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Database: UniProt
Entry: D7DW47_NOSA0
LinkDB: D7DW47_NOSA0
Original site: D7DW47_NOSA0 
ID   D7DW47_NOSA0            Unreviewed;       245 AA.
AC   D7DW47;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
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   OrderedLocusNames=Aazo_4224 {ECO:0000313|EMBL:ADI65618.1};
OS   Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI65618.1, ECO:0000313|Proteomes:UP000001511};
RN   [1] {ECO:0000313|EMBL:ADI65618.1, ECO:0000313|Proteomes:UP000001511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0708 {ECO:0000313|EMBL:ADI65618.1,
RC   ECO:0000313|Proteomes:UP000001511};
RX   PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA   Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA   Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT   "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT   multicellular cyanobacterium.";
RL   PLoS ONE 5:E11486-E11486(2010).
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}.
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DR   EMBL; CP002059; ADI65618.1; -; Genomic_DNA.
DR   RefSeq; WP_013192629.1; NC_014248.1.
DR   AlphaFoldDB; D7DW47; -.
DR   STRING; 551115.Aazo_4224; -.
DR   KEGG; naz:Aazo_4224; -.
DR   eggNOG; COG0565; Bacteria.
DR   HOGENOM; CLU_056931_3_0_3; -.
DR   OrthoDB; 9806346at2; -.
DR   Proteomes; UP000001511; Chromosome.
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|RuleBase:RU362024,
KW   ECO:0000313|EMBL:ADI65618.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW   S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU362024};
KW   Transferase {ECO:0000313|EMBL:ADI65618.1};
KW   tRNA processing {ECO:0000256|RuleBase:RU362024}.
FT   DOMAIN          6..155
FT                   /note="tRNA/rRNA methyltransferase SpoU type"
FT                   /evidence="ECO:0000259|Pfam:PF00588"
SQ   SEQUENCE   245 AA;  27520 MW;  5ED80B57676A62E8 CRC64;
     MGSAGIRIVL VEPAGPLNLG SIARVMKNFG LDNLVLVNPQ CDHLSFDALK MAVHAKEILE
     SAVIFPTLPE ALQGCVRVIA TIGRDYSGHI PLESPRTSLP WLLEETEKPV ALIFGREDRG
     LSNEELNYAH KLIFIPTNPQ YPSLNLATAV SICCYELSQY ELSQLAKIFT TPKPPTTEMA
     PVDMLEPYYQ ELESLLLFIG YLYPHTAASR MEKFRHLYNR AHIQTTEVAM LRGILRQIEW
     AIRNS
//
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