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Database: UniProt
Entry: Q9A2Z1_CAUVC
LinkDB: Q9A2Z1_CAUVC
Original site: Q9A2Z1_CAUVC 
ID   Q9A2Z1_CAUVC            Unreviewed;       238 AA.
AC   Q9A2Z1;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase E {ECO:0000256|ARBA:ARBA00013673, ECO:0000256|PIRNR:PIRNR015601};
DE            EC=2.1.1.193 {ECO:0000256|ARBA:ARBA00012328, ECO:0000256|PIRNR:PIRNR015601};
GN   OrderedLocusNames=CC_3415 {ECO:0000313|EMBL:AAK25377.1};
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650 {ECO:0000313|EMBL:AAK25377.1, ECO:0000313|Proteomes:UP000001816};
RN   [1] {ECO:0000313|EMBL:AAK25377.1, ECO:0000313|Proteomes:UP000001816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15 {ECO:0000313|Proteomes:UP000001816};
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R., Ohta N., Maddock J.R., Potocka I.,
RA   Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T.,
RA   Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J.,
RA   Craven M.B., Khouri H., Shetty J., Berry K., Utterback T., Tran K.,
RA   Wolf A., Vamathevan J., Ermolaeva M., White O., Salzberg S.L., Venter J.C.,
RA   Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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. {ECO:0000256|ARBA:ARBA00025699,
CC       ECO:0000256|PIRNR:PIRNR015601}.
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         Evidence={ECO:0000256|ARBA:ARBA00000792,
CC         ECO:0000256|PIRNR:PIRNR015601};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|PIRNR:PIRNR015601}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase RsmE family.
CC       {ECO:0000256|ARBA:ARBA00005528, ECO:0000256|PIRNR:PIRNR015601}.
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DR   EMBL; AE005673; AAK25377.1; -; Genomic_DNA.
DR   PIR; E87672; E87672.
DR   RefSeq; NP_422209.1; NC_002696.2.
DR   RefSeq; WP_010921244.1; NC_002696.2.
DR   AlphaFoldDB; Q9A2Z1; -.
DR   SMR; Q9A2Z1; -.
DR   STRING; 190650.CC_3415; -.
DR   EnsemblBacteria; AAK25377; AAK25377; CC_3415.
DR   KEGG; ccr:CC_3415; -.
DR   PATRIC; fig|190650.5.peg.3425; -.
DR   eggNOG; COG1385; Bacteria.
DR   HOGENOM; CLU_067442_4_0_5; -.
DR   BioCyc; CAULO:CC3415-MONOMER; -.
DR   Proteomes; UP000001816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   CDD; cd18084; RsmE-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR006700; RsmE.
DR   InterPro; IPR046886; RsmE_MTase_dom.
DR   InterPro; IPR046887; RsmE_PUA-like.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   NCBIfam; TIGR00046; RsmE family RNA methyltransferase; 1.
DR   PANTHER; PTHR30027:SF3; 16S RRNA (URACIL(1498)-N(3))-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR30027; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE E; 1.
DR   Pfam; PF04452; Methyltrans_RNA; 1.
DR   Pfam; PF20260; PUA_4; 1.
DR   PIRSF; PIRSF015601; MTase_slr0722; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR015601};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR015601};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001816};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW   ECO:0000256|PIRNR:PIRNR015601};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR015601};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR015601}.
FT   DOMAIN          21..63
FT                   /note="Ribosomal RNA small subunit methyltransferase E PUA-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF20260"
FT   DOMAIN          76..231
FT                   /note="Ribosomal RNA small subunit methyltransferase E
FT                   methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04452"
SQ   SEQUENCE   238 AA;  25873 MW;  5C7FF6059FECA5C1 CRC64;
     MIRLFVPNDL SAGAGVVPTV DQSRYLTSVM RLSVGAELLL FNGRDGEWRA TLVEATKRGC
     LLKAEEQTRP MTLGPDLDLI VAMVKRGRVE TIVEKAAELG ARRVRLTITR RTNVDFVKLG
     RLDAIAMEAA EQTGRLDVPE VADPEKLDKI LDAWDPARRL VFCDEGGDAR PMIEALSGTT
     GPAAILIGPE GGFAPEERER LRGLAFVTPV SLGPRILRAD TAAISAMTLW QAAAGDWR
//
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