RSMH_CORA7
ID RSMH_CORA7 Reviewed; 347 AA.
AC C3PHG4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=cauri_1675;
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=548476;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1;
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
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; CP001601; ACP33268.1; -; Genomic_DNA.
DR RefSeq; WP_010190538.1; NZ_ACLH01000088.1.
DR AlphaFoldDB; C3PHG4; -.
DR SMR; C3PHG4; -.
DR STRING; 548476.cauri_1675; -.
DR PRIDE; C3PHG4; -.
DR EnsemblBacteria; ACP33268; ACP33268; cauri_1675.
DR GeneID; 31924304; -.
DR KEGG; car:cauri_1675; -.
DR eggNOG; COG0275; Bacteria.
DR HOGENOM; CLU_038422_0_0_11; -.
DR OMA; NPAKRTF; -.
DR OrthoDB; 1272633at2; -.
DR Proteomes; UP000002077; 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..347
FT /note="Ribosomal RNA small subunit methyltransferase H"
FT /id="PRO_0000386827"
FT BINDING 50..52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 125
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT BINDING 132
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ SEQUENCE 347 AA; 37477 MW; 621CD89F92EE658B CRC64;
MEHDGTINYD VSENHGHVPV MRARMAQLLA PAIEAAGENA VIVDGTLGAG GHSEYFLTTF
PSVRIIGVDR DSASLSSASR RLSPFADRFV GVNARFDEVG SAIAEGESEV FSIAREHGIA
GALFDLGVSS MQLDQVDRGF AYKTDAPLDM RMDPRQGMTA ADILNTYSHG DLARILKTYG
DERFAGKIAS AVLREREKEP FGNSARLVDL LYATIPAATR RTGGHPAKRT FQALRVEVNR
ELEAIEQVIP VITDALSIGG RAVFMSYQSL EDRIVKHAFT KLSTSTTPAG LPMDLPGTAA
HYSVVTRGAE KASQEEIAEN PRAASVRVRA LERLEGTPSF HEPGGRP
