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Database: UniProt
Entry: A0A4S4C8A7_9BACL
LinkDB: A0A4S4C8A7_9BACL
Original site: A0A4S4C8A7_9BACL 
ID   A0A4S4C8A7_9BACL        Unreviewed;       537 AA.
AC   A0A4S4C8A7;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:THF83884.1};
GN   ORFNames=E6C55_04180 {ECO:0000313|EMBL:THF83884.1};
OS   Cohnella fermenti.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2565925 {ECO:0000313|EMBL:THF83884.1, ECO:0000313|Proteomes:UP000310636};
RN   [1] {ECO:0000313|EMBL:THF83884.1, ECO:0000313|Proteomes:UP000310636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-MHH1044 {ECO:0000313|EMBL:THF83884.1,
RC   ECO:0000313|Proteomes:UP000310636};
RA   Lin S.-Y., Hung M.-H., Young C.-C.;
RT   "Cohnella sp. nov. isolated from preserved vegetables.";
RL   Submitted (APR-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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:THF83884.1}.
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DR   EMBL; SSOB01000003; THF83884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S4C8A7; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000310636; 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:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   CDD; cd21147; RsmF_methylt_CTD1; 1.
DR   Gene3D; 2.30.130.60; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR031341; Methyltr_RsmF_N.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR027391; Nol1_Nop2_Fmu_2.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR031340; RsmF_methylt_CI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807:SF30; 28S RRNA (CYTOSINE(4447)-C(5))-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF17125; Methyltr_RsmF_N; 1.
DR   Pfam; PF13636; Methyltranf_PUA; 1.
DR   Pfam; PF17126; RsmF_methylt_CI; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
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:UP000310636};
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          22..324
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          329..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        242
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         120..126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         144
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         189
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   537 AA;  58199 MW;  83C7A3333AC8D9FD CRC64;
     MRLPDKFKNT MRSLLEGEAD AFFATYAQPR TAGLRINGLK LGLTEYEERF RDDGRAGFGS
     AGRTADPIPW AAGGVYIGEE DRPGKHLHYY LGLYYIQEPS AMLPAELLDV RPGHRVLDLC
     AAPGGKSTQL AAKLAGRGLL VTNDNAAERT KALAKNTERA GMANAIVTNE EPAALAAAFG
     DFFDRVLVDA PCSGEGMFRK DEDMIREWER HSVERCAAMQ EAILREAAKL VAPGGKLLYS
     TCTFSPKENE LSVARLLSER PDFDVVPLEA PPEWGLAPGR PDWLAAEDTF GLPEERLAQL
     AGTVRVWPHR ARGEGHYAAL LVRRPEPGAE AGESVAPAND GDWQFPPLPA PPAIAAAAKR
     PGRGEASPRG KKPAGKGTAG KGPATSAEDD PRDKLLAFAK TTLPGWRPRG TLYRRGEQLY
     LQPEELPDLG RLNAVRPGLL LGSATKHRFE PSQALAMGLR MEDAALSLRL RSGDGDALRY
     MKGETLQPEP AAIVGTDGEP APGRGWTLVC IDGFPAGWGR WDGTILKNEL LPGWRWI
//
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