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Database: UniProt
Entry: D1Y8C0_9BACT
LinkDB: D1Y8C0_9BACT
Original site: D1Y8C0_9BACT 
ID   D1Y8C0_9BACT            Unreviewed;       541 AA.
AC   D1Y8C0;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:EFB89376.1};
DE            EC=2.1.1.- {ECO:0000313|EMBL:EFB89376.1};
GN   Name=rumA {ECO:0000313|EMBL:EFB89376.1};
GN   ORFNames=HMPREF7215_0139 {ECO:0000313|EMBL:EFB89376.1};
OS   Pyramidobacter piscolens W5455.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Pyramidobacter.
OX   NCBI_TaxID=352165 {ECO:0000313|EMBL:EFB89376.1, ECO:0000313|Proteomes:UP000006462};
RN   [1] {ECO:0000313|EMBL:EFB89376.1, ECO:0000313|Proteomes:UP000006462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W5455 {ECO:0000313|EMBL:EFB89376.1,
RC   ECO:0000313|Proteomes:UP000006462};
RA   Shrivastava S., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RL   Submitted (DEC-2009) 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:EFB89376.1}.
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DR   EMBL; ADFP01000135; EFB89376.1; -; Genomic_DNA.
DR   RefSeq; WP_009166101.1; NZ_ADFP01000135.1.
DR   AlphaFoldDB; D1Y8C0; -.
DR   STRING; 352165.HMPREF7215_0139; -.
DR   eggNOG; COG2265; Bacteria.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000006462; 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..54
FT                   /note="TRAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50926"
FT   ACT_SITE        402
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        402
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         308
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         329
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         375
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   541 AA;  59957 MW;  0EF4927E3B0F3242 CRC64;
     MEQLYIDRMN SAGQGIGRAA DGRTVFVEGA LPGETAVIAV RQEKKSYIQA RVERVVEANP
     ERREPSCRWY RSCGGCQLQH AEYTLQCQIK AMLAADALRR IGGFEIDGEI PCVPSRNEWR
     YRNKASFPVR ARGRAGDVGF FKRGSHEIVP VDRCPVICDR ANKLYAVVKN MINYGRFCCY
     DEKSNSGWLR HVVIRSARDG EELLLILVAA ARPEGGALES LERLYDHLKE RFPELRGLVV
     NVNPDEGNVI IGAESVLVKG EDRLTERLGN FRLDYDGTSF FQANPGQAEQ LFAYAASLAE
     GQNLLELYCG VGALTAFLSR KAKTIRAVEV WASAVALARE NGESNRIEGL TVLQGAAENV
     VAPADLEGID CVVVDPPRAG CDKSLIETIA ASRVPRVLYI SCNPATLARD AALLRDAGYV
     LDMDSLKVFD MFPQTCHVET VCLLSKLHEA KHHVSVTLDM DEIDITSAES KATYEEIKEY
     VAEHNEGMKV SSLYIAQVKR KCGLELVENF NLPKSEDAKH PQCPKEKEDA IVEALKAFQM
     I
//
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