(data stored in ACNUC7421 zone)

SWISSPROT: A4ATM4_MARSH

ID   A4ATM4_MARSH            Unreviewed;       297 AA.
AC   A4ATM4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=rsmH {ECO:0000256|HAMAP-Rule:MF_01007};
GN   OrderedLocusNames=FB2170_16956 {ECO:0000313|EMBL:EAR00794.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00794.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00794.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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; CP002157; EAR00794.1; -; Genomic_DNA.
DR   RefSeq; WP_013304597.1; NC_014472.1.
DR   STRING; 313603.FB2170_16956; -.
DR   EnsemblBacteria; EAR00794; EAR00794; FB2170_16956.
DR   KEGG; fbc:FB2170_16956; -.
DR   eggNOG; ENOG4105CGJ; Bacteria.
DR   eggNOG; COG0275; LUCA.
DR   HOGENOM; HOG000049777; -.
DR   KO; K03438; -.
DR   OMA; VMRVAEK; -.
DR   OrthoDB; 1272633at2; -.
DR   BioCyc; MSP313603:G1GNS-169-MONOMER; -.
DR   Proteomes; UP000001602; 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; A4ATM4.
DR   SWISS-2DPAGE; A4ATM4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01007};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01007,
KW   ECO:0000313|EMBL:EAR00794.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
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:EAR00794.1}.
FT   REGION       31     33       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01007}.
FT   BINDING      51     51       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01007}.
FT   BINDING      73     73       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01007}.
FT   BINDING      94     94       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01007}.
FT   BINDING     101    101       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01007}.
SQ   SEQUENCE   297 AA;  34004 MW;  FC1944CA5CCD001A CRC64;
     MYHNPVLLKE SVEGLDVKKD GVYVDVTFGG GGHSKEILKR LGPKGRLLAF DQDEDALDNK
     LGDERFTLIN ENFRYIRQFL KFYGIRKVDG ILADFGVSSH QFDKAERGFS TRFDADLDMR
     MSKKNSVSAY DVVNSYEFND LRKVLFQYGD LRNANAMANK IITSREEAPI KTSAQLKEVL
     RQFLPKHKEH KILAQIYQAI RIEVNQEIQV IKELLEQVPE LLNLGGRLSV ISYHSLEDRL
     VKRFIRAGLF EGEPEKDFYG NIDVPLKKVG GLIVPSREET ALNNRARSAK LRIAERI
//

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