RSMA_METJA
ID RSMA_METJA Reviewed; 275 AA.
AC Q58435;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607};
DE EC=2.1.1.- {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}; OrderedLocusNames=MJ1029;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND FUNCTION.
RX PubMed=19520088; DOI=10.1016/j.jmb.2009.06.015;
RA Pulicherla N., Pogorzala L.A., Xu Z., O'Farrell H.C., Musayev F.N.,
RA Scarsdale J.N., Sia E.A., Culver G.M., Rife J.P.;
RT "Structural and functional divergence within the Dim1/KsgA family of rRNA
RT methyltransferases.";
RL J. Mol. Biol. 391:884-893(2009).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH AMP;
RP S-ADENOSYL-L-HOMOCYSTEINE; S-ADENOSYL-L-METHIONINE AND ADENOSINE, AND
RP FUNCTION.
RX PubMed=20163168; DOI=10.1021/bi901875x;
RA O'Farrell H.C., Musayev F.N., Scarsdale J.N., Rife J.P.;
RT "Binding of adenosine-based ligands to the MjDim1 rRNA methyltransferase:
RT implications for reaction mechanism and drug design.";
RL Biochemistry 49:2697-2704(2010).
CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines in the loop
CC of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle.
CC May play a critical role in biogenesis of 30S subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00607, ECO:0000269|PubMed:19520088,
CC ECO:0000269|PubMed:20163168}.
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}.
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DR EMBL; L77117; AAB99033.1; -; Genomic_DNA.
DR PIR; D64428; D64428.
DR RefSeq; WP_010870542.1; NC_000909.1.
DR PDB; 3FYC; X-ray; 2.15 A; A/B=10-272.
DR PDB; 3FYD; X-ray; 1.75 A; A=10-272.
DR PDB; 3GRR; X-ray; 1.80 A; A=1-275.
DR PDB; 3GRU; X-ray; 1.60 A; A=1-275.
DR PDB; 3GRV; X-ray; 1.90 A; A=1-275.
DR PDB; 3GRY; X-ray; 2.20 A; A=1-275.
DR PDBsum; 3FYC; -.
DR PDBsum; 3FYD; -.
DR PDBsum; 3GRR; -.
DR PDBsum; 3GRU; -.
DR PDBsum; 3GRV; -.
DR PDBsum; 3GRY; -.
DR AlphaFoldDB; Q58435; -.
DR SMR; Q58435; -.
DR STRING; 243232.MJ_1029; -.
DR EnsemblBacteria; AAB99033; AAB99033; MJ_1029.
DR GeneID; 1451926; -.
DR KEGG; mja:MJ_1029; -.
DR eggNOG; arCOG04131; Archaea.
DR HOGENOM; CLU_041220_0_2_2; -.
DR InParanoid; Q58435; -.
DR OMA; KEEEPYF; -.
DR OrthoDB; 99734at2157; -.
DR PhylomeDB; Q58435; -.
DR EvolutionaryTrace; Q58435; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IBA:GO_Central.
DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..275
FT /note="Probable ribosomal RNA small subunit
FT methyltransferase A"
FT /id="PRO_0000101656"
FT BINDING 13
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00607"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 101
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:3GRU"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:3GRU"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:3GRU"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3GRU"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:3GRU"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:3GRU"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:3GRU"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:3GRU"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3GRU"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:3GRU"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:3GRU"
FT TURN 204..207
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 225..236
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:3GRU"
FT HELIX 255..271
FT /evidence="ECO:0007829|PDB:3GRU"
SQ SEQUENCE 275 AA; 31771 MW; BB4DD454BD36427A CRC64;
MFKPKKKLGQ CFLIDKNFVN KAVESANLTK DDVVLEIGLG KGILTEELAK NAKKVYVIEI
DKSLEPYANK LKELYNNIEI IWGDALKVDL NKLDFNKVVA NLPYQISSPI TFKLIKRGFD
LAVLMYQYEF AKRMVAKEGT KDYGRLSVAV QSRADVEIVA KVPPSAFYPK PKVYSAIVKI
KPNKGKYHIE NENFFDDFLR AIFQHRNKSV RKALIDSSKE LNYNKDEMKK ILEDFLNTNS
EIKNLINEKV FKLSVKDIVN LSNEFYRFLQ NRGRL
