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Database: UniProt
Entry: E3CQD0_STRVE
LinkDB: E3CQD0_STRVE
Original site: E3CQD0_STRVE 
ID   E3CQD0_STRVE            Unreviewed;       453 AA.
AC   E3CQD0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EFQ59122.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:EFQ59122.1};
GN   Name=rumA {ECO:0000313|EMBL:EFQ59122.1};
GN   ORFNames=HMPREF9192_1386 {ECO:0000313|EMBL:EFQ59122.1};
OS   Streptococcus vestibularis F0396.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=904306 {ECO:0000313|EMBL:EFQ59122.1, ECO:0000313|Proteomes:UP000004896};
RN   [1] {ECO:0000313|EMBL:EFQ59122.1, ECO:0000313|Proteomes:UP000004896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0396 {ECO:0000313|EMBL:EFQ59122.1,
RC   ECO:0000313|Proteomes:UP000004896};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-2010) 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:EFQ59122.1}.
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DR   EMBL; AEKO01000007; EFQ59122.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3CQD0; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000004896; 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: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; RNA M5U METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11061:SF30; TRNA (URACIL(54)-C(5))-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          1..59
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        408
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        408
FT                   /note="Nucleophile"
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         312
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         333
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   453 AA;  51197 MW;  B3DD979EA0B1AAB5 CRC64;
     MLNKNAIVEV EIVDLTHEGA GVAKVDGFVF FVDNALPGEV IKMRVLKLKK NIGFGKVEEY
     VTLSPNRNQD IDATYLRSGI ADFGHMTYEE QLKFKRKQVV DNLYKTAGIS DVEVAETLGM
     DTPYAYRNKA QVPVRRVKGQ LETGFYRKNS HDLIPIEDFL IQDKEIDKLI VFVRDLLRRY
     DLKPYDEKEQ TGLIRHLVVR RGHYSGQMML VFVTTRPKVF RIDQVIAMIT EAFPSVVSII
     QNINDKNTNA IFGKEFRTLY GQDTITDSML GNDYEISAQS FYQVNTEMAE KLYQTAIDFS
     DLNSDSIVID AYSGIGTIGL SFAKQVKEVY GVEVIETAVE DAKKNAERNG ITNAHYVADS
     AENAMAKWSK DGIKPDIIIV DPPRKGLTES FIKASVAMQP EKITYVSCNP ATMARDIKSY
     QELGYELKKV QPVDLFPQTH HVECVVLLQR SKG
//
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