ID A0A0V1FYJ7_TRIPS Unreviewed; 333 AA.
AC A0A0V1FYJ7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-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 Name=FTSJ1 {ECO:0000313|EMBL:KRY90924.1};
GN ORFNames=T4A_10217 {ECO:0000313|EMBL:KRY71729.1}, T4B_235
GN {ECO:0000313|EMBL:KRZ27961.1}, T4C_4517 {ECO:0000313|EMBL:KRZ42385.1},
GN T4D_5118 {ECO:0000313|EMBL:KRY90924.1}, T4E_1266
GN {ECO:0000313|EMBL:KRX94191.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRY90924.1, ECO:0000313|Proteomes:UP000054995};
RN [1] {ECO:0000313|Proteomes:UP000054632, ECO:0000313|Proteomes:UP000054805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS13 {ECO:0000313|EMBL:KRY71729.1}, ISS141
RC {ECO:0000313|EMBL:KRX94191.1}, ISS176 {ECO:0000313|EMBL:KRZ42385.1},
RC ISS470 {ECO:0000313|EMBL:KRY90924.1}, and ISS588
RC {ECO:0000313|EMBL:KRZ27961.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRY90924.1}.
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DR EMBL; JYDU01000076; KRX94191.1; -; Genomic_DNA.
DR EMBL; JYDR01000054; KRY71729.1; -; Genomic_DNA.
DR EMBL; JYDT01000017; KRY90924.1; -; Genomic_DNA.
DR EMBL; JYDS01000064; KRZ27961.1; -; Genomic_DNA.
DR EMBL; JYDV01000014; KRZ42385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1FYJ7; -.
DR STRING; 6337.A0A0V1FYJ7; -.
DR Proteomes; UP000054632; Unassembled WGS sequence.
DR Proteomes; UP000054805; Unassembled WGS sequence.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR Proteomes; UP000054826; Unassembled WGS sequence.
DR Proteomes; UP000054995; 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}; Reference proteome {ECO:0000313|Proteomes:UP000054815};
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..201
FT /note="Ribosomal RNA methyltransferase FtsJ"
FT /evidence="ECO:0000259|Pfam:PF01728"
FT REGION 272..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
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 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03162"
SQ SEQUENCE 333 AA; 36807 MW; 5697B32838529058 CRC64;
MGKCSKDKRD VFYRLSKEEE YRARSSFKLK QINEEFGILK GVRRAVDLCA APGSWSQVIR
EEINKSSYKD SSVVIAVDIQ EMAPLEGVMM LQADITEKET AAKIKRLLPF GSADIVVCDG
APDVTGIHDL DEFLQGQLLV SALNIATMVL KNGGTFVSKI FRAKHPDLLI TQLKIFFNKV
EYVKPRSSRG SSYESFVVCQ GLTLPLGYQP TTVNLMLEPN YDLAVSKLKG VNRQIVPFVS
CGDLSGWDSD MSFSLRTIND ISTMRKKSLA LRHTSERQSS GKDKMKVAGT SGKTTKNTKR
NSGASNTELE GENENLTLDD AIELITACIL SDV
//
