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Database: UniProt
Entry: B1C027_9FIRM
LinkDB: B1C027_9FIRM
Original site: B1C027_9FIRM 
ID   B1C027_9FIRM            Unreviewed;       481 AA.
AC   B1C027;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=16S rRNA (cytosine(967)-C(5))-methyltransferase {ECO:0000256|ARBA:ARBA00012140};
DE            EC=2.1.1.176 {ECO:0000256|ARBA:ARBA00012140};
DE   AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|ARBA:ARBA00030399};
DE   AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|ARBA:ARBA00031088};
GN   Name=sun {ECO:0000313|EMBL:EDS75517.1};
GN   ORFNames=CLOSPI_00554 {ECO:0000313|EMBL:EDS75517.1};
OS   Thomasclavelia spiroformis DSM 1552.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=428126 {ECO:0000313|EMBL:EDS75517.1, ECO:0000313|Proteomes:UP000004910};
RN   [1] {ECO:0000313|EMBL:EDS75517.1, ECO:0000313|Proteomes:UP000004910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75517.1,
RC   ECO:0000313|Proteomes:UP000004910};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium spiroforme (DSM 1552).";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS75517.1, ECO:0000313|Proteomes:UP000004910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1552 {ECO:0000313|EMBL:EDS75517.1,
RC   ECO:0000313|Proteomes:UP000004910};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC       of 16S rRNA. {ECO:0000256|ARBA:ARBA00002724}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(967) in 16S rRNA + S-adenosyl-L-methionine = 5-
CC         methylcytidine(967) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42748, Rhea:RHEA-COMP:10219, Rhea:RHEA-COMP:10220,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74483, ChEBI:CHEBI:82748; EC=2.1.1.176;
CC         Evidence={ECO:0000256|ARBA:ARBA00000588};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EDS75517.1}.
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DR   EMBL; ABIK02000005; EDS75517.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1C027; -.
DR   STRING; 428126.CLOSPI_00554; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   HOGENOM; CLU_005316_0_1_9; -.
DR   Proteomes; UP000004910; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; 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; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00563; rsmB; 1.
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:UP000004910};
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          215..481
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        433
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         311..317
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         335
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         362
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         381
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   481 AA;  55548 MW;  82385EB5FEA991DE CRC64;
     MRYKEVVRSF LKSQSNKEKN TNPHSQLHIL TQPEVIPNNS GRKENWYIRF ITLCMSNFNI
     PGKIMAREVA LEILLKYHNE HSYLNITLNE YLKNSTLSRN DKDLVTRIVY GTVQNMIYLE
     YQLEPYIKNK KVKSREKMIL LMSLYQLIFL DKVPEYAIID EAVKLAKKKN FYAGKFVNAI
     LRNYLRNGKR KIETKDELEK LSIETSHPLW LVKMFTKQYD YETAKKICIH DNTPPGRTAR
     VNTLKTNKNT LLKEGCFENG NLAPDALLYN AGNIAESTYF KEGLVTIQDE SSQLVAPLLS
     PSEDDLVLDM CCAPGSKTTH LAALMNNKGK IIACDLFEHK IKLVKENLKR LNISNVELHA
     IDATTLKEKY LEGTFDKILL DAPCSGLGVM KRKPEIKYHD SSVMDTIIPL QAKLLDNAYY
     LLKNNGKMVY STCTINKKEN EQMIKKFLDK YPDMKIVEER KILPFVYDSD GFYMCKLEKG
     K
//
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