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Database: UniProt
Entry: A0A542SN37_9MICO
LinkDB: A0A542SN37_9MICO
Original site: A0A542SN37_9MICO 
ID   A0A542SN37_9MICO        Unreviewed;       515 AA.
AC   A0A542SN37;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:TQK75657.1};
GN   ORFNames=FB389_0289 {ECO:0000313|EMBL:TQK75657.1};
OS   Rarobacter incanus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Rarobacteraceae;
OC   Rarobacter.
OX   NCBI_TaxID=153494 {ECO:0000313|EMBL:TQK75657.1, ECO:0000313|Proteomes:UP000316181};
RN   [1] {ECO:0000313|EMBL:TQK75657.1, ECO:0000313|Proteomes:UP000316181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10596 {ECO:0000313|EMBL:TQK75657.1,
RC   ECO:0000313|Proteomes:UP000316181};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (JUN-2019) 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:TQK75657.1}.
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DR   EMBL; VFNV01000001; TQK75657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A542SN37; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000316181; 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   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; 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; 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:UP000316181};
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          217..514
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        444
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         320..326
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         345
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         373
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         391
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   515 AA;  54594 MW;  A59B644A0A235FA2 CRC64;
     MNQRSGQGRG GGRDDRPRAR DGRRDSAGHQ RGAARMRGDG RRSAAAPSMR DRSSDEPRAA
     AFDVLVDVET NDAYANLVLP ARLARADLGG RDAAFATELA YGTLRMQGHY DAILSECVDR
     ALPDIDAPVR VALRLGAHQL LGMRVPAHAA VSQTVGLVRH KIGAGPAQFV NAVLRKVSTK
     TADQWQAGIA AQLSDPVELA SFTYSHPAWI VRALKAALVA NGRDPGELEE LLRADNTPAP
     VMLVARPGLI DPAELLTHSG GGRVARLSPF AVEAGAVPPR HIAAVKDGRA GVQDEGSQLV
     ALALAAAPID GRDKRWLDMC AGPGGKTALL AALAARRGAR VVANEVQPHR AGLVRKNVAA
     AAPGSIEAVR TADGRDIGGD EPGSFDRVLV DAPCTGLGAL RRRPEARWRK QPSDLPELSA
     LQRELLESAL AAVRPGGIVA YVTCSPHVAE TKLVVDDVIR GRDDIEIVDA ARVLESVVVD
     PGDSRVDFGA GPAIQLWPHI HHTDAMHATM LRRLR
//
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