ID A0A1G7WV15_9FLAO Unreviewed; 471 AA.
AC A0A1G7WV15;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SDG75787.1};
GN ORFNames=SAMN04488027_106149 {ECO:0000313|EMBL:SDG75787.1};
OS Psychroflexus sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Psychroflexus.
OX NCBI_TaxID=470826 {ECO:0000313|EMBL:SDG75787.1, ECO:0000313|Proteomes:UP000199296};
RN [1] {ECO:0000313|EMBL:SDG75787.1, ECO:0000313|Proteomes:UP000199296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19803 {ECO:0000313|EMBL:SDG75787.1,
RC ECO:0000313|Proteomes:UP000199296};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNCW01000006; SDG75787.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7WV15; -.
DR STRING; 470826.SAMN04488027_106149; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000199296; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199296};
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 4..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 471 AA; 54242 MW; F5DCE56F3572D6FA CRC64;
MARRKNTKKT FENVEVLDAG SKGKGIGKAS DGRVLIIDQV VPGDVVDVTT YKKRKSYYQA
KPLRFVELSP KRTEPVCQHF GVCGGCKWQN MAYQHQLFYK EKEVLENLKR IGKIDIVETK
PILGSEEIYF YRNKMEFSFS NSRWLTESEI SSGIDIQDKN ALGFHIPGMW DKILNIEKCH
LQEDPSNDIR NKIRDFATEN ELDFFNPREQ TGLLRTLMIR TSSTGEFMIL IQFYQENKAK
RELLLDYIIQ EFPDVTSLQY VINEKGNDTI YDQEVINYFG RDFIYEEMEG LKFKINAKSF
YQTNSEQAYE LYKITREFAD LSGDELVYDL YTGTGTIAQF VAKKAKHVVG IEAIPEAIED
AKANAKLNGI ENTSFFAGDM KKIFTAGFIA EHGQPDVIIT DPPREGMHKE VVEQILNVRP
KRIVYVSCNS ATQARDLQLM DAHYQVEKSQ AVDMFPQTHH VENVVCLRLR E
//