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Database: UniProt
Entry: A0A1Q8RI43_9STRE
LinkDB: A0A1Q8RI43_9STRE
Original site: A0A1Q8RI43_9STRE 
ID   A0A1Q8RI43_9STRE        Unreviewed;       455 AA.
AC   A0A1Q8RI43;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:OLN83994.1};
GN   ORFNames=BMI76_02005 {ECO:0000313|EMBL:OLN83994.1};
OS   Streptococcus sp. 'caviae'.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1915004 {ECO:0000313|EMBL:OLN83994.1, ECO:0000313|Proteomes:UP000186915};
RN   [1] {ECO:0000313|EMBL:OLN83994.1, ECO:0000313|Proteomes:UP000186915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cavy grass 6 {ECO:0000313|EMBL:OLN83994.1,
RC   ECO:0000313|Proteomes:UP000186915};
RA   Palakawong Na Ayudthaya S., Marshall I.P., Schreiber L., Plugge C.M.;
RT   "Draft Genome Sequence of Streptococcus caviae Strain Cavy grass 6,
RT   Isolated from Domesticated Guinea Pig Faecal Samples.";
RL   Submitted (NOV-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}.
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:OLN83994.1}.
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DR   EMBL; MOWR01000002; OLN83994.1; -; Genomic_DNA.
DR   RefSeq; WP_075345956.1; NZ_MOWR01000002.1.
DR   AlphaFoldDB; A0A1Q8RI43; -.
DR   STRING; 1915004.BMI76_02005; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000186915; 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: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          2..60
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   455 AA;  51852 MW;  740BBAA3280E0259 CRC64;
     MNLRMKQKIP LKIKRMGING EGIGFYKRTL VFVPGALKGE DVFCQVTRVK ANFAEARLLV
     INKKSKFRIK PQCPIYEECG GCQIMHLRYD KQLDFKEDLL RQALKKFKPQ GYEIYDIRPT
     IGMDEPKHYR AKLQFQTRRF GGVTKAGLFQ EGSHHLVDIK DCLVQDELTQ SIVNHVCQLL
     DKYSIPIYDE RRNAGIRTIM VRKAQATGQV QLIFVSSKEV NLVPVIRELT ADFSEIKTVA
     VNFNASKSSS IYGDRTEILW GADTIAEKVL DYSFSLSPRA FYQLNPRQTQ VLYSQAVKAL
     DVHENDEVID AYCGVGTIGF AFADKVKSVR GMDIIPEAIA DAKENARRMG YTNTHYETGK
     AEDIIPQWYK EGYRATALVV DPPRTGLDDK LLKTICRYQP EKMVYVSCNV STLARDLVKL
     TKSYDVVYIQ SVDMFPHTAR TEAVVKLVKR QKDLS
//
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