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Database: UniProt
Entry: G5K9F4_9STRE
LinkDB: G5K9F4_9STRE
Original site: G5K9F4_9STRE 
ID   G5K9F4_9STRE            Unreviewed;       453 AA.
AC   G5K9F4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EHI64502.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:EHI64502.1};
GN   Name=rumA_1 {ECO:0000313|EMBL:EHI64502.1};
GN   ORFNames=STRPS_0373 {ECO:0000313|EMBL:EHI64502.1};
OS   Streptococcus pseudoporcinus LQ 940-04.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=875093 {ECO:0000313|EMBL:EHI64502.1, ECO:0000313|Proteomes:UP000003217};
RN   [1] {ECO:0000313|EMBL:EHI64502.1, ECO:0000313|Proteomes:UP000003217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LQ940-04 {ECO:0000313|Proteomes:UP000003217};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA   Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
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:EHI64502.1}.
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DR   EMBL; AEUY02000005; EHI64502.1; -; Genomic_DNA.
DR   RefSeq; WP_007894741.1; NZ_AEUY02000005.1.
DR   AlphaFoldDB; G5K9F4; -.
DR   STRING; 361101.GCA_900102825_01578; -.
DR   GeneID; 58554932; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000003217; Unassembled WGS sequence.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; IEA:UniProt.
DR   GO; GO:0001510; P:RNA methylation; IEA:GOC.
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:SF48; 23S RRNA (URACIL(747)-C(5))-METHYLTRANSFERASE RLMC; 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          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;  51191 MW;  7720148DD9FA3583 CRC64;
     MLKKNDIVEV VIEDLSHQGS GIAKVDGFVF FVENALPTER ITMRVLKLNK KIGFGKVEDY
     LEKSPHRNEN LDLAYLRTGI ADFGHLAYEE QLLFKAKQVK DNLYKTAGIK AVELLPTIGM
     EQPYAYRNKA QIPVRRVNGQ LETGFFRKNS HDLLPISDFY IQDKEIDKLI LFVRNLLRRF
     QVSPYNEADQ SGLIKNLVVR RGHYSGQMML VFVTSRPKVF RVEQMVQLIT EAFPQVVSIM
     QNVNDQNSNA IFSKDFKVLY GQDYITDSIL GNDYMISAQS FYQVNTVMAE KLYQTAIDFS
     DLSADDVVID AYSGIGTIGL SFAKKVKKVY GVEVIEAAVK DARKNAERNG IRNAEFLVGS
     AEAAMEKWSK EGIKPSVILV DPPRKGLTES FIKASAAMAP KKITYVSCNP ATMARDIKHY
     QELGYNLIKA QPVDLFPHTH HVECIALIQR VKS
//
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