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RSMH_HELMI
ID   RSMH_HELMI              Reviewed;         313 AA.
AC   B0TGB2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Helmi_19830; ORFNames=HM1_2051;
OS   Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC   Heliomicrobium.
OX   NCBI_TaxID=498761;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51547 / Ice1;
RX   PubMed=18441057; DOI=10.1128/jb.00299-08;
RA   Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA   Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA   Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA   Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT   "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT   of the Firmicutes containing the simplest photosynthetic apparatus.";
RL   J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ84608.1; -; Genomic_DNA.
DR   RefSeq; WP_012283108.1; NC_010337.2.
DR   AlphaFoldDB; B0TGB2; -.
DR   SMR; B0TGB2; -.
DR   STRING; 498761.HM1_2051; -.
DR   EnsemblBacteria; ABZ84608; ABZ84608; HM1_2051.
DR   KEGG; hmo:HM1_2051; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_2_0_9; -.
DR   OMA; NPAKRTF; -.
DR   OrthoDB; 1272633at2; -.
DR   Proteomes; UP000008550; 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_0000386927"
FT   REGION          291..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         102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   313 AA;  33923 MW;  FC2C1B989E285DBF CRC64;
     MVFHHIPVLL HQVLEVLKPR PEGVYLDGTV GGGGHSAAIL QKLSGRGRVI GLDQDPAALA
     AAGRKLASFG DRVTLVRSNF RHIGAVVAEL GLTGKIDGIL LDIGVSSHQL DEAERGFTYR
     MDAPLDMRMN PESALTASKL LNEAPEGEIA RILRDYGEER WAKRIAQFIV KRRALQPLER
     TGELVDIIRA AIPAAARQEG GHPAKRTFQA LRIAVNDELG ALEEALPAAL EALAPGGRLA
     VISFHSLEDR IVKSFFAEQA RGCLCPPDFP VCACGNRPKV KIITKKPLVG SDEEMRANPR
     AQSAKLRAAE KIR
 
 
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