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Database: UniProt
Entry: A0A085EMA0_9FLAO
LinkDB: A0A085EMA0_9FLAO
Original site: A0A085EMA0_9FLAO 
ID   A0A085EMA0_9FLAO        Unreviewed;       470 AA.
AC   A0A085EMA0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:KFC60345.1};
GN   ORFNames=FEM08_08220 {ECO:0000313|EMBL:KFC60345.1};
OS   Flavobacterium gilvum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC60345.1, ECO:0000313|Proteomes:UP000028636};
RN   [1] {ECO:0000313|EMBL:KFC60345.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1308 {ECO:0000313|EMBL:KFC60345.1};
RA   Shin S.-K., Yi H.;
RT   "Genome Sequence of Flavobacterium sp. EM1308.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KFC60345.1}.
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DR   EMBL; JNCP01000020; KFC60345.1; -; Genomic_DNA.
DR   RefSeq; WP_035634746.1; NZ_JNCP01000020.1.
DR   AlphaFoldDB; A0A085EMA0; -.
DR   STRING; 1492737.EM308_09905; -.
DR   KEGG; fgl:EM308_09905; -.
DR   PATRIC; fig|1492737.3.peg.813; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000028636; 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; 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};
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          3..64
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        428
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        428
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         302
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         331
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         352
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         401
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   470 AA;  53985 MW;  C49320BD171D4B74 CRC64;
     MARKNTDKVV FHQIKVLDAG AKGVSVAKAP DGKVIFIPNV VPGDVVDVQT FKKRKAYYEG
     KAVHFHQLSE HRVDPICEHF GVCGGCKWQN MNYDQQLFFK HNEVKNHLQR IGKIELPEFE
     PILGSEKKFF YRNKMEFSFS NSRWLTEAEI GSEENLGNRN ALGFHIPKMW DKILDINKCH
     LQEDPSNAIR NEVRAFANQN SLTFFNPRAH EGLLRTLMLR TASTGEIMVL IQFFEDDKAN
     RELLLDHLYE KFPQITSLQY VVNNKANDTL YDTDIKLYKG RDYILEEMEG LKFSINAKSF
     YQTNSEQAYE LYKITRDFAG LTGNEIVYDL YTGTGTIAQF VSKKAKKVIG VESVPDAIKD
     AKANAERNNI DNCEFFVGDM KVVFNDSFIA QHGHPEVIIT DPPRDGMHKD VIEQIMKIAP
     EKVVYVSCNS ATQARDLALM DEKYKVTRVR PVDMFPQTHH VENVVLLERR
//
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