ID A0A1H9TXP6_9MICO Unreviewed; 384 AA.
AC A0A1H9TXP6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=23S rRNA m(5)U-747 methyltransferase {ECO:0000313|EMBL:SES02015.1};
GN ORFNames=SAMN05216199_1815 {ECO:0000313|EMBL:SES02015.1};
OS Pedococcus cremeus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Pedococcus.
OX NCBI_TaxID=587636 {ECO:0000313|EMBL:SES02015.1, ECO:0000313|Proteomes:UP000199019};
RN [1] {ECO:0000313|Proteomes:UP000199019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6963 {ECO:0000313|Proteomes:UP000199019};
RA Varghese N., Submissions S.;
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; FOHB01000002; SES02015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9TXP6; -.
DR STRING; 587636.SAMN05216199_1815; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000199019; 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 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:UP000199019};
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 ACT_SITE 343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 343
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 212
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 241
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 265
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 316
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 384 AA; 42089 MW; A32C29244860E7AE CRC64;
MQCDYFDAGR CRSCALMGVP YAAQLADKDA AVRTLLADAA PADVWLEPFT GPESAFRNKA
KLVVGGRRGE PTLGILDPTG AGVDLRHCGL YEPGLHEAVL RLPDLVGRLG LTPYDVPRRT
GELKHVLVTH SPDGELMVRF VLRSPGQLGR LERSLPDLLA RLPGTRVVTA NFLPQHAALL
EGEQEQVLTE HATLPMRVNG ITLHLRPQSF FQTNTTVAAG LYRQAQEWLA EVAPTSLWDL
YCGVGGFALH ALTTATPPAQ VTGIEVSEEA VASAEHTLGE IPLQDNGTHA TFRADDATRY
AVQRPPEQAP DAVVVNPPRR GFGRELAAWL DHSRVQHVVY SSCNARSLAV DLEAMPHLQV
RRARLFDMFP QTSHHEVMVL LERR
//
