ID A0A2C9CP04_9RHOB Unreviewed; 404 AA.
AC A0A2C9CP04;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=23S rRNA (Uracil1939-C5)-methyltransferase {ECO:0000313|EMBL:SOH92962.1};
GN ORFNames=SAMN06273572_101813 {ECO:0000313|EMBL:SOH92962.1};
OS Monaibacterium marinum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Monaibacterium.
OX NCBI_TaxID=1690039 {ECO:0000313|EMBL:SOH92962.1, ECO:0000313|Proteomes:UP000220034};
RN [1] {ECO:0000313|EMBL:SOH92962.1, ECO:0000313|Proteomes:UP000220034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 {ECO:0000313|EMBL:SOH92962.1,
RC ECO:0000313|Proteomes:UP000220034};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OCTN01000001; SOH92962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9CP04; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000220034; 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; 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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51687; SAM_MT_RNA_M5U; 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 362
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 240
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 267
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 287
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 336
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 404 AA; 43490 MW; 4EA8B1258160A23B CRC64;
MEQITIDRLG HQGDGVVQGG GERFVPYTLP GEVVEVNAKG DLQNVVTASP HRVDPLCKHF
GTCGGCAVQH GADAFVAEWK VDVVRRALSA RSIEMKFGGL ATSPAGTRRR AVFGGRRTRK
GVSVGFHQRG SNQLVEIEEC TVVDPKVLAA MPALEELTAI GASRNSTIRL SVTLSVAGLD
VFVDEAHELE RPMLPQLAEI ATRHNLARLT WNDEVIVSAN APIQRMGRAR VVPPPGAFLQ
ATPHGQAALL ATVKQAVGKA SRIVDLFAGC GTFALPLAEN AEIHAVENDG PMLSALETAW
RRTEGALHRI TTENRDLFRR PMLSSELKGY DAVVIDPPRA GAASQIAELA QSAIKTIVFV
SCNPVTFARD AEVLTNAGYT MGSVRVIDQF RWSPHIELTA TFTK
//
