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Database: UniProt
Entry: Y0KIB3_9PROT
LinkDB: Y0KIB3_9PROT
Original site: Y0KIB3_9PROT 
ID   Y0KIB3_9PROT            Unreviewed;       251 AA.
AC   Y0KIB3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=Meth11DRAFT_1872 {ECO:0000313|EMBL:EUJ11038.1};
OS   Methylophilaceae bacterium 11.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae.
OX   NCBI_TaxID=1101195 {ECO:0000313|EMBL:EUJ11038.1, ECO:0000313|Proteomes:UP000022668};
RN   [1] {ECO:0000313|EMBL:EUJ11038.1, ECO:0000313|Proteomes:UP000022668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11 {ECO:0000313|EMBL:EUJ11038.1,
RC   ECO:0000313|Proteomes:UP000022668};
RG   DOE Joint Genome Institute;
RA   Chistoserdova L., Huntemann M., Han J., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Palaniappan K., Ivanova N., Schaumberg A.,
RA   Pati A., Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-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:EUJ11038.1}.
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DR   EMBL; JCKJ01000001; EUJ11038.1; -; Genomic_DNA.
DR   AlphaFoldDB; Y0KIB3; -.
DR   STRING; 1101195.Meth11DRAFT_1872; -.
DR   PATRIC; fig|1101195.3.peg.1833; -.
DR   eggNOG; COG0565; Bacteria.
DR   Proteomes; UP000022668; 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:UP000022668};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EUJ11038.1};
KW   tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT   DOMAIN          14..163
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
SQ   SEQUENCE   251 AA;  28266 MW;  91EA4FFF8899A425 CRC64;
     MTEDLLTDRI FNHIRIVLCQ TSHPGNIGST ARAMKTMGLS RLYLVRPKHF PDSEANALAV
     NAADLLDTAV VTQTLEEAIA DCQFVIGVSG KQRSLSQQVV TVREAAAEVK DIAAHQEVAL
     VFGTEMSGLS NEEADRCHML ATIPANPEYT SLNLAQAVQI MCYELRMAIT TGDLHYQEKT
     AELATQDDLE RFYEHMREVL EHIGYINPRA PKKLFERLRR LYGRTRLEKE EVNLLRGILT
     LSVTPKKHTK Y
//
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