ID A0A1M6YES1_9FLAO Unreviewed; 481 AA.
AC A0A1M6YES1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SHL16814.1};
GN ORFNames=SAMN05444484_101549 {ECO:0000313|EMBL:SHL16814.1};
OS Flavobacterium chilense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=946677 {ECO:0000313|EMBL:SHL16814.1, ECO:0000313|Proteomes:UP000184028};
RN [1] {ECO:0000313|EMBL:SHL16814.1, ECO:0000313|Proteomes:UP000184028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24724 {ECO:0000313|EMBL:SHL16814.1,
RC ECO:0000313|Proteomes:UP000184028};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRBT01000001; SHL16814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M6YES1; -.
DR STRING; 946677.SAMN05444484_101549; -.
DR Proteomes; UP000184028; 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 14..75
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 439
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 439
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 313
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 342
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 363
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 412
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 481 AA; 55218 MW; 8FC82D1E0F30045F CRC64;
MKKFTNPYFC AMGRKNTDKI VFHQIQVLDA GAKGVSVAKA PDGKVIFIPN VVPGDVVDVQ
TFKKRKAYYE GKAVKFHELS EHRIDPICDH FGVCGGCKWQ NMKYSQQLYY KQNEVKNHLQ
RIGKVELPEF ETILGSEKQF FYRNKMEFSF SNSRWLTEKE IGSTEDLGNR NALGFHIPKM
WDKILDINKC HLQEDPSNAI RNEIRAFAND HNLAFFNPRE HSGLLRTLMI RTASTGEIMV
LIQFFEDDKE NRELVLDHLY EKFPQITSLQ YVVNAKQNDT IYDQDIKLYK GRDYILEEME
GLKFSINAKS FYQTNSDQAY ELYKITRDFA GLSGNETVYD LYTGTGTIAQ FVSKKAKKVI
GVESVPEAIL DAKANAERNN ITNCEFFVGD MKVVFNESFI AQHGKPDVII TDPPRDGMHA
AVIDQILKIA PKKVVYVSCN SATQARDLAL MDEKYKVTRV RPVDMFPQTH HVENVVLLEL
R
//