ID A0A1M6NXD0_9BACL Unreviewed; 465 AA.
AC A0A1M6NXD0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=23S rRNA m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SHK00322.1};
GN ORFNames=SAMN05443507_10714 {ECO:0000313|EMBL:SHK00322.1};
OS Alicyclobacillus montanus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1830138 {ECO:0000313|EMBL:SHK00322.1, ECO:0000313|Proteomes:UP000184016};
RN [1] {ECO:0000313|Proteomes:UP000184016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA-503 {ECO:0000313|Proteomes:UP000184016};
RA Varghese N., Submissions S.;
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; FRAF01000007; SHK00322.1; -; Genomic_DNA.
DR RefSeq; WP_072873491.1; NZ_FRAF01000007.1.
DR AlphaFoldDB; A0A1M6NXD0; -.
DR STRING; 1830138.SAMN05443507_10714; -.
DR Proteomes; UP000184016; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184016};
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 7..65
FT /note="TRAM"
FT /evidence="ECO:0000259|PROSITE:PS50926"
FT ACT_SITE 418
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 418
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 293
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 322
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 343
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 391
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 465 AA; 52497 MW; CA22B32F3FE024DC CRC64;
MPKSELLSCV GQQVTLSPIR INDDGEGVAT LEGVTIFVPH LLPGEVANVR VQSAGRSFLR
GEMIERLGTE SKDRVHPPCS VFGQCGGCQL QHLSYRGQLL HKQKVVEHHL RRSLRGLPAI
ENLQVQPTIA SPSPYGYRNH VQIPVRYDGQ KDKLLFGFYA PSSHELVPTE DCWLISPRLM
LLWQAVRKGM ETWPRELKAA IHHLHLREAV ATGQQMIIWA VQAEYEKVVE HIQKFYQNLE
SSLRKLLTVG INRTSHETDR PNSRRADILA GSSWIEEELL GVRFRLSAES FFQVNSAQAE
QLYRHVIDRL QKHSATRLLD AYSGTGTLSL LLSPYAKTVV GVESVRASVE NARQNAEINH
IFNVQFIEDT VEHWLPRQIS DNDSFDTILV DPPRKGLHSE VISAILKANP QTFLYVSCNP
VTLARDLRPF AENGYQITSV QPFDMFPQTS HVECVVTLVR KVVTT
//
