ID A0A1G5GUJ6_9FIRM Unreviewed; 465 AA.
AC A0A1G5GUJ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase {ECO:0000313|EMBL:SCY54840.1};
GN ORFNames=SAMN02910371_02732 {ECO:0000313|EMBL:SCY54840.1};
OS Butyrivibrio sp. INlla14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520808 {ECO:0000313|EMBL:SCY54840.1, ECO:0000313|Proteomes:UP000199551};
RN [1] {ECO:0000313|EMBL:SCY54840.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INlla14 {ECO:0000313|EMBL:SCY54840.1};
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; FMVS01000021; SCY54840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5GUJ6; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000199551; 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:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.40.50.1070; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 1.
DR PROSITE; PS01230; TRMA_1; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000199551};
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 REGION 15..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 422
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 326
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 347
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 395
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 465 AA; 52140 MW; 5D06080749EAF7FA CRC64;
MSYNERMRKF EKINQKMSGG KDKAKALGKA DDKAQDKAKA KKQIKSHDFQ YEETGAFGKK
PAGRNTVGRP GDRNTQKDME MAVDKKKSRC PYFKKCGACQ MIDTPYDKQL RQKHAHVAEL
LEPYTRVAAF VGMEEPEHYR CKVHAVFTHD KKGNPVSGIY REGTHDVVPI DSCLLEDQKA
DAIIASIRGM LKSFKIKTYD EDNGYGLLRH VLIRIGKKTG EIMVVLVTVS PIFPSKNNFV
KALLKEHPEI TTIVLNVNDK QTSMILGDKE KPMYGPGFIY DECCGMRFKI SPKSFYQVNP
IQQEVLYNKA IELADLKGTE VALDCYSGVG TIGIIASPHV KEVISVELNP DAVKDAKLNA
KINNVENITF YENDATRFMQ QMADSGDKVD LVFMDPPRAG STPEFISSMI ALNPEKVVYI
SCSPDSLARD LELITKDGYK VKKAVPVDMF PFTRSIETVV CLSKH
//