ID   RSMH_BIFAS              Reviewed;         353 AA.
AC   C6AJH2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=Balat_1206;
OS   Bifidobacterium animalis subsp. lactis (strain DSM 10140 / JCM 10602 / LMG
OS   18314).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=555970;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10140 / JCM 10602 / LMG 18314;
RX   PubMed=19376856; DOI=10.1128/jb.00155-09;
RA   Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M.,
RA   Horvath P., Coute-Monvoisin A.-C., Leyer G., Rendulic S., Steele J.L.,
RA   Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A.,
RA   Roberts R.F.;
RT   "Comparison of the complete genome sequences of Bifidobacterium animalis
RT   subsp. lactis DSM 10140 and Bl-04.";
RL   J. Bacteriol. 191:4144-4151(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; CP001606; ACS48129.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6AJH2; -.
DR   SMR; C6AJH2; -.
DR   KEGG; blt:Balat_1206; -.
DR   HOGENOM; CLU_038422_0_0_11; -.
DR   OMA; NPAKRTF; -.
DR   BioCyc; BANI555970:G1GVE-1227-MON; -.
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; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..353
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000386748"
FT   REGION          334..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39..41
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         90
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"
FT   BINDING         115
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   353 AA;  38853 MW;  03A6CA1DA6AEA4BC CRC64;
     MTDFSQIHKP VLLQECVDLV TPALHASDSV AVDCTLGLAG HTIAFLKAAP NATVIGIDRD
     EEALDKATAR IAQEGLSARF VPVHAAFDQF DEVLRAQGVS RVQAVFMDLG LSSLQIDERE
     RGFSYAHDAP LDMRMDTSQA LTAREILATY DADRLAHIFK EYGEERFSKP IAKRIVQQRQ
     SSPLETSSQL TALVDAVIPA ARRGSGNPAK RVFQALRIEV NGELDKLRRT LPQIGLHLAV
     GGRLVVESYH SLEDRTVKNF MAQGLRVDAP ADMPVIPPDM QPFFKALTKG AVKADAGEIA
     YNPRSASVRL RAVELTRPLP QRWVHAFELE SQGSEDGVRG AHGHRRRTQA RRG