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RSMH_NEOSM
ID   RSMH_NEOSM              Reviewed;         296 AA.
AC   Q2GCL1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=NSE_0921;
OS   Neorickettsia sennetsu (strain ATCC VR-367 / Miyayama) (Ehrlichia
OS   sennetsu).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Neorickettsia.
OX   NCBI_TaxID=222891;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-367 / Miyayama;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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; CP000237; ABD46126.1; -; Genomic_DNA.
DR   RefSeq; WP_011452291.1; NC_007798.1.
DR   AlphaFoldDB; Q2GCL1; -.
DR   SMR; Q2GCL1; -.
DR   STRING; 222891.NSE_0921; -.
DR   EnsemblBacteria; ABD46126; ABD46126; NSE_0921.
DR   KEGG; nse:NSE_0921; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_1_1_5; -.
DR   OMA; NPAKRTF; -.
DR   OrthoDB; 1272633at2; -.
DR   Proteomes; UP000001942; 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..296
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000387007"
FT   BINDING         41..43
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         59
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         86
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         104
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   296 AA;  33161 MW;  38D7F05A2E8B2FD2 CRC64;
     MSVTGGSKDE ILHKPVLLSE ALKFLAPKNG GVYVDATFGA GGYTRAILSS VDCFVYAIDR
     DETVRRFFQV IENDFPKRTN FINGNFVDIG SLLGEVKVDG IVFDLGVSTM QLKVADRGFS
     FLHEGPLDMR MDRSTLLTAE TVVNSYTEVK IASIIYQFGE ERMSRKIAHA IVNARRKKRI
     TTTSSLAEIV RSCFPKRYYK IDPATKTFQA LRIFINDELG ALECGLRTAL TMLKVGSRAV
     VVSFHSLEDR IVKHLFRSVH GNGFNLLTKK IVVPSRDEVR ENPSSRSARM RVIEKV
 
 
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