ID L0RX03_MYCC1 Unreviewed; 300 AA.
AC L0RX03;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase H {ECO:0000256|HAMAP-Rule:MF_01007};
DE EC=2.1.1.199 {ECO:0000256|HAMAP-Rule:MF_01007};
DE AltName: Full=16S rRNA m(4)C1402 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01007};
DE AltName: Full=rRNA (cytosine-N(4)-)-methyltransferase RsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN Name=MCYN0389 {ECO:0000313|EMBL:CCP24121.1};
GN Synonyms=rsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN OrderedLocusNames=MCYN_0389 {ECO:0000313|EMBL:CCP24121.1};
OS Mycoplasmopsis cynos (strain C142) (Mycoplasma cynos).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=1246955 {ECO:0000313|EMBL:CCP24121.1, ECO:0000313|Proteomes:UP000010466};
RN [1] {ECO:0000313|Proteomes:UP000010466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C142 {ECO:0000313|Proteomes:UP000010466};
RX PubMed=23409256; DOI=10.1128/genomeA.00196-12;
RA Walker C.A., Mannering S.A., Shields S., Blake D.P., Brownlie J.;
RT "Complete genome sequence of Mycoplasma cynos strain C142.";
RL Genome Announc. 1:E00196-E00196(2013).
CC -!- FUNCTION: Specifically methylates the N4 position of cytidine in
CC position 1402 (C1402) of 16S rRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01007};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01007}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH family.
CC {ECO:0000256|ARBA:ARBA00010396, ECO:0000256|HAMAP-Rule:MF_01007}.
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DR EMBL; HF559394; CCP24121.1; -; Genomic_DNA.
DR RefSeq; WP_015287248.1; NC_019949.1.
DR AlphaFoldDB; L0RX03; -.
DR STRING; 1246955.MCYN_0389; -.
DR GeneID; 74931994; -.
DR KEGG; mcy:MCYN_0389; -.
DR PATRIC; fig|1246955.3.peg.353; -.
DR eggNOG; COG0275; Bacteria.
DR HOGENOM; CLU_038422_2_0_14; -.
DR OrthoDB; 9806637at2; -.
DR Proteomes; UP000010466; 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; Putative methyltransferase TM0872, insert domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR00006; 16S rRNA (cytosine(1402)-N(4))-methyltransferase RsmH; 1.
DR PANTHER; PTHR11265:SF0; 12S RRNA N4-METHYLCYTIDINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR11265; S-ADENOSYL-METHYLTRANSFERASE MRAW; 1.
DR Pfam; PF01795; Methyltransf_5; 1.
DR PIRSF; PIRSF004486; MraW; 1.
DR SUPFAM; SSF81799; Putative methyltransferase TM0872, insert domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01007};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01007}; Reference proteome {ECO:0000313|Proteomes:UP000010466};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_01007};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01007};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01007}.
FT BINDING 33..35
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 52
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 79
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01007"
SQ SEQUENCE 300 AA; 34163 MW; A64A865492CAD9C2 CRC64;
MEKLHYSVLL NETIDALNIK ENGIYVDLTL GMGGHSAKIL EKLKTGHLFA FDKDDYALKV
ADQKLSKISK NYTLIKSDFQ NIKSELKKKG VNKVDGIIAD LGFSSPQVDT PERGFSYNKD
AKLDMRMDQQ QDFSAYDLIN TYSESKLNQI LLDYADVKLH YKVAKAIVKN RPITNTLELV
EIIKSVYPAA LLRVKNLAKP VFQAIRIEVN NELDSLAKML NDAVEMLSLN SSLCIITFHS
IEDRIVKNFF KNLTKNDVPD KMPIQVKKMY QTKQLLPSLC EINENKRSKS AKLRILKKCL
//
