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Database: UniProt
Entry: A0A194QTY9_PAPMA
LinkDB: A0A194QTY9_PAPMA
Original site: A0A194QTY9_PAPMA 
ID   A0A194QTY9_PAPMA        Unreviewed;       289 AA.
AC   A0A194QTY9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
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=RR48_12213 {ECO:0000313|EMBL:KPJ08460.1};
OS   Papilio machaon (Old World swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ08460.1, ECO:0000313|Proteomes:UP000053240};
RN   [1] {ECO:0000313|EMBL:KPJ08460.1, ECO:0000313|Proteomes:UP000053240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ08460.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPJ08460.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
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; KQ461154; KPJ08460.1; -; Genomic_DNA.
DR   RefSeq; XP_014367275.1; XM_014511789.1.
DR   AlphaFoldDB; A0A194QTY9; -.
DR   STRING; 76193.A0A194QTY9; -.
DR   GeneID; 106717859; -.
DR   KEGG; pmac:106717859; -.
DR   InParanoid; A0A194QTY9; -.
DR   OMA; FIVCLNF; -.
DR   OrthoDB; 119516at2759; -.
DR   Proteomes; UP000053240; 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   CDD; cd02440; AdoMet_MTases; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000053240};
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..203
FT                   /note="Ribosomal RNA methyltransferase FtsJ"
FT                   /evidence="ECO:0000259|Pfam:PF01728"
FT   ACT_SITE        160
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         53
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         79
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT   BINDING         120
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
SQ   SEQUENCE   289 AA;  32172 MW;  8A97AE329C6727A9 CRC64;
     MGKTSKDKRD IYYRLAKEEG WRARSAFKLL QINEEYNIFN GVLRAVDLCA APGSWSQVLT
     KKLKENASNV DDVKIVAVDL QAMAALPGVK QIQGDITKVS TAHEIIKEFE GSQADLVVCD
     GAPDVTGLHD IDEYVQSQLL LAALNITTHV LKNGGVFVAK IFRGKDVTLL YSQLKQFFEL
     VTVSKPRSSR NSSIEAFVIC QNYAPPAGFI PTMINPLLDH KYCDFNQLTG PNRFIVPFNV
     CGDLSAYDSD TSYSLLLEGQ SKYEYKDPVQ GPINPPYKDI LEKTKNIQI
//
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