TRM10_CRYNB
ID TRM10_CRYNB Reviewed; 429 AA.
AC P0CS11; Q55WD7; Q5KJW1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
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}; OrderedLocusNames=CNBC2000;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000013; EAL22062.1; -; Genomic_DNA.
DR RefSeq; XP_776709.1; XM_771616.1.
DR AlphaFoldDB; P0CS11; -.
DR SMR; P0CS11; -.
DR EnsemblFungi; EAL22062; EAL22062; CNBC2000.
DR GeneID; 4934865; -.
DR KEGG; cnb:CNBC2000; -.
DR VEuPathDB; FungiDB:CNBC2000; -.
DR HOGENOM; CLU_034384_1_1_1; -.
DR Proteomes; UP000001435; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0052905; F:tRNA (guanine(9)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.1280.30; -; 1.
DR InterPro; IPR028564; MT_TRM10-typ.
DR InterPro; IPR038459; MT_TRM10-typ_sf.
DR InterPro; IPR007356; tRNA_m1G_MeTrfase_euk.
DR InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR PANTHER; PTHR13563; PTHR13563; 1.
DR Pfam; PF01746; tRNA_m1G_MT; 1.
DR PROSITE; PS51675; SAM_MT_TRM10; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..429
FT /note="tRNA (guanine(9)-N1)-methyltransferase"
FT /id="PRO_0000410318"
FT DOMAIN 131..379
FT /note="SAM-dependent MTase TRM10-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01012"
FT REGION 383..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..422
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:O14214"
FT BINDING 285..286
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 305
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 309..313
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 317
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 331
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
FT BINDING 344..346
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q12400"
SQ SEQUENCE 429 AA; 48438 MW; 7A2AABEC020D3AC7 CRC64;
MRFHLGLTEA LQEREPNINA SSKDLSLLHF ELYRRSEPIM DIDEESYLNA GPSAPSKIPQ
GGEGDGLQGM SKKAMKRAAK QARLEEIKPL KRAAERERRR QRTAQLAEGY AAGTLSEADK
ELVERRRRVE KERKEAQRRI ESGDQANDWL GGVVIDLGFD DLMTDQEIAS MAQQLGYLYS
SNRTAEKPVR TVIHTTFSPA ASPRLWQRME NFNWHKWSRC HWWEQGLETL KSQLDPSTSI
LSVQSVVSKE TQDKAGIDTK SLLSRLTGPQ VPVDLQAGKH KLVYLSADAE DELLSLSEDE
IYIIGGIVDR NRHKNLCQGK AEQLGIRTAR LPIGTFLEML PTRKALTVNQ VFDILVKYLH
LGDWAAAFEA VIPIRKYAPG RKAKRAKTET KRNEKVEEEV ECTSAEGEED IGVIEESAEV
DPEDVFSNQ
