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Database: UniProt
Entry: F7RNQ5_9GAMM
LinkDB: F7RNQ5_9GAMM
Original site: F7RNQ5_9GAMM 
ID   F7RNQ5_9GAMM            Unreviewed;       241 AA.
AC   F7RNQ5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=SOHN41_01996 {ECO:0000313|EMBL:EGM70103.1};
OS   Shewanella sp. HN-41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM70103.1, ECO:0000313|Proteomes:UP000002956};
RN   [1] {ECO:0000313|EMBL:EGM70103.1, ECO:0000313|Proteomes:UP000002956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HN-41 {ECO:0000313|EMBL:EGM70103.1,
RC   ECO:0000313|Proteomes:UP000002956};
RX   PubMed=21868804; DOI=10.1128/JB.05578-11;
RA   Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA   Hur H.G.;
RT   "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT   Arsenic-Sulfide Nanotubes.";
RL   J. Bacteriol. 193:5039-5040(2011).
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:EGM70103.1}.
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DR   EMBL; AFOZ01000023; EGM70103.1; -; Genomic_DNA.
DR   RefSeq; WP_007648193.1; NZ_AFOZ01000023.1.
DR   AlphaFoldDB; F7RNQ5; -.
DR   STRING; 327275.SOHN41_01996; -.
DR   OrthoDB; 9806346at2; -.
DR   Proteomes; UP000002956; 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:0001510; P:RNA methylation; IEA:GOC.
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:EGM70103.1};
KW   tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT   DOMAIN          5..154
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
SQ   SEQUENCE   241 AA;  26300 MW;  6694A2D5D4AF90BC CRC64;
     MLSNIRVVLV GTSHPGNIGS TARAMKTMGL STLYLAEPRV EPDGHSIALA AGASDILKHL
     VKVDSLAEAI ADCSLVIATS ARSRTLDWPM LDPREAGQKL VTESLSGPVA IVFGRENHGL
     SNEELQQCTY HVAIPANPEY SSLNLAQAVQ IICYETRVAH LAQTETIAES TEYPLAADQE
     RFFVHLESTL LSTGFIIKNH PGQVMTKLRR LFSRARIESQ EMNILRGILT SIDKVVGNKQ
     K
//
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