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Database: UniProt
Entry: D9RY73_THEOJ
LinkDB: D9RY73_THEOJ
Original site: D9RY73_THEOJ 
ID   D9RY73_THEOJ            Unreviewed;       450 AA.
AC   D9RY73;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:ADL08297.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ADL08297.1};
GN   OrderedLocusNames=Toce_1553 {ECO:0000313|EMBL:ADL08297.1};
OS   Thermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 /
OS   JW/IW-1228P).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Thermosediminibacteraceae; Thermosediminibacter.
OX   NCBI_TaxID=555079 {ECO:0000313|EMBL:ADL08297.1, ECO:0000313|Proteomes:UP000000272};
RN   [1] {ECO:0000313|EMBL:ADL08297.1, ECO:0000313|Proteomes:UP000000272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1034 / DSM 16646 / JW/IW-1228P
RC   {ECO:0000313|Proteomes:UP000000272};
RX   PubMed=21304740;
RA   Pitluck S., Yasawong M., Munk C., Nolan M., Lapidus A., Lucas S.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Bruce D., Detter C., Tapia R.,
RA   Han C., Goodwin L., Liolios K., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Spring S., Sikorski J., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Thermosediminibacter oceani type strain
RT   (JW/IW-1228P).";
RL   Stand. Genomic Sci. 3:108-116(2010).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
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DR   EMBL; CP002131; ADL08297.1; -; Genomic_DNA.
DR   RefSeq; WP_013276325.1; NC_014377.1.
DR   AlphaFoldDB; D9RY73; -.
DR   STRING; 555079.Toce_1553; -.
DR   KEGG; toc:Toce_1553; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_7_0_9; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000000272; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 2.40.50.1070; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR030390; MeTrfase_TrmA_AS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-METHYLTRANSFERASE; 1.
DR   Pfam; PF01938; TRAM; 1.
DR   Pfam; PF05958; tRNA_U5-meth_tr; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR   PROSITE; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000000272};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}.
FT   DOMAIN          1..59
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        407
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        407
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         311
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         332
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         380
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   450 AA;  50699 MW;  291424BD371C89A6 CRC64;
     MLKKRDRIAI DITAMAHEGQ GVGRVDGLAV FVEGALKGER VLAVVEKVSK NYAIARAEEI
     ISPSPDRIIP RCPHADECGG CSLQHLSYKG QLEFKTQKVR DSLERIGRIY TTVFDTIGME
     DPWKYRNKAQ YPVGKKDYRP ALGFYMKRSH DLVPIEGCLI QHELSWRAAE VVRDWMEKFR
     VSIYDEINHK GLIRHVVTRI GAKTGEVMVV LVINGREVPH LRELLGALEK NVEGLKSVYL
     NVNTKKTNVI MGDENILVYG EPHIIDFIGE IKFTLSPNSF FQVNPVQVEV LYKKVMEYAG
     LTGEETVIDA YCGIGTITLF LAGKARMVYG IEVVPQAVMD ARNNALLNGI ENVEFIEGAA
     EEVMPQLVER GIRADVIVMD PPRRGCDEKL LDAAVKMNPP RMVYVSCNPA TLARDLRYLE
     DRGYRTELVQ PVDMFPFTHH VECVALIKKT
//
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