RSME_AQUAE
ID RSME_AQUAE Reviewed; 229 AA.
AC O66552;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase E;
DE EC=2.1.1.193;
DE AltName: Full=16S rRNA m3U1498 methyltransferase;
GN Name=rsmE; OrderedLocusNames=aq_165;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- FUNCTION: Specifically methylates the N3 position of the uracil ring of
CC uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S
CC ribosomal subunit (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) +
CC N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42920, Rhea:RHEA-COMP:10283, Rhea:RHEA-COMP:10284,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74502; EC=2.1.1.193;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase RsmE family.
CC {ECO:0000305}.
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DR EMBL; AE000657; AAC06516.1; -; Genomic_DNA.
DR PIR; E70315; E70315.
DR RefSeq; NP_213112.1; NC_000918.1.
DR RefSeq; WP_010880050.1; NC_000918.1.
DR PDB; 2EGV; X-ray; 1.45 A; A/B=1-229.
DR PDB; 2EGW; X-ray; 2.80 A; A/B=1-229.
DR PDBsum; 2EGV; -.
DR PDBsum; 2EGW; -.
DR AlphaFoldDB; O66552; -.
DR SMR; O66552; -.
DR STRING; 224324.aq_165; -.
DR EnsemblBacteria; AAC06516; AAC06516; aq_165.
DR KEGG; aae:aq_165; -.
DR PATRIC; fig|224324.8.peg.141; -.
DR eggNOG; COG1385; Bacteria.
DR HOGENOM; CLU_067442_3_0_0; -.
DR InParanoid; O66552; -.
DR OMA; TQWKGER; -.
DR OrthoDB; 1490892at2; -.
DR EvolutionaryTrace; O66552; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070042; F:rRNA (uridine-N3-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR006700; rRNA_ssu_MeTrfase-E.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR30027; PTHR30027; 1.
DR Pfam; PF04452; Methyltrans_RNA; 1.
DR PIRSF; PIRSF015601; MTase_slr0722; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00046; TIGR00046; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; Reference proteome;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..229
FT /note="Ribosomal RNA small subunit methyltransferase E"
FT /id="PRO_0000176204"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2EGV"
FT HELIX 19..26
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 42..51
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:2EGV"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2EGV"
FT HELIX 113..134
FT /evidence="ECO:0007829|PDB:2EGV"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2EGW"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:2EGV"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2EGV"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2EGV"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:2EGV"
SQ SEQUENCE 229 AA; 26683 MW; 5E83FB8432B5B500 CRC64;
MHVFYSEERR GNLLILREGE VKHFRVRRIE KDEEFGVIHE GKIYVCKVRR EDKREISCEI
VEELETKLPP KDITLYQSVT VDLKTMDTIV RQATELGVLT FVPIISERSF QKEEAILKKT
EKWKRIVIEA MKQSRRPIPM EIKKPVRLSD LIPESEENII LDNFYEGVKP KDVNLEAKTY
SVVVGPEGGF SKRESQILRE KGFKSVLLEP YTLRTETAVV SIVSILMNF
