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Database: UniProt
Entry: A0A0P0SD59_9PSEU
LinkDB: A0A0P0SD59_9PSEU
Original site: A0A0P0SD59_9PSEU 
ID   A0A0P0SD59_9PSEU        Unreviewed;       325 AA.
AC   A0A0P0SD59;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=RNA methyltransferase {ECO:0000313|EMBL:ALL82173.1};
GN   ORFNames=AD017_15085 {ECO:0000313|EMBL:ALL82173.1};
OS   Pseudonocardia sp. EC080619-01.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL82173.1, ECO:0000313|Proteomes:UP000066228};
RN   [1] {ECO:0000313|EMBL:ALL82173.1, ECO:0000313|Proteomes:UP000066228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL82173.1,
RC   ECO:0000313|Proteomes:UP000066228};
RX   PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA   Van Arnam E.B., Sit C.S.;
RT   "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL   J. Am. Chem. Soc. 137:14272-14274(2015).
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family.
CC       {ECO:0000256|ARBA:ARBA00007228}.
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DR   EMBL; CP012184; ALL82173.1; -; Genomic_DNA.
DR   RefSeq; WP_060574608.1; NZ_CP012184.1.
DR   AlphaFoldDB; A0A0P0SD59; -.
DR   STRING; 1096856.AD017_15085; -.
DR   KEGG; pecq:AD017_15085; -.
DR   PATRIC; fig|1096856.3.peg.3164; -.
DR   OrthoDB; 9785673at2; -.
DR   Proteomes; UP000066228; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd18103; SpoU-like_RlmB; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR013123; SpoU_subst-bd.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   NCBIfam; TIGR00186; rRNA_methyl_3; 1.
DR   PANTHER; PTHR46429; 23S RRNA (GUANOSINE-2'-O-)-METHYLTRANSFERASE RLMB; 1.
DR   PANTHER; PTHR46429:SF1; 23S RRNA (GUANOSINE-2'-O-)-METHYLTRANSFERASE RLMB; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000313|EMBL:ALL82173.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066228};
KW   Transferase {ECO:0000313|EMBL:ALL82173.1}.
FT   DOMAIN          81..157
FT                   /note="RNA 2-O ribose methyltransferase substrate binding"
FT                   /evidence="ECO:0000259|SMART:SM00967"
FT   REGION          1..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   325 AA;  33928 MW;  AED2ACF97621866C CRC64;
     MAGNSKRRGA VRKEGTKKGP VIGSGGQPRR SLRGKGPTPS GEMRPGHPKQ KAAARRDRQD
     QQQQRRRPVA GRRGDGEGPE TVLGRNPVVE CLRAGVPSTA LHVATGMSAD ERVAEAVSLA
     AEQGISILEV PRNDLDRLTG GALHQGLALQ VPPYSYAHPD ELLEAAADSG RPALTVALDG
     VTDPRNLGAV VRSVGAFGGH GVVVPQRRAA GMTAVAWRTS AGTAVRVPVA RATNLTRTLR
     EYASAGLMVV GLAADGDVSL DEFDLATGPL ALVTGSEGKG LSRLVRETCD LTVSIPLAGR
     VESLNASVAT GVVLAEVARR RRLER
//
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