RSMB_SYNY3
ID RSMB_SYNY3 Reviewed; 446 AA.
AC P72943;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable ribosomal RNA small subunit methyltransferase B {ECO:0000305};
DE EC=2.1.1.176 {ECO:0000250|UniProtKB:P36929};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000250|UniProtKB:P36929};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000250|UniProtKB:P36929};
GN Name=rsmB {ECO:0000250|UniProtKB:P36929}; Synonyms=sun;
GN OrderedLocusNames=slr0679;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000250|UniProtKB:P36929}.
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:0000250|UniProtKB:P36929};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P36929}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000255|PROSITE-ProRule:PRU01023}.
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DR EMBL; BA000022; BAA16960.1; -; Genomic_DNA.
DR PIR; S74920; S74920.
DR AlphaFoldDB; P72943; -.
DR SMR; P72943; -.
DR IntAct; P72943; 5.
DR STRING; 1148.1652035; -.
DR PaxDb; P72943; -.
DR EnsemblBacteria; BAA16960; BAA16960; BAA16960.
DR KEGG; syn:slr0679; -.
DR eggNOG; COG0144; Bacteria.
DR eggNOG; COG0781; Bacteria.
DR InParanoid; P72943; -.
DR OMA; RVNRQHH; -.
DR PhylomeDB; P72943; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 1.10.940.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR InterPro; IPR001678; MeTrfase_RsmB/NOP2.
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 PANTHER; PTHR22807; PTHR22807; 1.
DR Pfam; PF01189; Methyltr_RsmB-F; 1.
DR Pfam; PF01029; NusB; 1.
DR PRINTS; PR02008; RCMTFAMILY.
DR SUPFAM; SSF48013; SSF48013; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00563; rsmB; 1.
DR PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..446
FT /note="Probable ribosomal RNA small subunit
FT methyltransferase B"
FT /id="PRO_0000211817"
FT ACT_SITE 383
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 260..266
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 311
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
FT BINDING 330
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 446 AA; 49730 MW; 70E42B574FC42FF8 CRC64;
MISARQLAFL ILRDINRRDS YTDVAIDRAL QKHPLSPPDR RFCTELVYGV VRRQRTLDCL
IEQLGDRPIG KQPPDLRRIV QLGLYQLRYL DQVPASAAVN TGVDLAKANG LKGLSKVVNG
MLRRYQRAEE QGKNILDQEK ISLGEQYSFP DWLMELFEQT WGKAETESLC AYFNQNPSLD
LRINPLKTSR VEVAQSLAEL NLTTTAMAGL PQGLRLGGKT GAITQLPGFA EGWWTVQDAS
AQWVAQILNP QPEETIFDVC AAPGGKTTHI AELMGDQGQI YAGDRHGWRL QKLAVTQQRL
GLTSIKIWEG DLTQPGVKPP VELVDRALLD VPCSGLGTLH RNPDLRWRQT PATIATLLPL
QQALLKAIAP LVKSGGTLVY STCTLNPAEN EAQIERFLQD HEDWRSEPFE WTSPQGQTNS
VTSGMLTILP HHHHQDGFFI ANLKKA
