(data stored in ACNUC10821 zone)

SWISSPROT: C8U1F4_ECO10

ID   C8U1F4_ECO10            Unreviewed;       313 AA.
AC   C8U1F4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 54.
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=mraW {ECO:0000313|EMBL:BAI28962.1};
GN   Synonyms=rsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN   OrderedLocusNames=ECO103_0084 {ECO:0000313|EMBL:BAI28962.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28962.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28962.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Specifically methylates the N4 position of cytidine in
CC       position 1402 (C1402) of 16S rRNA. {ECO:0000256|HAMAP-
CC       Rule:MF_01007}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine =
CC         H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42928, Rhea:RHEA-COMP:10286,
CC         Rhea:RHEA-COMP:10287, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74506, ChEBI:CHEBI:82748;
CC         EC=2.1.1.199; 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
CC       family. {ECO:0000256|HAMAP-Rule:MF_01007}.
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DR   EMBL; AP010958; BAI28962.1; -; Genomic_DNA.
DR   RefSeq; WP_000970479.1; NC_013353.1.
DR   SMR; C8U1F4; -.
DR   EnsemblBacteria; BAI28962; BAI28962; ECO103_0084.
DR   KEGG; eoh:ECO103_0084; -.
DR   HOGENOM; HOG000049778; -.
DR   KO; K03438; -.
DR   OMA; VMRVAEK; -.
DR   BioCyc; ECOL585395:ECO103_RS00425-MONOMER; -.
DR   Proteomes; UP000000959; 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   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.
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;
DR   PRODOM; C8U1F4.
DR   SWISS-2DPAGE; C8U1F4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01007};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01007,
KW   ECO:0000313|EMBL:BAI28962.1};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01007};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01007};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01007,
KW   ECO:0000313|EMBL:BAI28962.1}.
FT   REGION       35     37       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01007}.
FT   BINDING      55     55       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01007}.
FT   BINDING      79     79       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01007}.
FT   BINDING     101    101       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01007}.
FT   BINDING     108    108       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01007}.
SQ   SEQUENCE   313 AA;  34878 MW;  43174C907A36ECC1 CRC64;
     MMENYKHTTV LLDEAVNGLN IRPDGIYIDG TFGRGGHSRL ILSQLGEEGR LLAIDRDPQA
     IAVAKTIDDP RFSIIHGPFS ALGEYVAERD LIGKIDGILL DLGVSSPQLD DAERGFSFMR
     DGPLDMRMDP TRGQSAAEWL QTAEEADIAW VLKTYGEERF AKRIARAIVE RNREQPMTRT
     KELAEVVAAA TPVKDKFKHP ATRTFQAVRI WVNSELEEIE QALKSSLNVL APGGRLSIIS
     FHSLEDRIVK RFMRENSRGP QVPAGLPMTE EQLKKLGGRQ LRALGKLMPG EEEVAENPRA
     RSSVLRIAER TNA
//

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