位置:首页 > 蛋白库 > RSMA_STRA1
RSMA_STRA1
ID   RSMA_STRA1              Reviewed;         290 AA.
AC   Q3JZA5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607};
DE            EC=2.1.1.182 {ECO:0000255|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000255|HAMAP-Rule:MF_00607};
DE   AltName: Full=16S rRNA dimethylase {ECO:0000255|HAMAP-Rule:MF_00607};
DE   AltName: Full=S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607};
GN   Name=rsmA {ECO:0000255|HAMAP-Rule:MF_00607};
GN   Synonyms=ksgA {ECO:0000255|HAMAP-Rule:MF_00607};
GN   OrderedLocusNames=SAK_1801;
OS   Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS   SS700).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=205921;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27591 / A909 / CDC SS700;
RX   PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA   Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA   Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA   Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA   Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA   Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA   Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA   Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA   Wessels M.R., Rappuoli R., Fraser C.M.;
RT   "Genome analysis of multiple pathogenic isolates of Streptococcus
RT   agalactiae: implications for the microbial 'pan-genome'.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
CC   -!- FUNCTION: Specifically dimethylates two adjacent adenosines (A1518 and
CC       A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA
CC       in the 30S particle. May play a critical role in biogenesis of 30S
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00607}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-
CC         methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-
CC         dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:19609, Rhea:RHEA-COMP:10232, Rhea:RHEA-COMP:10233,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74411, ChEBI:CHEBI:74493; EC=2.1.1.182;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00607};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00607}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. rRNA adenine N(6)-methyltransferase family. RsmA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00607}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000114; ABA44983.1; -; Genomic_DNA.
DR   RefSeq; WP_001216821.1; NC_007432.1.
DR   AlphaFoldDB; Q3JZA5; -.
DR   SMR; Q3JZA5; -.
DR   KEGG; sak:SAK_1801; -.
DR   HOGENOM; CLU_041220_0_0_9; -.
DR   OMA; KEEEPYF; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052908; F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.100; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00607; 16SrRNA_methyltr_A; 1.
DR   InterPro; IPR001737; KsgA/Erm.
DR   InterPro; IPR023165; rRNA_Ade_diMease-like_C.
DR   InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS.
DR   InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N.
DR   InterPro; IPR011530; rRNA_adenine_dimethylase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR11727; PTHR11727; 1.
DR   Pfam; PF00398; RrnaAD; 1.
DR   SMART; SM00650; rADc; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00755; ksgA; 1.
DR   PROSITE; PS01131; RRNA_A_DIMETH; 1.
DR   PROSITE; PS51689; SAM_RNA_A_N6_MT; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..290
FT                   /note="Ribosomal RNA small subunit methyltransferase A"
FT                   /id="PRO_0000257356"
FT   BINDING         27
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         29
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
SQ   SEQUENCE   290 AA;  32513 MW;  B5EE50038BB9BBC8 CRC64;
     MRIADKTVTR AILERHGFTF KKSFGQNFLT DTNILQKIVD TAEIDKGVNV IEIGPGIGAL
     TEFLAENAAE VMAFEIDDRL IPILADTLAR FDNVQVVNQD ILKADLQTQI QAFKNPDLPI
     KVVANLPYYI TTPILMHLIE SKIPFAEFVV MMQKEVADRI SAMPNTKAYG SLSIAVQYYM
     TAKVSFIVPR TVFVPAPNVD SVILKMVRRD QPVVSVQDED FFFRVSKVAF VHRRKTLWNN
     LTSHFGKSED TKAKLEKALE IAKIKPSIRG EALSIPDFAS LADALKEVEI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024