ID A0A208XIR7_9BURK Unreviewed; 252 AA.
AC A0A208XIR7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=tRNA (cytidine/uridine-2'-O-)-methyltransferase TrmJ {ECO:0000256|RuleBase:RU362024};
DE EC=2.1.1.200 {ECO:0000256|RuleBase:RU362024};
DE AltName: Full=tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase {ECO:0000256|RuleBase:RU362024};
DE AltName: Full=tRNA Cm32/Um32 methyltransferase {ECO:0000256|RuleBase:RU362024};
GN Name=trmJ {ECO:0000256|RuleBase:RU362024};
GN ORFNames=CDO44_22230 {ECO:0000313|EMBL:OVZ55874.1};
OS Pigmentiphaga sp. NML080357.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pigmentiphaga.
OX NCBI_TaxID=2008675 {ECO:0000313|EMBL:OVZ55874.1, ECO:0000313|Proteomes:UP000196551};
RN [1] {ECO:0000313|EMBL:OVZ55874.1, ECO:0000313|Proteomes:UP000196551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML080357 {ECO:0000313|EMBL:OVZ55874.1,
RC ECO:0000313|Proteomes:UP000196551};
RA Bernier A.-M., Bernard K.;
RT "Pigmentiphaga species Genome sequencing and assembly.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or
CC 2'O-methylated uridine (Um32) at position 32 in tRNA.
CC {ECO:0000256|RuleBase:RU362024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(32) in tRNA = 2'-O-
CC methyluridine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42936, Rhea:RHEA-COMP:10107, Rhea:RHEA-COMP:10290,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74478; EC=2.1.1.200;
CC Evidence={ECO:0000256|RuleBase:RU362024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-
CC methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42932, Rhea:RHEA-COMP:10288, Rhea:RHEA-COMP:10289,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74495, ChEBI:CHEBI:82748; EC=2.1.1.200;
CC Evidence={ECO:0000256|RuleBase:RU362024};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362024}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362024}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase TrmH family.
CC {ECO:0000256|ARBA:ARBA00007228}.
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:OVZ55874.1}.
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DR EMBL; NINW01000048; OVZ55874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A208XIR7; -.
DR OrthoDB; 9806346at2; -.
DR Proteomes; UP000196551; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd18093; SpoU-like_TrmJ; 1.
DR Gene3D; 1.10.8.590; -; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR004384; RNA_MeTrfase_TrmJ/LasT.
DR InterPro; IPR001537; SpoU_MeTrfase.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR NCBIfam; TIGR00050; rRNA_methyl_1; 1.
DR PANTHER; PTHR42786:SF2; TRNA (CYTIDINE_URIDINE-2'-O-)-METHYLTRANSFERASE TRMJ; 1.
DR PANTHER; PTHR42786; TRNA/RRNA METHYLTRANSFERASE; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR PIRSF; PIRSF004808; LasT; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU362024};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU362024};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OVZ55874.1};
KW tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT DOMAIN 6..160
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
SQ SEQUENCE 252 AA; 26660 MW; D47673A449DE9519 CRC64;
MLSLVSFVMV EPSHPGNVGS AARALKTMGF SRLVLVNPRV ADAANHPEAL ALASGATDVL
AAARVCATLE EALAPVTMAF AMTARLRDLG PPACDMRQAA ELVRDHLAGH AGAQAAVVLG
TERSGLTNEQ VALCHRICHI PANPEYSSLN VAQALQLAAY ELRYALLGAE QLAVAGPRAE
PASGEAVEAL LAHWEEALIA VGYLDPRHPK KLMPRMRHLF ARAGLSREET DLLRGVCTAM
IAQSRKISHG SS
//
