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Database: UniProt
Entry: A0A1S1NWK5_9GAMM
LinkDB: A0A1S1NWK5_9GAMM
Original site: A0A1S1NWK5_9GAMM 
ID   A0A1S1NWK5_9GAMM        Unreviewed;       470 AA.
AC   A0A1S1NWK5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=23S rRNA (Uracil(1939)-C(5))-methyltransferase RlmD {ECO:0000313|EMBL:QEL11000.1};
DE            EC=2.1.1.190 {ECO:0000313|EMBL:QEL11000.1};
DE   SubName: Full=23S rRNA (Uracil-5-)-methyltransferase RumA {ECO:0000313|EMBL:OHV12341.1};
GN   Name=rlmD {ECO:0000313|EMBL:QEL11000.1};
GN   ORFNames=BH688_03825 {ECO:0000313|EMBL:OHV12341.1}, FY550_07580
GN   {ECO:0000313|EMBL:QEL11000.1};
OS   Kushneria phosphatilytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Kushneria.
OX   NCBI_TaxID=657387 {ECO:0000313|EMBL:OHV12341.1, ECO:0000313|Proteomes:UP000179907};
RN   [1] {ECO:0000313|EMBL:OHV12341.1, ECO:0000313|Proteomes:UP000179907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCWA18 {ECO:0000313|EMBL:OHV12341.1,
RC   ECO:0000313|Proteomes:UP000179907};
RA   Wang C., Qu L.;
RT   "The draft genome suquence of Kushneria sp. YCWA18.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEL11000.1, ECO:0000313|Proteomes:UP000322553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCWA18 {ECO:0000313|EMBL:QEL11000.1,
RC   ECO:0000313|Proteomes:UP000322553};
RA   Du G.-X., Qu L.-Y.;
RT   "Complete genome sequence of Kushneria sp. YCWA18, a halophilic phosphate-
RT   solubilizing bacterium isolated from Daqiao saltern in China.";
RL   Submitted (AUG-2019) 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; MKZT01000006; OHV12341.1; -; Genomic_DNA.
DR   EMBL; CP043420; QEL11000.1; -; Genomic_DNA.
DR   RefSeq; WP_070977879.1; NZ_MKZT01000006.1.
DR   AlphaFoldDB; A0A1S1NWK5; -.
DR   STRING; 657387.BH688_03825; -.
DR   KEGG; kuy:FY550_07580; -.
DR   OrthoDB; 9804590at2; -.
DR   Proteomes; UP000179907; Unassembled WGS sequence.
DR   Proteomes; UP000322553; Chromosome.
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:0001510; P:RNA methylation; IEA:GOC.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; 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; PS01230; TRMA_1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01024}; Reference proteome {ECO:0000313|Proteomes:UP000179907};
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   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10015"
FT   ACT_SITE        422
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         297
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         326
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         347
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
FT   BINDING         396
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01024"
SQ   SEQUENCE   470 AA;  52588 MW;  A88979DACF63A970 CRC64;
     MAKLGVRRPV AERQKRRRGK NAGECRRQEE DGLLTIERQA HDGRGVTRNA HGKTVFVERA
     LPGERLIPAV HAEHRRYDEA HVRELLATAP ERVTPHCRHF GQCGGCDLQH QALSAQQAHR
     QAVLVEQFAH HDLTLPDVEL ISCDDDRSGY GYRRRARLGV RVDHEAALYF GFRRRGQDML
     FNIEQCPILV PRLEALLLPL RRHLDQLEAP RRVGHVELLQ LDDQCCLSIR QLREVPGDIE
     RWRRFAAEHQ LALVMNIGRD DMTSHRLDNG APLQQTLEVG QKREKVTLEL SPGDFLQANA
     AVNQALVDTV LDWSAVTAEE LVFDLFAGIG NFSLPLAAAG ACVTAVEGRA SMVESLRRNA
     ELNGLSQQLT ATRADLGEPQ VLKDESLSKA GLVVLDPPRH GARSIVSRLA VARPERVIYV
     SCDPATLARD VRTLVDGGYR IERAAVVDMF PQTAHQESVL LLRRTDRTAI
//
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