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Database: UniProt
Entry: A0A063BMP0_9BURK
LinkDB: A0A063BMP0_9BURK
Original site: A0A063BMP0_9BURK 
ID   A0A063BMP0_9BURK        Unreviewed;       467 AA.
AC   A0A063BMP0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Sun protein {ECO:0000313|EMBL:KDB09894.1};
GN   ORFNames=LIG30_1096 {ECO:0000313|EMBL:KDB09894.1};
OS   Burkholderia sp. lig30.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB09894.1, ECO:0000313|Proteomes:UP000027020};
RN   [1] {ECO:0000313|EMBL:KDB09894.1, ECO:0000313|Proteomes:UP000027020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA   Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA   Brown S.D., Hazen T.C.;
RT   "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT   Isolated from Wet Tropical Forest Soil.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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:KDB09894.1}.
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DR   EMBL; JGVW01000049; KDB09894.1; -; Genomic_DNA.
DR   RefSeq; WP_038709750.1; NZ_JGVW01000049.1.
DR   AlphaFoldDB; A0A063BMP0; -.
DR   STRING; 1192124.LIG30_1096; -.
DR   PATRIC; fig|1192124.4.peg.771; -.
DR   eggNOG; COG0144; Bacteria.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000027020; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00563; rsmB; 1.
DR   PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000027020};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          194..467
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          434..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        402
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         282..288
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         304
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         330
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         349
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   467 AA;  50009 MW;  591A386206A9242A CRC64;
     MTRPRSSAKP SPVRPARFSA LHLAPDSLGF ALDAAAQAVD AVARGTALPA ALAAVFAGMV
     PGAQTIARGA TQDIAYRTMR RLGSADWLIG RLVSKAPPAH VHAVLACSLA LLLDDASDAA
     YSPFTVVDQA VTTIGARREF VFAKGLVNAV LRRFLRERAA LVAAMQADPV ARWNYRAWWV
     DAVERAWPND WQAVLAAGDR PGPLTLRVNA RRTTVDAYLE LLRAQGIDAA AIGRHAVRLA
     SPLPVERIPG FADGVVSVQD AGAQLAAQWL DARDGMRVLD ACAAPGGKTG HLLELADVEV
     VALESDAIRA TRIGENLARL SLAADVRVGD AGTPAQWHDG RPFDRILADV PCSASGIVRR
     HPDIRWLRRA TDIDALVAEQ RRILSALWPL VKPGGELLYV TCSIFPEEGE AQARWFEAAC
     EDAVRLDAPG QLLPCSVPGG PQDGSGSSEP GQHTDHDGFF YARFQKR
//
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