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Database: UniProt
Entry: A0A089J8J5_9BACL
LinkDB: A0A089J8J5_9BACL
Original site: A0A089J8J5_9BACL 
ID   A0A089J8J5_9BACL        Unreviewed;       508 AA.
AC   A0A089J8J5;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=rRNA cytosine-C5-methyltransferase {ECO:0000313|EMBL:AIQ17474.1};
GN   ORFNames=H70357_12985 {ECO:0000313|EMBL:AIQ17474.1};
OS   Paenibacillus sp. FSL H7-0357.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536774 {ECO:0000313|EMBL:AIQ17474.1, ECO:0000313|Proteomes:UP000029508};
RN   [1] {ECO:0000313|EMBL:AIQ17474.1, ECO:0000313|Proteomes:UP000029508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0357 {ECO:0000313|EMBL:AIQ17474.1,
RC   ECO:0000313|Proteomes:UP000029508};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-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|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}.
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DR   EMBL; CP009241; AIQ17474.1; -; Genomic_DNA.
DR   RefSeq; WP_038599354.1; NZ_CP009241.1.
DR   AlphaFoldDB; A0A089J8J5; -.
DR   STRING; 1536774.H70357_12985; -.
DR   KEGG; paeh:H70357_12985; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG3270; Bacteria.
DR   HOGENOM; CLU_005316_6_1_9; -.
DR   Proteomes; UP000029508; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent 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; IPR001678; MeTrfase_RsmB/NOP2.
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};
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          16..296
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          315..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        233
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         111..117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         135
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         180
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   508 AA;  54806 MW;  52C4A9ED67C0B6EF CRC64;
     MAAQLPGTFT QRMKELLGTE YEQFAETYKE TPYGGIRANT LKISVKDLLA LAPFELEPIP
     WCPTGFYTGE GARPGKHPYY HAGLYYIQEP SAMAPVELLD VQPGDRVLDL CAAPGGKSTQ
     IAAKLQGEGL LVSNDLHPER TKALAKNLEL YGVRNGIVLN ESPERIAAAF PGFFDRILID
     APCSGEGMFR KDEDMVKQWE PGTPEKYAAM QRDILVSAAA ALKPGGTLVY STCTFAVEEN
     EGTIADFLAA HPRFSPVPAG GTGSFAPGFG ELPETARLWP HKVKGEGHFM AVLRHDGSLA
     PEEEDGDRDI ALGIAARNKS GKASPSAKAA GGKTERGRGG KGGRAFGKSG NGSGREQQSI
     GEETRLAAYT DFFKEQLGWQ PAGYPVWFGE HLYISPLPKE ALDGLKTIRP GWYVGHVRSG
     RFIPGHPLAT ALHPEESCRS LSLSGSSGEA VSYLKGETLS IPAERLSVKS GSALKGYVLV
     CIDGYSAGWA KWQDGMLKNE YPAGWRWT
//
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