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Database: UniProt
Entry: A0A1G5GUJ6_9FIRM
LinkDB: A0A1G5GUJ6_9FIRM
Original site: A0A1G5GUJ6_9FIRM 
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}.
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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
//
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