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
//