ID A0A1H9G906_9BACI Unreviewed; 458 AA.
AC A0A1H9G906;
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 m(5)U-1939 methyltransferase {ECO:0000313|EMBL:SEQ46582.1};
GN ORFNames=SAMN05216362_11460 {ECO:0000313|EMBL:SEQ46582.1};
OS Piscibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Piscibacillus.
OX NCBI_TaxID=571933 {ECO:0000313|EMBL:SEQ46582.1, ECO:0000313|Proteomes:UP000199427};
RN [1] {ECO:0000313|EMBL:SEQ46582.1, ECO:0000313|Proteomes:UP000199427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21633 {ECO:0000313|EMBL:SEQ46582.1,
RC ECO:0000313|Proteomes:UP000199427};
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; FOES01000014; SEQ46582.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9G906; -.
DR STRING; 571933.SAMN05216362_11460; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000199427; 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:UP000199427};
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 414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 414
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 289
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 318
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 339
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 387
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 458 AA; 51887 MW; 9C76DC05B21C251E CRC64;
MAKKIAPVKK NEYIDLEFVD LTHEGNGVGK IDGYPVFVPY GLPGEKAKVK IVKVKKNVAF
GKLIELIEPS ENRIEPPCDV FYQCGGCQIQ HMSYERQLKM KQKQVQDVMH KIAHMPDVPV
HPVIGMDEPW SYRNKVQIPV GERDGKVLTG FYQKRSHRII DMDTCPVQNE ANDHIVREMR
GIIEELGIEP YDEETHRGVI RHIVVRSGYH TGEIMVVLVT RTKKIPNQEA LIEKIKELNP
NIKGIIHNVN SKQTNVIMGR ESKTLWGEDV IIDKIGDLEF AISAHSFFQV NPEQTERLYE
QALKFANLTG NETVIDAYCG IGSISLFLAQ HAKKVYGVEV VPQAVDDAKD NAKRNHIDHA
EFFVGEAEKV MPWWRAQGLR PNVIVVDPPR KGCDEELLKA MIDMKPERIV YVSCNPSTLA
RDIKILADGG YSAKQIQPVD MFPQSNHIES VTELVLEN
//