(data stored in ACNUC7421 zone)

SWISSPROT: RSMH_SHESH

ID   RSMH_SHESH              Reviewed;         314 AA.
AC   A8FQ92;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
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=Ssed_0402;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates the N4 position of cytidine in
CC       position 1402 (C1402) of 16S rRNA. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01007};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01007}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmH
CC       family. {ECO:0000255|HAMAP-Rule:MF_01007}.
DR   EMBL; CP000821; ABV35015.1; -; Genomic_DNA.
DR   SMR; A8FQ92; -.
DR   STRING; 425104.Ssed_0402; -.
DR   EnsemblBacteria; ABV35015; ABV35015; Ssed_0402.
DR   KEGG; sse:Ssed_0402; -.
DR   eggNOG; ENOG4105CGJ; Bacteria.
DR   eggNOG; COG0275; LUCA.
DR   HOGENOM; HOG000049777; -.
DR   KO; K03438; -.
DR   OMA; VMRVAEK; -.
DR   Proteomes; UP000002015; 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; A8FQ92.
DR   SWISS-2DPAGE; A8FQ92.
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    314       Ribosomal RNA small subunit
FT                                methyltransferase H.
FT                                /FTId=PRO_0000387121.
FT   REGION       36     38       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01007}.
FT   BINDING      56     56       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01007}.
FT   BINDING      81     81       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01007}.
FT   BINDING     103    103       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01007}.
FT   BINDING     110    110       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01007}.
SQ   SEQUENCE   314 AA;  35147 MW;  9223BEAE4519CA62 CRC64;
     MMSQEFAHLS VLLTETVAGL NIKEDGIYID GTFGRGGHSR EVLKHLGENG RLIAIDRDPQ
     AIAAAEQFAD DARFSIVHGG FGQLATYVED LGLKGKIDGV LLDFGVSSPQ LDDAERGFSF
     LRDGPLDMRM DNSQGETAAD WIARAEIEDM AWVFKTYGEE KNSRHIARCI AADREKTPFL
     RTKELADLIA RISKNKERNK HPATRVFQAI RIYINSELEQ IDQALEGALS VLAPHGRLSV
     ISFHSLEDRM VKRFIRRHCQ GESVPHGLPI TEAEINKSRL LKGIGKAIKP SEEEVERNTR
     ARSSVLRIAE RLEY
//

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