ID A0A061QDM1_9PROT Unreviewed; 417 AA.
AC A0A061QDM1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Putative RNA methyltransferase {ECO:0000313|EMBL:GAK33646.1};
GN Name=BMEI1496 {ECO:0000313|EMBL:GAK33646.1};
GN ORFNames=AQ1_01536 {ECO:0000313|EMBL:GAK33646.1};
OS alpha proteobacterium Q-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK33646.1, ECO:0000313|Proteomes:UP000027360};
RN [1] {ECO:0000313|EMBL:GAK33646.1, ECO:0000313|Proteomes:UP000027360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q-1 {ECO:0000313|EMBL:GAK33646.1,
RC ECO:0000313|Proteomes:UP000027360};
RX PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT "Iodide oxidation by a novel multicopper oxidase from the
RT alphaproteobacterium strain Q-1.";
RL Appl. Environ. Microbiol. 78:3941-3949(2012).
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:GAK33646.1}.
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DR EMBL; BAYV01000015; GAK33646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061QDM1; -.
DR STRING; 1492281.AQ1_01536; -.
DR Proteomes; UP000027360; 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; 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; IPR012340; NA-bd_OB-fold.
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; 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; 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:UP000027360};
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 374
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 374
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 253
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 280
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 300
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 348
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 417 AA; 44695 MW; 407873C3088A3A64 CRC64;
MRLRIERIGA QGDGIAQTGD GPIFVPFTLA GDEIDAWLEP GPRGTIRAQM EGLITPGPGR
QDAPCRHHGQ CGGCSLQHLD ADLYARWVAD RVQMAMAQHG LGDCPMAPPQ ISPPSSRRRL
SLKAMRTSRG VLLGFAMRQS HHLVDVRQCP VARPSLVALF KPLRALLHDL MPLRAASVIS
LTEADNGIDM VIDGGIAPGL SMREALAAFA QSRDIASLHV MEDGLCDPVA VNRRVEMVFD
GIPVPLPPGG FIQATAEGEA ALRALMLEWL EGAQNCVDLF AGIGTFSFPL ARRARVLAVE
GARTALDALQ SGVNKASHLK GLTALHRDLF RRPLSAAELA PFDGLIIDPP RAGAVAQMGE
IAKSGVRTVV AFSCNPNSFA RDARILVDGG YQLCQISPVD QFLWSPHVEL AALFTKS
//
