GenomeNet

Database: UniProt
Entry: B7HU21_BACC7
LinkDB: B7HU21_BACC7
Original site: B7HU21_BACC7 
ID   B7HU21_BACC7            Unreviewed;       459 AA.
AC   B7HU21;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:ACJ82271.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:ACJ82271.1};
GN   Name=rumA {ECO:0000313|EMBL:ACJ82271.1};
GN   OrderedLocusNames=BCAH187_A0542 {ECO:0000313|EMBL:ACJ82271.1};
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ82271.1, ECO:0000313|Proteomes:UP000002214};
RN   [1] {ECO:0000313|EMBL:ACJ82271.1, ECO:0000313|Proteomes:UP000002214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187 {ECO:0000313|EMBL:ACJ82271.1,
RC   ECO:0000313|Proteomes:UP000002214};
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
RL   Submitted (OCT-2008) 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; CP001177; ACJ82271.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7HU21; -.
DR   KEGG; bcr:BCAH187_A0542; -.
DR   HOGENOM; CLU_014689_7_1_9; -.
DR   Proteomes; UP000002214; Chromosome.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0009451; P:RNA modification; IEA:UniProt.
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; IPR030391; MeTrfase_TrmA_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002792; TRAM_dom.
DR   InterPro; IPR010280; U5_MeTrfase_fam.
DR   NCBIfam; TIGR00479; rumA; 1.
DR   PANTHER; PTHR11061:SF45; -; 1.
DR   PANTHER; PTHR11061; RNA M5U METHYLTRANSFERASE; 1.
DR   Pfam; PF01938; TRAM; 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; PS50926; TRAM; 1.
DR   PROSITE; PS01230; TRMA_1; 1.
DR   PROSITE; PS01231; TRMA_2; 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   DOMAIN          9..67
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        417
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        417
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         292
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         321
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         342
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         390
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   459 AA;  51986 MW;  A3CCCA075F20124E CRC64;
     MIQKQHESKL EVGQTFPVTI KRLGINGEGV GYFKRQVVFI PGALPGEEVV AETTKIQRGF
     AEAKVKKVRK ASPHRVKAPC PVYEECGGCQ LQHLDYKEQL NQKRDIVVQA FEKYMNNSLE
     EKIRPTLGME NPWHYRNKSQ LQVGRKDEKV ITGLYKQNSH QLIDIAHCMI QHKATNEATK
     VVRRILEKLN VSIYNEKKQK GLVRTIVTRT AVQTGEVQVT LITTKEELPN KEQFITEVQK
     QMPAVKSIMQ NVNWRKTSVI FGDKTFKLAG KEVIQETLGD LSFELSARAF FQLNPEQTVV
     LYNEAKKAAA LTGNEKIVDA YCGVGTIGLW LANDAAEVRG MDVIPEAIAD ARKNAKHHGF
     TNTKYEAGKA EQWLPKWVKE GWRPDVIVVD PPRTGCDDKL LETILKVKPK QVVYVSCNPS
     SLARDVQALM KSYEVEYVQP VDMFPHTAHV ENVVKLVRK
//
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