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Database: UniProt
Entry: A0A2S4Z4P9_9ACTN
LinkDB: A0A2S4Z4P9_9ACTN
Original site: A0A2S4Z4P9_9ACTN 
ID   A0A2S4Z4P9_9ACTN        Unreviewed;       475 AA.
AC   A0A2S4Z4P9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:POX55968.1};
GN   ORFNames=C3489_07355 {ECO:0000313|EMBL:POX55968.1};
OS   Streptomyces sp. Ru71.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2080746 {ECO:0000313|EMBL:POX55968.1, ECO:0000313|Proteomes:UP000237414};
RN   [1] {ECO:0000313|EMBL:POX55968.1, ECO:0000313|Proteomes:UP000237414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ru71 {ECO:0000313|EMBL:POX55968.1,
RC   ECO:0000313|Proteomes:UP000237414};
RA   Suneja G., Sharma R.;
RT   "Genome sequencing of cellulose degrading bacteria.";
RL   Submitted (FEB-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|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:POX55968.1}.
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DR   EMBL; PQSS01000008; POX55968.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4Z4P9; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000237414; 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; 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:UP000237414};
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          188..474
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        412
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         291..297
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         316
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         342
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         359
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   475 AA;  51229 MW;  3646F3EA7BADCCDC CRC64;
     MSDTPGTSRR PRRPAKPYRR PQKDPVRILA FEALRAVDER DAYANLVLPP LLRKAREKSD
     FDARDAALAT ELVYGTLRRQ GTYDAVIAAC VDRPLREVDP PVLDVLSLGA HQLLGTRIPT
     HAAVSATVEL ARVVLGDGRA KFVNAVLRKV AQRDLDAWLA EVAPPYDDDP EDHLAVVHAH
     PRWVVSALWD SLGGGREGIE RLLAADNERP EVTLVARPGR ATPEELLGEE AAVPGRWSPY
     AVRLAEGGEP GAVEAVREGR AGVQDEGSQL VALALANAPV EGRDRLWLDG CAGPGGKAAL
     LGALAAERGA MLLASEKQPH RAGLVAKALA GNPGPYQVIT ADGTRPAWRP GSFDRVLVDV
     PCSGLGALRR RPEARWRRRP EDLDAFAPLQ RGLLRTALES VRVGGVVGYA TCSPHLAETR
     AVVADVLKQF PDTDLLDARP LLPDVTDLGD GPDIQLWPHI HGTDAMYLAL IRRTG
//
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