ID A0A1F6M925_9BACT Unreviewed; 403 AA.
AC A0A1F6M925;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:OGH68126.1};
GN ORFNames=A3C15_03395 {ECO:0000313|EMBL:OGH68126.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_02_FULL_50_9b.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798682 {ECO:0000313|EMBL:OGH68126.1, ECO:0000313|Proteomes:UP000176532};
RN [1] {ECO:0000313|EMBL:OGH68126.1, ECO:0000313|Proteomes:UP000176532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA M5U methyltransferase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01024}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGH68126.1}.
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DR EMBL; MFQD01000010; OGH68126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6M925; -.
DR Proteomes; UP000176532; Unassembled WGS sequence.
DR GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IEA:GOC.
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; IPR030391; MeTrfase_TrmA_CS.
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; PS01231; TRMA_2; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU01024};
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 360
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 234
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 281
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 333
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 403 AA; 45688 MW; ECBF01CE1DB4C8F1 CRC64;
MKKTKREKLS AIDELSIGLS KIKARCRYFG ECGGCLMQHI AYPDQLELKR QLVNRAFEKN
GLAARLDIAS ITPSPQQWFY RNRMDYPVGE NGEIGLKPFG KWRDVLDLKE CFILSKETPE
ILQLVRDWMT AHNLAGWNNV RYTGFVRYVV IREGKQTGER MVMVVTSGAE HDPAIWPELV
RRLKSSCTTL YWGVNPTITD ISIPQDLRLL HGAQFLTEKI NDYTYKIFPS SFFQTNSDGA
ALLQQRVAAH VHGARVLDLY CGMGFFSIDL AARGKKVFGV ELDVAAIELA RENARVNNVA
AEFAAASMEE WVTGDGGGPE IIKKFKPDSV VIDPPRMGLH PRVVEWLCAN PTPELLYVSC
NFEQLAREMV ELQKVYQLTA LEAVDMFPHT PHIELIARFI HKQ
//