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Database: UniProt
Entry: A0A0B9A3X4_BRELN
LinkDB: A0A0B9A3X4_BRELN
Original site: A0A0B9A3X4_BRELN 
ID   A0A0B9A3X4_BRELN        Unreviewed;       499 AA.
AC   A0A0B9A3X4;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Fmu (Sun) domain protein {ECO:0000313|EMBL:KHS53403.1};
GN   ORFNames=AE0388_0891 {ECO:0000313|EMBL:KHS53403.1};
OS   Brevibacterium linens.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS53403.1, ECO:0000313|Proteomes:UP000031488};
RN   [1] {ECO:0000313|EMBL:KHS53403.1, ECO:0000313|Proteomes:UP000031488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AE038-8 {ECO:0000313|EMBL:KHS53403.1,
RC   ECO:0000313|Proteomes:UP000031488};
RA   Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT   "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL   Submitted (NOV-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|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:KHS53403.1}.
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DR   EMBL; JTJZ01000015; KHS53403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B9A3X4; -.
DR   PATRIC; fig|1703.6.peg.774; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000031488; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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:UP000031488};
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          213..498
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        421
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         304..310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         329
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         354
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         368
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   499 AA;  53104 MW;  7E4B8FECDB6A4324 CRC64;
     MAESADRDRR GGSRGGNRGG NRGQRRGDPR DRKQQDRGAP QAERAGKNLP RRIAWEVLLD
     VATKDAYANL LLPAKLSRTH MGAQDAAFTT ELTYGALRRQ KFYDAVIEVA SSRAIEKIDP
     EPLAAMRLGA HQLLSMRVPN HAALSETVAV VKRSSPKTAG FVNAVLRRIS EAEPAEWLDR
     VTAETSETAR LAIEHSHPEW VVRALTQALK GHGRDAAELE ALLAADNAPA KVGVTALPGL
     IDRTELPGEP TPLSPIGVTL NTAAPRDVAA VADGRARVQD EGSALVALAL AEVDAPAGTW
     ADLCAGPGGK AAVLGAAAAG ESLTLEAFDS SEHRVDLVRD STKALSNVTA ALRDGRDARG
     PYSKILVDVP CSGLGALRRR PEARYRRRPE DITALSGLQR ELLSSALDAC APGGVIAYST
     CSPHYAETVL IVDEVLRLRA KSGSDDIEVL DAPAVLSSIT GTEAESFASV TRDGGRYAQL
     WPHLHNSDGM FLALLRKAK
//
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