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Database: UniProt
Entry: A0A3D9UWL0_9MICO
LinkDB: A0A3D9UWL0_9MICO
Original site: A0A3D9UWL0_9MICO 
ID   A0A3D9UWL0_9MICO        Unreviewed;       512 AA.
AC   A0A3D9UWL0;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=16S rRNA (Cytosine967-C5)-methyltransferase {ECO:0000313|EMBL:REF30985.1};
GN   ORFNames=DFJ65_2023 {ECO:0000313|EMBL:REF30985.1};
OS   Calidifontibacter indicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Calidifontibacter.
OX   NCBI_TaxID=419650 {ECO:0000313|EMBL:REF30985.1, ECO:0000313|Proteomes:UP000256253};
RN   [1] {ECO:0000313|EMBL:REF30985.1, ECO:0000313|Proteomes:UP000256253}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22967 {ECO:0000313|EMBL:REF30985.1,
RC   ECO:0000313|Proteomes:UP000256253};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2018) 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:REF30985.1}.
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DR   EMBL; QTUA01000001; REF30985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D9UWL0; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000256253; 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; 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};
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..510
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        443
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         318..324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         343
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         372
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         390
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   512 AA;  54607 MW;  3F73830D244AE7A1 CRC64;
     MSDRPNHGAD GSDPGDSGYR NARGRQRPDA RRTSDRARSA QAPSQRRRTG DPTRRIAWEV
     LRDVHENGAY ANLALPKALR HKRIDGRDAA FASELVYGTL RMRGFYDKVI EHAAGRGAAQ
     IDPPVLDTIR LGAHQLLAMR VPSHAAASET VALAREVNGA GAAGFTNAVL RRISERTREE
     WVAQVTAGRQ PLDALAVEHS HPEWVVRALR GALIGSGVAD AESADSELGR LLAADNDPAD
     VTLVARPHLA TVEELVDAGA VASTLSPFAA RLSGGDPGAI RAVRETRAAV QDEGSQLLAI
     ALASVPVDGD QQEWLDLCAG PGGKAALLAC LAAEQDSVLF ANEASEHRTE LVRRTMDAAL
     RSGIEVMIGT GDGRDLGREE PNTYDKVLVD APCTGLGALR RRPEARWRKT AADVPPLATL
     QGELLDSAIA ATRPGGVIGY ATCSPHTAET AAVVADALKR HPEVVQEDAR PYFKDASGKQ
     IADLGDGPAV QLWPHLHDTD AMFFALLRKT DN
//
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