RSMH_AGGAN
ID RSMH_AGGAN Reviewed; 322 AA.
AC C6AKG2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=NT05HA_0210;
OS Aggregatibacter aphrophilus (strain NJ8700) (Haemophilus aphrophilus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=634176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ8700;
RX PubMed=19447908; DOI=10.1128/jb.00447-09;
RA Di Bonaventura M.P., DeSalle R., Pop M., Nagarajan N., Figurski D.H.,
RA Fine D.H., Kaplan J.B., Planet P.J.;
RT "Complete genome sequence of Aggregatibacter (Haemophilus) aphrophilus
RT NJ8700.";
RL J. Bacteriol. 191:4693-4694(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}.
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DR EMBL; CP001607; ACS96648.1; -; Genomic_DNA.
DR RefSeq; WP_005701429.1; NZ_CP009230.1.
DR AlphaFoldDB; C6AKG2; -.
DR SMR; C6AKG2; -.
DR PRIDE; C6AKG2; -.
DR KEGG; aap:NT05HA_0210; -.
DR PATRIC; fig|634176.19.peg.198; -.
DR HOGENOM; CLU_038422_2_0_6; -.
DR OMA; NPAKRTF; -.
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..322
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000386700"
FT BINDING 40..42
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 84
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 322 AA; 35849 MW; 789C4FDAC8D87D54 CRC64;
MTHLNAFSSV EHSTVLLHET VDGLALKENG IYIDGTFGRG GHSRLILSKL SANGKLIAID
RDPKAVAEAQ KIQDPRFQIE HNTFSEILSI CEKRGLVGKI DGILLDLGVS SPQLDDAARG
FSFMKDGPLD MRMDDSKGIS AAEWLQQVSE QDLAWVLKTF GEERFAKKIA KAIVNYNKSA
VQNGSEFLTR TLQLAELIAH TVPFKDKHKH PATRSFQAIR IFINAELDEL EKVLQSALTV
LAPAGRLSVI SFHSLEDRMV KHFMRKQSQG REIPKGLPLR EDQIQRNQTL KVIGKAIMPT
DAEIAQNPRA RSAVLRVAER LN
