ID A5P7X1_9SPHN Unreviewed; 397 AA.
AC A5P7X1;
DT 10-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 10-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Putative RNA methyltransferase {ECO:0000313|EMBL:EDL50422.1};
GN ORFNames=ED21_28163 {ECO:0000313|EMBL:EDL50422.1};
OS Erythrobacter sp. SD-21.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=161528 {ECO:0000313|EMBL:EDL50422.1, ECO:0000313|Proteomes:UP000005498};
RN [1] {ECO:0000313|EMBL:EDL50422.1, ECO:0000313|Proteomes:UP000005498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD-21 {ECO:0000313|EMBL:EDL50422.1,
RC ECO:0000313|Proteomes:UP000005498};
RA Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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}.
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:EDL50422.1}.
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DR EMBL; ABCG01000001; EDL50422.1; -; Genomic_DNA.
DR RefSeq; WP_006832244.1; NZ_ABCG01000001.1.
DR AlphaFoldDB; A5P7X1; -.
DR STRING; 161528.ED21_28163; -.
DR eggNOG; COG2265; Bacteria.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000005498; 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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR030390; MeTrfase_TrmA_AS.
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}; Reference proteome {ECO:0000313|Proteomes:UP000005498};
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 355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 236
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 283
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 329
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 397 AA; 42978 MW; 9454694E3B4C1919 CRC64;
MSEETILRIA AKGDGVTENG RHVSGAVTGD TVREDETILP GPHHVEPPCR HFGTCGGCQL
QQADEAALRQ FVTERVAFAA EAQELNVGEV LLTHLSPPCT RRRATLHALK AGKSAVIGFR
EARSTRVVDM RECHILAPEL FALVSPLRNL IAKHSGRRPI DISLTLADQG VDCQLKGFTA
EGLAATEALL DFARDHGLAR LALDQGYGAE TVWEPEPVTI TLGSIPVGLP QNSFRQPTRD
GEQVLVSDTA EFVGDARTVA DLFAGLGTFA FALSDPAKVL AVEAARDAHL ACKTAANMRG
VPVHAMHRDL FRNPLTAEEV SRFGAIVLDP PRAGAREQVA QIAQSTASRV VYVSCNPSSW
ARDVKTLVDA GFRLEKLRPV GQFRWSTHVE LTSYFTR
//
