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Database: UniProt
Entry: V7I5Z9_9CLOT
LinkDB: V7I5Z9_9CLOT
Original site: V7I5Z9_9CLOT 
ID   V7I5Z9_9CLOT            Unreviewed;       449 AA.
AC   V7I5Z9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:ETA80726.1};
GN   ORFNames=T472_0210330 {ECO:0000313|EMBL:ETA80726.1};
OS   Youngiibacter fragilis 232.1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Youngiibacter.
OX   NCBI_TaxID=994573 {ECO:0000313|EMBL:ETA80726.1, ECO:0000313|Proteomes:UP000017747};
RN   [1] {ECO:0000313|EMBL:ETA80726.1, ECO:0000313|Proteomes:UP000017747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232.1 {ECO:0000313|EMBL:ETA80726.1,
RC   ECO:0000313|Proteomes:UP000017747};
RX   PubMed=24459265;
RA   Wawrik C.B., Callaghan A.V., Stamps B.W., Wawrik B.;
RT   "Genome Sequence of Youngiibacter fragilis, the Type Strain of the Genus
RT   Youngiibacter.";
RL   Genome Announc. 2:e01183-13(2014).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01024}.
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:ETA80726.1}.
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DR   EMBL; AXUN02000175; ETA80726.1; -; Genomic_DNA.
DR   RefSeq; WP_023387147.1; NZ_AXUN02000175.1.
DR   AlphaFoldDB; V7I5Z9; -.
DR   STRING; 994573.T472_0210330; -.
DR   PATRIC; fig|994573.3.peg.1924; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000017747; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
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; IPR030391; MeTrfase_TrmA_CS.
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.
DR   PROSITE; PS01231; TRMA_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000017747};
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..58
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        405
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        405
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         309
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         378
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   449 AA;  49852 MW;  1D3922334B91830F CRC64;
     MKKNDIIKAD ITGQGYNGEG IARIEGMPVF IENALPGEKA SIHILKVNKN LAFGKIASID
     VPSKLRVEPP CPYYWKCGGC DLQHQTYESQ LEFKKKRVRD AIERIGGVKD PVVNDTLGME
     NPFRYRNKVQ LPVGLENGKI VSGFYAKRSH RIIDMESCII QHEDGDKVLK IVREWMEDKG
     ILPYQADGTG LIRHIMVRKG FTTGDLMVVI VATKAELPNN EDLTRRLSSI DGFKSLILNI
     NDRDTNVILG ESNIVLYGTD HIEDYISEFK FRISPHSFFQ VNPAQTQVMY SKALEYAGLT
     GNEIVFDAYC GAGTISMFLS KKARKVYGVE IVREAVADAW LNAEMNGVTN IEFIEGKSED
     VISDLIGQGI HADVVVVDPP RKGCERSLLE SIAAMGPKRL VYVSCDAATL GRDIGILAEL
     GYELVEATPV DNFPQTAHVE TVALITRNI
//
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