ID   A0A1G5KE41_9BACL        Unreviewed;       576 AA.
AC   A0A1G5KE41;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase {ECO:0000313|EMBL:SCY98511.1};
GN   ORFNames=SAMN05720606_114122 {ECO:0000313|EMBL:SCY98511.1};
OS   Paenibacillus polysaccharolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=582692 {ECO:0000313|EMBL:SCY98511.1, ECO:0000313|Proteomes:UP000198538};
RN   [1] {ECO:0000313|EMBL:SCY98511.1, ECO:0000313|Proteomes:UP000198538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BL9 {ECO:0000313|EMBL:SCY98511.1,
RC   ECO:0000313|Proteomes:UP000198538};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FMVM01000014; SCY98511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5KE41; -.
DR   STRING; 582692.SAMN05720606_114122; -.
DR   Proteomes; UP000198538; 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; PF01938; TRAM; 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          75..133
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        531
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        531
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         406
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         435
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         456
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         504
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   576 AA;  64008 MW;  AE0B3133FE785A2F CRC64;
     MSNTNRSGRG KNRRNSAAPQ GKGNASASRQ PSQSMQSTRP STSHSGKEVR PRSASISGVR
     SKGRTRESAP IEGLPVSKNE ETVIEIIGMN HDGEGVGRAD GYTLFVQGAL PGETVRVRVM
     KTKKQYGYAK LLEIVKASPD RVSAPCPIYD QCGGCQIQHM SYAGQLAWKR QLVIDNLQRI
     GKLNVMVEDE TQANHSEQSP FDEQIEEQTV QTNESNRIRL RLEGVMSEED TEHAIRVLPT
     MGMDEPWRYR NKAQVPIGVT EGGLVGGFYA KGSHRIIDME TCLIQHEHND EVVAKVKEIG
     SHLGISAYNE ETGRGLLRHV VVKKAFRTGE MMLVLVTNGR DIQHKDEWIG SIREAIPQVA
     SICQNVNKKQ TNVIFGDETR VLWGRDVIYD FIGDVQFAIS PRSFYQVNPV QTEVLYGKTV
     EYAGLSGKET VIDAYCGIGT ISLFLAQHAD QVYGVEIVPE AIEDARSNAM LNEMKNVKFE
     VGASEDVIPR WKEQGIEADV IVVDPPRKGC DPRLLDTILE MKPERVVYVS CNPSTLARDL
     RVLEDGGYHT VEVTPVDMFP HTVHVESVAM LVRIKE
//