; EAA63581; AN3010.2.
DR GeneID; 2873735; -.
DR KEGG; ani:AN3010.2; -.
DR eggNOG; KOG2967; Eukaryota.
DR HOGENOM; CLU_034384_0_0_1; -.
DR InParanoid; Q5B8X0; -.
DR OMA; FKKNDGW; -.
DR OrthoDB; 1396299at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR016653; TRM10/TRM10A.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR PANTHER; PTHR13563:SF13; PTHR13563:SF13; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..415
FT /note="tRNA (guanine(9)-N1)-methyltransferase"
FT /id="PRO_0000060515"
FT DOMAIN 140..358
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 289
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14214"
FT BINDING 265..266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 285
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 289..293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 311
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 323..325
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
SQ SEQUENCE 415 AA; 46963 MW; 6BAEC34EA09F58A2 CRC64;
MEEEERPRKI QKLGSSEAHE SEPLITGAIK GSQDDTSPAE QTNSQKAIPG ATTDNSKESE
EPASSTATDG PETTEQKISK RQLRRQAKLE QWEAKREERK IIRKQKTAAR KERRRELWEE
AKREGKDPNE ELNKLFPMTT RTRHRKSTRL PLTLIIDCGF DDLMQDKERV SLGQQLTRSY
SENNKSAFNG HLIISSFNKK LKERFETVLH KTHEGWKGVR FTGEDWLQAA KEASEVMQGP
NGGKLVGPFE DKTDAKPEDG EIVYLTSDSS ETLTELKPYS TYIIGGLVDK NRHKGICHKR
ATELGIRTAK LPIGQYIQMN SRPVLATNHV VEIMVRWLQL RDWAEAFMQT LPPRKGGALK
DSVKGQRDST PRDDVESNTE KGTVSETVED TEATEPAEAV TPKDIDAVQE NKQDE
