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Database: UniProt
Entry: RSMH2_LACP7
LinkDB: RSMH2_LACP7
Original site: RSMH2_LACP7 
ID   RSMH2_LACP7             Reviewed;         317 AA.
AC   A9KM86;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase H 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01007};
DE   AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH 2 {ECO:0000255|HAMAP-Rule:MF_01007};
GN   Name=rsmH2 {ECO:0000255|HAMAP-Rule:MF_01007}; Synonyms=mraW2;
GN   OrderedLocusNames=Cphy_2479;
OS   Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS   (Clostridium phytofermentans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=357809;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA   Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA   LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT   "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000885; ABX42840.1; -; Genomic_DNA.
DR   RefSeq; WP_012200493.1; NC_010001.1.
DR   AlphaFoldDB; A9KM86; -.
DR   SMR; A9KM86; -.
DR   STRING; 357809.Cphy_2479; -.
DR   KEGG; cpy:Cphy_2479; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_2_0_9; -.
DR   OrthoDB; 9806637at2; -.
DR   Proteomes; UP000000370; 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; Putative methyltransferase TM0872, insert domain; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00006; 16S rRNA (cytosine(1402)-N(4))-methyltransferase RsmH; 1.
DR   PANTHER; PTHR11265:SF0; 12S RRNA N4-METHYLCYTIDINE METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR11265; S-ADENOSYL-METHYLTRANSFERASE MRAW; 1.
DR   Pfam; PF01795; Methyltransf_5; 1.
DR   PIRSF; PIRSF004486; MraW; 1.
DR   SUPFAM; SSF81799; Putative methyltransferase TM0872, insert domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 2"
FT                   /id="PRO_0000386824"
FT   BINDING         38..40
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         58
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         85
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"
FT   BINDING         113
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   317 AA;  36189 MW;  52F91E1F74069443 CRC64;
     MSLEEKEFKH ISVLLQETID SLNIKPDGIY VDGTLGGGGH AYEVLKRLSP KGRYIGIDQD
     EDAIAAAGKR LSEFSDQVTI VRSNYCNMKQ VLKDLGIDKV DGILLDLGVS SYQLDTPERG
     FSYRENAPLD MRMDNRNSLT ARDIVNEYSE QEIYRIIRDY GEDKFAKNIA KHIVRMRSEK
     PLETTDELTE AIKAAIPMKI RMNTGHPAKK TFQAIRIELN HELEVLTNTL EDMIDLLKED
     GRLSIITFHS LEDRIVKAAF RKNENPCVCP PNFPVCVCNR KPKGIHITKK PILPSEQELE
     YNKRSKSAKL RVFEKHE
//
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