ID A0A319AQM1_ASPLB Unreviewed; 432 AA.
AC A0A319AQM1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_03162};
DE EC=2.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03162};
DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog {ECO:0000256|HAMAP-Rule:MF_03162};
GN ORFNames=BO96DRAFT_406678 {ECO:0000313|EMBL:PYH61884.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH61884.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH61884.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH61884.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and
CC 34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000256|HAMAP-
CC Rule:MF_03162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine
CC = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) +
CC 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42396, Rhea:RHEA-
CC COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74445, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC EC=2.1.1.205; Evidence={ECO:0000256|ARBA:ARBA00035600,
CC ECO:0000256|HAMAP-Rule:MF_03162};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03162}.
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DR EMBL; KZ821338; PYH61884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319AQM1; -.
DR OrthoDB; 119516at2759; -.
DR Proteomes; UP000247441; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0106339; F:tRNA (cytidine(32)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106340; F:tRNA (guanine(34)-2'-O)-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0002181; P:cytoplasmic translation; IEA:UniProtKB-UniRule.
DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1.
DR InterPro; IPR028590; RNA_methyltr_E_TRM7.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10920; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10920:SF12; TRNA (CYTIDINE(32)_GUANOSINE(34)-2'-O)-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03162};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_03162};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_03162};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03162};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03162}.
FT DOMAIN 21..266
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT BINDING 141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT BINDING 183
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
SQ SEQUENCE 432 AA; 47021 MW; DAC38094D8AEE9AD CRC64;
MGKSSKDKRD AYYRLAKEQN WRARSAFKLI QIDEQFDLFE HENPDKVTRV VDLCAAPGSW
SQVLSRVLIK GESFGRRAWV EKKRKEKEAL DRVRNGDNTT TVTSSEDTDM AELKPRKNVK
IVSIDLQPMA PLEGITTLKA DITHPSTIPL LLRALDPEAY DSSTSSTPSA IRPPHPVDLV
ISDGAPDVTG LHDLDIYIQS QLLYSALNLA LGVLRPGGKF VAKIFRGRDV DLLYAQLRTV
FEKVSVAKPR SSRASSLEAF VVCEGFIPPS IHAGTDALKN PIFGGVAVPP AVSADGNVGV
EVVESEDDEA RPVKLARFAP AEATLGAASA ESSQTEARLL HDDSLASVTP TPLAYKSAGE
KFAVENRWIP RFIACGDLSA WDSDASYTLP PDHVSLDPVQ PPTAPPYRRA LELRKEKGGA
YGKTKLGSLG RA
//
