RSMH_SHEVD
ID RSMH_SHEVD Reviewed; 313 AA.
AC Q9F1N8; D4ZDV1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase H {ECO:0000255|HAMAP-Rule:MF_01007};
DE EC=2.1.1.199 {ECO:0000255|HAMAP-Rule:MF_01007};
DE AltName: Full=16S rRNA m(4)C1402 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01007};
DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH {ECO:0000255|HAMAP-Rule:MF_01007};
GN Name=rsmH {ECO:0000255|HAMAP-Rule:MF_01007}; Synonyms=mraW;
GN OrderedLocusNames=SVI_4041;
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12153713; DOI=10.1093/oxfordjournals.jbchem.a003208;
RA Ishii A., Nakasone K., Sato T., Wachi M., Sugai M., Nagai K., Kato C.;
RT "Isolation and characterization of the dcw cluster from the piezophilic
RT deep-sea bacterium Shewanella violacea.";
RL J. Biochem. 132:183-188(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12;
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
CC -!- FUNCTION: Specifically methylates the N4 position of cytidine in
CC position 1402 (C1402) of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_01007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42928, Rhea:RHEA-COMP:10286, Rhea:RHEA-COMP:10287,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74506, ChEBI:CHEBI:82748; EC=2.1.1.199;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01007};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01007}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000255|HAMAP-Rule:MF_01007}.
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DR EMBL; AB052554; BAB19194.1; -; Genomic_DNA.
DR EMBL; AP011177; BAJ04012.1; -; Genomic_DNA.
DR RefSeq; WP_013053303.1; NC_014012.1.
DR AlphaFoldDB; Q9F1N8; -.
DR SMR; Q9F1N8; -.
DR STRING; 637905.SVI_4041; -.
DR EnsemblBacteria; BAJ04012; BAJ04012; SVI_4041.
DR KEGG; svo:SVI_4041; -.
DR eggNOG; COG0275; Bacteria.
DR HOGENOM; CLU_038422_2_0_6; -.
DR OMA; NPAKRTF; -.
DR OrthoDB; 1272633at2; -.
DR Proteomes; UP000002350; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071424; F:rRNA (cytosine-N4-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.150.170; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01007; 16SrRNA_methyltr_H; 1.
DR InterPro; IPR002903; RsmH.
DR InterPro; IPR023397; SAM-dep_MeTrfase_MraW_recog.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11265; PTHR11265; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR PIRSF; PIRSF004486; MraW; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF81799; SSF81799; 1.
DR TIGRFAMs; TIGR00006; TIGR00006; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..313
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000108701"
FT BINDING 35..37
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 102
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 109
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ SEQUENCE 313 AA; 35024 MW; EEF017A946AC43A1 CRC64;
MSQEFSHLSV LLTETVAGLN IKPDGIYIDG TFGRGGHSRE VLKHLGDNGR LIAIDRDPQA
IIAAEQFADD ARFSIVHGGF GQLADYVEDL GLKGKVDGVL LDFGVSSPQL DDAERGFSFL
RDGPLDMRMD NSQGQTAAEW IARTEIEDMA WVFKTYGEEK NSRHIARCIA ADRDKTPFLR
TKELADLIAR ICKSKERNKH PATRVFQAIR IYINSELEQI DQALEGALKV LAPQGRLSVI
SFHSLEDRIV KRFIRRHSQG MSVPHGLPIT EAEINKTRLL KAVGKATKPS TEEVEMNKRS
RSSVLRVAER LEY
