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Database: UniProt
Entry: B6IUE3_RHOCS
LinkDB: B6IUE3_RHOCS
Original site: B6IUE3_RHOCS 
ID   B6IUE3_RHOCS            Unreviewed;       449 AA.
AC   B6IUE3;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=RNA (Uracil-5-)-methyltransferase, putative {ECO:0000313|EMBL:ACJ00123.1};
GN   OrderedLocusNames=RC1_2750 {ECO:0000313|EMBL:ACJ00123.1};
OS   Rhodospirillum centenum (strain ATCC 51521 / SW).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=414684 {ECO:0000313|EMBL:ACJ00123.1, ECO:0000313|Proteomes:UP000001591};
RN   [1] {ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA   Touchman J.W., Bauer C., Blankenship R.E.;
RT   "Genome sequence of Rhodospirillum centenum.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACJ00123.1, ECO:0000313|Proteomes:UP000001591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX   PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA   Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA   Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA   Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT   "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT   proteobacterium Rhodospirillum centenum.";
RL   BMC Genomics 11:325-325(2010).
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; CP000613; ACJ00123.1; -; Genomic_DNA.
DR   RefSeq; WP_012567903.1; NC_011420.2.
DR   AlphaFoldDB; B6IUE3; -.
DR   STRING; 414684.RC1_2750; -.
DR   KEGG; rce:RC1_2750; -.
DR   eggNOG; COG2265; Bacteria.
DR   HOGENOM; CLU_014689_8_0_5; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000001591; 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; 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:UP000001591};
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..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        407
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        407
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         288
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         315
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         335
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   449 AA;  47544 MW;  819BB89F4BED0EA4 CRC64;
     MSPRRPPGRG RPGNRPERRS ESRPEPPVRG PVEIVVERVG ARGDGLAEWQ GHRLYVPQAL
     AGDRMMVTFG EPRADGWEAV PVTLLAEAPG RADPPCPHAG LCGGCALQHM DDATYAAWKT
     DLLASALERA GLAGPEVRLN PLVRTPPGSR RRAVLTAVRR GRRLWLGFNE RASHRLVDVE
     TCPVLAPALA ALLAPLRAVL ADILSDGQQI DVALTLLDDG PDLVLEGLPE PDLPRLEALS
     AFAGAQDLAR LSYRTKPGGD ALPVARRRTG LVGFGGVTVS PAPGAFLQAS REGEAALVAA
     ALSGCAGAES VADLFAGSGT IGFPLAARTR VHAVEGDAQA LATLDQGARQ LAGRLTMERR
     DLFRDPVTAA ELARFQAVVI DPPRAGAQAQ AAELARSAVP AVVALSCNPA TFVRDARTLV
     EGGYRLLEVT PIDQFLWSPH LELAALFRR
//
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