(data stored in ACNUC7421 zone)

SWISSPROT: RSMH_PARDP

ID   RSMH_PARDP              Reviewed;         322 AA.
AC   A1AZK1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
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=Pden_0583;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) 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; CP000489; ABL68695.1; -; Genomic_DNA.
DR   RefSeq; WP_011746928.1; NC_008686.1.
DR   SMR; A1AZK1; -.
DR   STRING; 318586.Pden_0583; -.
DR   PRIDE; A1AZK1; -.
DR   EnsemblBacteria; ABL68695; ABL68695; Pden_0583.
DR   KEGG; pde:Pden_0583; -.
DR   eggNOG; ENOG4105CGJ; Bacteria.
DR   eggNOG; COG0275; LUCA.
DR   HOGENOM; HOG000049778; -.
DR   KO; K03438; -.
DR   OMA; VMRVAEK; -.
DR   BioCyc; PDEN318586:G1GW1-591-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; A1AZK1.
DR   SWISS-2DPAGE; A1AZK1.
KW   Complete proteome; Cytoplasm; Methyltransferase; Reference proteome;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    322       Ribosomal RNA small subunit
FT                                methyltransferase H.
FT                                /FTId=PRO_0000387020.
FT   REGION       33     35       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01007}.
FT   BINDING      51     51       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01007}.
FT   BINDING      78     78       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01007}.
FT   BINDING      95     95       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01007}.
FT   BINDING     102    102       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01007}.
SQ   SEQUENCE   322 AA;  34319 MW;  E646013EDF55E047 CRC64;
     MAEAPHIPVL LGPLLRAVAP VEGTWVDGTF GAGGYARGLL EQGADRVIGI DRDPAVFRMA
     EAWAGEYGDR LRLVEGTFSD LDSLAGGPVD GVVLDLGVSS MQLDQPERGF SFLRDGPLDM
     RMGGDGPTAA ELLNTAPEQV IADVLYLYGE ERASRRIAKA IVAARPLSRT GQLSDIVSAC
     LPRPKPGQSH PSTRAFQAIR IWVNDEFGQL VAGLAAAERA LRPGGKLAVV SFHSLEDRIV
     KRFMQARSNS AGGGSRYAPE AAREEPAFTL PFRRAIGPDE AELATNPRAR SALLRVGIRT
     EAPAGRVDPA ALGLPLLSER RA
//

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