ID   RSMH_MAGMM              Reviewed;         313 AA.
AC   A0L5N9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Mmc1_0761;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(2009).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000471; ABK43282.1; -; Genomic_DNA.
DR   RefSeq; WP_011712442.1; NC_008576.1.
DR   AlphaFoldDB; A0L5N9; -.
DR   SMR; A0L5N9; -.
DR   STRING; 156889.Mmc1_0761; -.
DR   EnsemblBacteria; ABK43282; ABK43282; Mmc1_0761.
DR   KEGG; mgm:Mmc1_0761; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_1_1_5; -.
DR   OMA; NPAKRTF; -.
DR   OrthoDB; 1272633at2; -.
DR   Proteomes; UP000002586; 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_0000386966"
FT   REGION          282..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         33..35
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         53
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         101
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   313 AA;  34026 MW;  D7DE3DDBE8BE5D17 CRC64;
     MSFQHTTVLL QETVAALAPQ RGGCYLDGTF GGGGHSRLLL EQCAPTGRVI GLDRDADAIA
     NGQALVAQMA GRLTLVKAPF AQVAEVLQQL EIAALDGAML DLGVSSHQLD TAERGFSFIR
     SGPLDMRMDG DSTTPTAAAL LNTLDADALA DIFFHYGEER HARRIARMVV KVRQQHPFTT
     TTDLAERIAH MTPGYSRIHP ATRVFQGLRI AVNEELQQLE QALSVLIGLL KPGGHLAVIS
     FHSLEDRIVK RLFRDAAKPP EDPVLRGLPI AQAQRPKATL KLVHNKPLTP SEAEIEQNPR
     ARSAKLRVAQ KLA