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RSMH_HELHP
ID   RSMH_HELHP              Reviewed;         317 AA.
AC   Q7VGP1;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
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=HH_1279;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP77876.1; -; Genomic_DNA.
DR   RefSeq; WP_011116119.1; NC_004917.1.
DR   AlphaFoldDB; Q7VGP1; -.
DR   SMR; Q7VGP1; -.
DR   STRING; 235279.HH_1279; -.
DR   PRIDE; Q7VGP1; -.
DR   EnsemblBacteria; AAP77876; AAP77876; HH_1279.
DR   KEGG; hhe:HH_1279; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_3_0_7; -.
DR   OMA; NPAKRTF; -.
DR   OrthoDB; 1272633at2; -.
DR   Proteomes; UP000002495; 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..317
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000108636"
FT   BINDING         32..34
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         51
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         78
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         106
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   317 AA;  36003 MW;  46914B751054BE9B CRC64;
     MKHYSVLKNE MIQALDCLKE DSILIDCTLG FGGHTIGALQ AYPNIEVYAF DKDIYALNLA
     KERLKPYLQN IHFCHNAFSQ FLDIVPNVVL PRVRGIIADI GVSSMQLDET QRGFSFVSST
     LDMRMDTRAD LNATKVINTY SPIRLEEIFR IYGEVRQSKK LAEIIAYERK KKPFSSCLEL
     STLIEQHFPR VGGIHPATLA FQALRIEVND ELGELKRLLH NIELAFDEGK IASCRVGIIS
     FHSLEDRIIK QCFKQWSKSC ICAEESLRCE CGNNHAKGQI LTKKPIIPTP QEIAQNKRSR
     SAKLRIFELK SSKDKGV
 
 
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