ID G9Y317_HAFAL Unreviewed; 430 AA.
AC G9Y317;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase B {ECO:0000256|HAMAP-Rule:MF_01856};
DE EC=2.1.1.176 {ECO:0000256|HAMAP-Rule:MF_01856};
DE AltName: Full=16S rRNA m5C967 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01856};
DE AltName: Full=rRNA (cytosine-C(5)-)-methyltransferase RsmB {ECO:0000256|HAMAP-Rule:MF_01856};
GN Name=rsmB {ECO:0000256|HAMAP-Rule:MF_01856};
GN Synonyms=sun {ECO:0000256|HAMAP-Rule:MF_01856};
GN ORFNames=HMPREF0454_00942 {ECO:0000313|EMBL:EHM46424.1};
OS Hafnia alvei ATCC 51873.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1002364 {ECO:0000313|EMBL:EHM46424.1, ECO:0000313|Proteomes:UP000005959};
RN [1] {ECO:0000313|EMBL:EHM46424.1, ECO:0000313|Proteomes:UP000005959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51873 {ECO:0000313|EMBL:EHM46424.1,
RC ECO:0000313|Proteomes:UP000005959};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the cytosine at position 967 (m5C967)
CC of 16S rRNA. {ECO:0000256|ARBA:ARBA00002724, ECO:0000256|HAMAP-
CC Rule:MF_01856}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01856};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01856}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC ECO:0000256|HAMAP-Rule:MF_01856, 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:EHM46424.1}.
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DR EMBL; AGCI01000013; EHM46424.1; -; Genomic_DNA.
DR RefSeq; WP_004846538.1; NZ_JH417492.1.
DR AlphaFoldDB; G9Y317; -.
DR PATRIC; fig|1002364.3.peg.864; -.
DR HOGENOM; CLU_005316_0_4_6; -.
DR Proteomes; UP000005959; 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:0016434; F:rRNA (cytosine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd00620; Methyltransferase_Sun; 1.
DR Gene3D; 1.10.287.730; Helix hairpin bin; 1.
DR Gene3D; 1.10.940.10; NusB-like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_01856; 16SrRNA_methyltr_B; 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; IPR023541; rRNA_ssu_MeTfrase_B_ent.
DR InterPro; IPR048019; RsmB-like_N.
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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01856};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01856};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01856};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01856};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01856};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01856}.
FT DOMAIN 165..430
FT /note="SAM-dependent MTase RsmB/NOP-type"
FT /evidence="ECO:0000259|PROSITE:PS51686"
FT ACT_SITE 376
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 255..261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 278
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 304
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
FT BINDING 323
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01856,
FT ECO:0000256|PROSITE-ProRule:PRU01023"
SQ SEQUENCE 430 AA; 48669 MW; 26145DBD470F877B CRC64;
MKNTPYNLRA IAAKALGSVL DQGQSLSTVL PALSKEVSEK DRALLQELCF GVLRVLPQLE
WYIQQLMAKV LTGKQRPLHY LIMVGIYQLV YTRIPPHAAL AETVNGAVAL KRPQLKGLIN
GVLRQFQRQE DQLKERAQNN ECRFLHPSWL LKRLQQAYPQ QWESIVDANN QRPPMWLRVN
RLHHTRDEYL ALLAKAEINA FAHPQFPDAI CLEEASPVGR LPGFEQGWVT VQDASAQHCV
DLLDPQNGEQ ILDLCCAPGG KTTHILEAAP KAHVLAVDVD ENRLKRVKEN LHRLQQQAEV
KCGDGRYPEN WCGDRQFDRI LLDAPCSATG VIRRHPDIKW LRRDRDIAEL AALQKEIIEA
IWPHLKSGGV MVYATCSVLP EENAQQMREF LARHPEAQLV TTGDQENPGQ QHLPHAQDGD
GFFYAKLIKA
//
