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Database: UniProt
Entry: F4A2D7_MAHA5
LinkDB: F4A2D7_MAHA5
Original site: F4A2D7_MAHA5 
ID   F4A2D7_MAHA5            Unreviewed;       447 AA.
AC   F4A2D7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
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   OrderedLocusNames=Mahau_0986 {ECO:0000313|EMBL:AEE96184.1};
OS   Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family IV. Incertae Sedis; Mahella.
OX   NCBI_TaxID=697281 {ECO:0000313|EMBL:AEE96184.1, ECO:0000313|Proteomes:UP000008457};
RN   [1] {ECO:0000313|Proteomes:UP000008457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC   {ECO:0000313|Proteomes:UP000008457};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Pukall R.,
RA   Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Mahella australiensis DSM 15567.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEE96184.1, ECO:0000313|Proteomes:UP000008457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC   {ECO:0000313|Proteomes:UP000008457};
RX   PubMed=21886860;
RA   Sikorski J., Teshima H., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA   Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M.,
RA   Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Ngatchou-Djao O.D., Rohde M.,
RA   Pukall R., Spring S., Abt B., Goker M., Detter J.C., Woyke T., Bristow J.,
RA   Markowitz V., Hugenholtz P., Eisen J.A., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Mahella australiensis type strain (50-1
RT   BON).";
RL   Stand. Genomic Sci. 4:331-341(2011).
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|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CP002360; AEE96184.1; -; Genomic_DNA.
DR   RefSeq; WP_013780614.1; NC_015520.1.
DR   AlphaFoldDB; F4A2D7; -.
DR   STRING; 697281.Mahau_0986; -.
DR   KEGG; mas:Mahau_0986; -.
DR   eggNOG; COG0144; Bacteria.
DR   eggNOG; COG0781; Bacteria.
DR   HOGENOM; CLU_005316_0_1_9; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000008457; Chromosome.
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   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
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; 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:UP000008457};
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          169..446
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        381
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         259..265
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         283
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         310
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         328
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   447 AA;  51058 MW;  731EDD0F7FAA2BE3 CRC64;
     MVDKARNAAL KLLRDIDIKK AYINLEIKPA LKDNSLSTLD RAFITDMVYG VTRYRLTLDW
     LIKRYSRGGK ASPWIRNILR MGMYQILYMD RVPDFAACDS SVELAKKYAG QREAGYVNAV
     LRRLIQEKDH LVSLFPQDTV SRIALKYSFP EWMVRLWLNT MSETSVEELC AAQNIRPSLT
     IRANELKISQ DDLIKLLEQR SIMYSCGVYL PEALNIEQNV DVESLPGYDD GLFAVQDEAS
     MMVAHVVDPR PGQIIIDACS APGGKAVHMA QFMKDQGRIL SVDVYPHRIE LIKAQCARLG
     VNCVEPVCYD STIYNEDWYG VADAVLIDAP CSALGIIRHK PDIKWRRIEK DIGELLQIQR
     QILDTCSLYV KPRGALIYST CTINPDENQN MVNSFLNDHS DFILDDVYQK LPHALSASRD
     SRDKWVQFYP NEDKIDGFFV ARMLKVR
//
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