ID A0A0P0DKV8_9CAUL Unreviewed; 414 AA.
AC A0A0P0DKV8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:ALJ08945.1};
GN ORFNames=JL11_11790 {ECO:0000313|EMBL:ALJ08945.1};
OS Brevundimonas sp. DS20.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Brevundimonas.
OX NCBI_TaxID=1532555 {ECO:0000313|EMBL:ALJ08945.1, ECO:0000313|Proteomes:UP000059212};
RN [1] {ECO:0000313|EMBL:ALJ08945.1, ECO:0000313|Proteomes:UP000059212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS20 {ECO:0000313|EMBL:ALJ08945.1,
RC ECO:0000313|Proteomes:UP000059212};
RA Scott D., Ely B.;
RT "Conservation of the essential genome among Caulobacter and Brevundimonas
RT species.";
RL Submitted (OCT-2015) 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; CP012897; ALJ08945.1; -; Genomic_DNA.
DR RefSeq; WP_054765825.1; NZ_CP012897.1.
DR AlphaFoldDB; A0A0P0DKV8; -.
DR STRING; 1532555.JL11_11790; -.
DR KEGG; brd:JL11_11790; -.
DR Proteomes; UP000059212; Chromosome.
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 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; 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};
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 REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 372
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 278
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 298
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 346
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 414 AA; 44008 MW; 4F5F32B73119E437 CRC64;
MQTFTISRVG GQGDGVAETP QGPVFAGLTL PGETVRGEVV DGRLEQVEIL TPSPDRIAPV
SPQYGDCGGC SLQHWADRPY LEWKREQVRL ALAREKIETE VEATVASPTG TRRRVALHAR
RTQDGRVVLG FKARRSWRLV EVRECPVADS RIIRAIPALT EVAAAFLEHP KSAPTLHVTW
TLSGLDVDVT GVERRSGGGL SADAQMRAIE AARRADLARL SLAGETLMMA RQPLIGFGPA
TVPLPAGGFL QAVPQAEAAM VERAVAAVKG AKKIADLFCG AGTFTFPLAT VAPVIAADAS
KAGIAALKAG AGSAKGMKAI TAEARDLFRR PLTPYDLKGC EAIVFDPPRA GAIDQTAQIA
GTKAAVVVGV SCNPQTFARD ARVLIDAGFR LERVTPVDQF LWSAHVELVS VFKR
//
