ID S3MW33_9GAMM Unreviewed; 279 AA.
AC S3MW33;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=F945_02341 {ECO:0000313|EMBL:EPF71995.1};
OS Acinetobacter rudis CIP 110305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=421052 {ECO:0000313|EMBL:EPF71995.1, ECO:0000313|Proteomes:UP000014568};
RN [1] {ECO:0000313|EMBL:EPF71995.1, ECO:0000313|Proteomes:UP000014568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 110305 {ECO:0000313|EMBL:EPF71995.1,
RC ECO:0000313|Proteomes:UP000014568};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter rudis CIP 110305.";
RL Submitted (JUN-2013) 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:EPF71995.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ATGI01000031; EPF71995.1; -; Genomic_DNA.
DR RefSeq; WP_016656745.1; NZ_KE340353.1.
DR AlphaFoldDB; S3MW33; -.
DR STRING; 632955.GCA_000829675_01626; -.
DR PATRIC; fig|421052.3.peg.2285; -.
DR eggNOG; COG0565; Bacteria.
DR HOGENOM; CLU_056931_0_1_6; -.
DR OrthoDB; 9806346at2; -.
DR Proteomes; UP000014568; 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 Reference proteome {ECO:0000313|Proteomes:UP000014568};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362024};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPF71995.1};
KW tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT DOMAIN 16..167
FT /note="tRNA/rRNA methyltransferase SpoU type"
FT /evidence="ECO:0000259|Pfam:PF00588"
SQ SEQUENCE 279 AA; 31434 MW; EF35B7C9B77A6DB2 CRC64;
MQNFDNAAVS TQLAHVRIVM VNTTLPANIG SALRAMKTMG LSKLVLVAPK TYPHPDIDAL
AAGATDLIEQ IEIVSSLEEA IADCHLVFGT SARSRTIPWP LLDVRPAANL AMQAISEKNQ
EVAIVFGRED RGLTNEELAL ANYHLTIPVN TDYGVLNVAQ AIQIVCYEMR MAILEHSTTA
SAQQEQAMPV TAEEQMQWDE PLVTQQQMQQ FYPHMQQMLA DIEFFDPENP RLLPLRLRRL
FGRIQLDRME YHLLRGVFTR VQALSNGTWK KSTHREDQN
//
