ID Q07SR8_RHOP5 Unreviewed; 411 AA.
AC Q07SR8;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:ABJ05016.1};
DE EC=2.1.1.- {ECO:0000313|EMBL:ABJ05016.1};
GN OrderedLocusNames=RPE_1062 {ECO:0000313|EMBL:ABJ05016.1};
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ05016.1};
RN [1] {ECO:0000313|EMBL:ABJ05016.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ05016.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) 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; CP000463; ABJ05016.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07SR8; -.
DR STRING; 316055.RPE_1062; -.
DR KEGG; rpe:RPE_1062; -.
DR eggNOG; COG2265; Bacteria.
DR HOGENOM; CLU_014689_8_0_5; -.
DR OrthoDB; 9804590at2; -.
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};
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 369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 369
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 249
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 276
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 296
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT BINDING 343
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 411 AA; 44278 MW; E0E2E8765C91DC52 CRC64;
MTETLVIDHV GHRGDGVALR DGASIYVPFA LGGETVAVEP VAGHPDRRAL LSVEQPSAER
ITPFCKHFGV CGGCAIQHWR ADRYQAWKRE LVVEALSQAG IDCEVAPLID AHGQGRRRIT
LHARKGTHEV LKVGFAAAGS HDIVPIDRCP ILDPALDGAL DAAWALAEPL TTEAKPLDIQ
VTAADEGLDV DIRGSGPVSS RMLTTLSKLA EQHRLARLTR HGELVLMRTP PTIQVGAARL
TLPPGAFLQA TRAGEETLAD LVSERCGKAK NVVDLFCGVG PFALRLATKA RVAAYDSEAS
AIAALQKAAG TPGLKPMTIE IRDLFRRPLV PQQLEDVDAV VFDPPRQGAQ AQCQQLAKSR
VPLIVAVSCN AATFARDARL LLDGGYRIDQ LTPVDQFRHT PHVELVARFR K
//
