ID A0A192H3P8_9LACO Unreviewed; 467 AA.
AC A0A192H3P8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:ANK63444.1};
GN ORFNames=AYR53_12135 {ECO:0000313|EMBL:ANK63444.1};
OS Loigolactobacillus backii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Loigolactobacillus.
OX NCBI_TaxID=375175 {ECO:0000313|EMBL:ANK63444.1, ECO:0000313|Proteomes:UP000078582};
RN [1] {ECO:0000313|EMBL:ANK63444.1, ECO:0000313|Proteomes:UP000078582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMW 1.1989 {ECO:0000313|EMBL:ANK63444.1,
RC ECO:0000313|Proteomes:UP000078582};
RA Behr J., Geissler A.J., Vogel R.F.;
RT "Pediococcus and Lactobacillus from brewery environment - whole genome
RT sequencing and assembly.";
RL Submitted (MAR-2016) 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; CP014873; ANK63444.1; -; Genomic_DNA.
DR RefSeq; WP_068225422.1; NZ_RHNQ01000019.1.
DR STRING; 375175.AYR53_12135; -.
DR GeneID; 42983011; -.
DR KEGG; lbt:AYR52_07405; -.
DR OrthoDB; 9804590at2; -.
DR Proteomes; UP000078582; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000078582};
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 421
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT ACT_SITE 421
FT /note="Nucleophile"
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 325
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"
FT BINDING 394
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ SEQUENCE 467 AA; 52412 MW; E0BF12282BC54F73 CRC64;
MANSNYEHGT SNIEIGQRFP LTIKRLGING EGIGYYKHTV VFVQGALPDE VVVAEVVATA
PHFITAKIHK IRQQSPARVT PRDEQYGDVG GIELEHLAYP EQLKFKADVI QQALEKFRPQ
GYKNYDVRPT IGMDDPYEYR NKAQFQVRQL NGHVAAGLYR KNSHDLVDLP TFSTQRPAIM
TTMRYLVNLI EQLAIPVYDE TAKSGIIKTI AIRESITTGH LQVTLITNTP KLPKKHALLT
AIAADLPEVT SVMQNINPGE TSLIWGEETR HLAGDTYLTE TINGYTFKLS ARAFFQLNPK
QTEKLYQLAE QALNLSQHET LIDAYCGVGT LGISLADTAS EVRGMDTIPE AIADAKENAE
LNQVTNAHYE VGKAEELLPQ WLREGFEPDA LIVDPPRTGL DNQLRQAILD SRPEKFVYIS
CNPSTLARDL VSLVKDYRVD YIQSIDMFPQ TARVEAVVKF SKRQLYR
//
