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Database: UniProt
Entry: RSMH_KOSOT
LinkDB: RSMH_KOSOT
Original site: RSMH_KOSOT 
ID   RSMH_KOSOT              Reviewed;         298 AA.
AC   C5CGS3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=Kole_1911;
OS   Kosmotoga olearia (strain ATCC BAA-1733 / DSM 21960 / TBF 19.5.1).
OC   Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae;
OC   Kosmotoga.
OX   NCBI_TaxID=521045;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1733 / DSM 21960 / TBF 19.5.1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Noll K.;
RT   "Complete sequence of Thermotogales bacterium TBF 19.5.1.";
RL   Submitted (JUN-2009) 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; CP001634; ACR80592.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5CGS3; -.
DR   SMR; C5CGS3; -.
DR   STRING; 521045.Kole_1911; -.
DR   KEGG; kol:Kole_1911; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_3_0_0; -.
DR   OrthoDB; 9806637at2; -.
DR   Proteomes; UP000002382; 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   CDD; cd02440; AdoMet_MTases; 1.
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..298
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000386938"
FT   BINDING         37..39
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         57
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         91
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         105
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         112
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   298 AA;  34045 MW;  904BBC8D6D313883 CRC64;
     MQRQYNESHR SVMVQETLHY LRPTYNGVYV DGTLGEGGHT KAIIEATSGK CKVIGLDIDE
     EVLAIAEQNL KEFKENVELF NVSYVDFDLV LESLAVDKVD GFLLDIGVST YQLKAKGRGF
     SYEIDEPLDM RMSLSGSVTA ADVVNSYPEK ELARIIFEYG EEKRYARRIA RKIVERRPIQ
     TTIQLVEAIK AALPPQERFR RKRHYATRTF QAIRIEVNGE LKGLRTALEK FPNYLKPGGR
     IVIISFHSLE DRTVKHFFRE QDGVTLKILT RKPVVPSVEE VSENPRARSA KLRAAERI
//
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