(data stored in SCRATCH3701 zone)

SWISSPROT: RSMH_RICTY

ID   RSMH_RICTY              Reviewed;         306 AA.
AC   Q68WG7;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 86.
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=RT0557;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU04025.1; -; Genomic_DNA.
DR   RefSeq; WP_011191006.1; NC_006142.1.
DR   SMR; Q68WG7; -.
DR   STRING; 257363.RT0557; -.
DR   EnsemblBacteria; AAU04025; AAU04025; RT0557.
DR   KEGG; rty:RT0557; -.
DR   eggNOG; ENOG4105CGJ; Bacteria.
DR   eggNOG; COG0275; LUCA.
DR   HOGENOM; HOG000049777; -.
DR   KO; K03438; -.
DR   OMA; NPAKRTF; -.
DR   OrthoDB; 1272633at2; -.
DR   BioCyc; RTYP257363:G1G0L-563-MONOMER; -.
DR   Proteomes; UP000000604; 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; Q68WG7.
DR   SWISS-2DPAGE; Q68WG7.
KW   Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..306
FT                   /note="Ribosomal RNA small subunit methyltransferase H"
FT                   /id="PRO_0000108695"
FT   REGION          33..35
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         51
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         78
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         96
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
FT   BINDING         103
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01007"
SQ   SEQUENCE   306 AA;  34890 MW;  BA860BEDB2017994 CRC64;
     MSQYHIPVML SEVLEVLAPK GYESYLDCTF GAGGYSNAIL KSCYCSVTSL DCDPHVIERV
     EQIKQDYGER FSFIKTNFAD SFGKLKQQKF DGIVMDLGVS SMQLDIAGRG FSFLYDGPLD
     MRMSAQGFSA EEFVNTADEE EISDVIYKYG NESLSRRIAK NIIKYRKIAR IDSTRKLAEI
     VRYSIGFRKG KIDSATKTFQ AIRIYINNEL GELERFLANV KNILKKNGRL VVVSFHSLED
     RIVKNFFKEN SAKPVARSKY AKDEIKIDQN KWLEIITHKV LTPSSQEIRL NVRARSAKLR
     AAKKIL
//

If you have problems or comments...

PBIL Back to PBIL home page