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Database: UniProt
Entry: A0A238XAG9_9FLAO
LinkDB: A0A238XAG9_9FLAO
Original site: A0A238XAG9_9FLAO 
ID   A0A238XAG9_9FLAO        Unreviewed;       470 AA.
AC   A0A238XAG9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SNR55608.1};
GN   ORFNames=SAMN04487979_11144 {ECO:0000313|EMBL:SNR55608.1};
OS   Flavobacterium sp. ov086.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1761785 {ECO:0000313|EMBL:SNR55608.1, ECO:0000313|Proteomes:UP000198291};
RN   [1] {ECO:0000313|EMBL:SNR55608.1, ECO:0000313|Proteomes:UP000198291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV086 {ECO:0000313|EMBL:SNR55608.1,
RC   ECO:0000313|Proteomes:UP000198291};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; FZNL01000011; SNR55608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238XAG9; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000198291; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
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:SF48; 23S RRNA (URACIL(747)-C(5))-METHYLTRANSFERASE RLMC; 1.
DR   PANTHER; PTHR11061; RNA M5U 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          1..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;  54186 MW;  2150196A786906BB CRC64;
     MGRKNTDKVV FHQIQVLDAG AKGVSVAKAP DGKVIFIPNV VPGDVVDVQT FKKRKAYYEG
     KAVKFHEFSE HRIEPICEHF GVCGGCKWQN MKYSQQLYYK QNEVKNHLQR IGKVELPEFE
     AILGSEKQFF YRNKMEFSFS NSRWLTEKEI ESTEDLGNRN ALGFHIPKMW DKILDIQKCH
     LQEDPSNAIR NEIRDFANEH NLAFFNPREQ SGLLRTFMIR TASTGEIMVL IQFFENDKKN
     RELILDHLYE KFPQITSLQY VVNAKQNDTI YDQNIKLYKG RDYILEEMEG LKFSINAKSF
     YQTNSDQAYE LYKITRDFAG LSGNETVYDL YTGTGTIAQF VSKKAKKVIG VESVPEAILD
     AKANAERNNI TNCEFFVGDM KVVFNESFIA QHGKPDVIIT DPPRDGMHKD VIDQILKIAP
     KKVVYVSCNS ATQARDLALM DEKYKVTRVR PVDMFPQTHH VENVVLLELR
//
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