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Database: UniProt
Entry: G5GDT9_9BACT
LinkDB: G5GDT9_9BACT
Original site: G5GDT9_9BACT 
ID   G5GDT9_9BACT            Unreviewed;       243 AA.
AC   G5GDT9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Ribosomal RNA small subunit methyltransferase E {ECO:0000256|PIRNR:PIRNR015601};
DE            EC=2.1.1.193 {ECO:0000256|PIRNR:PIRNR015601};
GN   ORFNames=HMPREF9332_01741 {ECO:0000313|EMBL:EHG21222.1};
OS   Alloprevotella rava F0323.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Alloprevotella.
OX   NCBI_TaxID=679199 {ECO:0000313|EMBL:EHG21222.1, ECO:0000313|Proteomes:UP000015993};
RN   [1] {ECO:0000313|EMBL:EHG21222.1, ECO:0000313|Proteomes:UP000015993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0323 {ECO:0000313|EMBL:EHG21222.1,
RC   ECO:0000313|Proteomes:UP000015993};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA   Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. oral taxon 302 str. F0323.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHG21222.1}.
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DR   EMBL; ACZK01000032; EHG21222.1; -; Genomic_DNA.
DR   RefSeq; WP_009348273.1; NZ_JH376834.1.
DR   AlphaFoldDB; G5GDT9; -.
DR   STRING; 679199.HMPREF9332_01741; -.
DR   PATRIC; fig|679199.3.peg.1939; -.
DR   eggNOG; COG1385; Bacteria.
DR   HOGENOM; CLU_067442_4_1_10; -.
DR   OrthoDB; 9815641at2; -.
DR   Proteomes; UP000015993; Unassembled WGS sequence.
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:UP000015993};
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          18..65
FT                   /note="Ribosomal RNA small subunit methyltransferase E PUA-
FT                   like"
FT                   /evidence="ECO:0000259|Pfam:PF20260"
FT   DOMAIN          77..237
FT                   /note="Ribosomal RNA small subunit methyltransferase E
FT                   methyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04452"
SQ   SEQUENCE   243 AA;  27556 MW;  FC1FDEE694659E79 CRC64;
     MKEVHLFYAP DIEQTQELPT EEAIHAIRVL RLKEGQQLLI TDGKGTFYDA ELSLASQKHC
     KIKIINAYPE KKLWKGSIHL VVAPTKSIDR IEWLVEKATE IGVDKISFLN CDNSERHIVK
     SERIEKIVIA AMKQSHKATK PTIEEMMNFD KFIAKPFQGQ RFIAHCYLES DISESTEKSF
     LGQIVKTEEG TQVLIGPEGD FSIDEVRKAI KAGFQSISLG ECRLRTETAA LVAVHLMYLA
     KRL
//
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