ID   RSMH_FLAPJ              Reviewed;         291 AA.
AC   A6H1A2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=FP2064;
OS   Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS   JIP02/86).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=402612;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX   PubMed=17592475; DOI=10.1038/nbt1313;
RA   Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA   Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA   Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT   "Complete genome sequence of the fish pathogen Flavobacterium
RT   psychrophilum.";
RL   Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL44126.1; -; Genomic_DNA.
DR   RefSeq; YP_001296928.1; NC_009613.3.
DR   AlphaFoldDB; A6H1A2; -.
DR   SMR; A6H1A2; -.
DR   STRING; 402612.FP2064; -.
DR   EnsemblBacteria; CAL44126; CAL44126; FP2064.
DR   KEGG; fps:FP2064; -.
DR   PATRIC; fig|402612.5.peg.2091; -.
DR   eggNOG; COG0275; Bacteria.
DR   HOGENOM; CLU_038422_2_0_10; -.
DR   OMA; NPAKRTF; -.
DR   Proteomes; UP000006394; 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..291
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000386895"
FT   BINDING         25..27
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         88
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   291 AA;  33464 MW;  82FDB31A67F698C7 CRC64;
     MLKETVDGLN IKPDGVYVDV TFGGGGHSKE ILSRLGPEGK LFGFDQDEDA WENALPDERF
     TLIQENFRYI KRFLRFNGIK KVDGILADLG VSSHQFDVPE RGFSTRFDAE LDMRMSKKND
     LTAFNIVNEY DETNLRRIFA EYGELGNALA IARAIIEARE KEKIVNTEDL KQVLARFLPN
     NKAHKILAQI YQSIRIEVNQ EMDVLKEFLE QSLEVLDQGG RLSVISYHSL EDRLVKRFMK
     NGLFEGEPEK DFFGRFEVPF KLIGKMIIPS NQEIKINNRA RSAKLRIAEK K