ID A0A2P6TXS0_CHLSO Unreviewed; 323 AA.
AC A0A2P6TXS0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=16S rRNA (uracil(1498)-N(3))-methyltransferase {ECO:0000256|ARBA:ARBA00012328};
DE EC=2.1.1.193 {ECO:0000256|ARBA:ARBA00012328};
GN ORFNames=C2E21_2301 {ECO:0000313|EMBL:PRW58851.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW58851.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW58851.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
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 -!- 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the RNA methyltransferase RsmE family.
CC {ECO:0000256|ARBA:ARBA00005528}.
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:PRW58851.1}.
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DR EMBL; LHPG02000004; PRW58851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6TXS0; -.
DR STRING; 3076.A0A2P6TXS0; -.
DR OrthoDB; 324904at2759; -.
DR Proteomes; UP000239899; 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:InterPro.
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; 2.
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; 2.
DR Pfam; PF20260; PUA_4; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 2.
DR SUPFAM; SSF88697; PUA domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:PRW58851.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PRW58851.1}.
FT DOMAIN 66..106
FT /note="Ribosomal RNA small subunit methyltransferase E PUA-
FT like"
FT /evidence="ECO:0000259|Pfam:PF20260"
FT DOMAIN 127..164
FT /note="Ribosomal RNA small subunit methyltransferase E
FT methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04452"
FT DOMAIN 201..318
FT /note="Ribosomal RNA small subunit methyltransferase E
FT methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04452"
FT REGION 160..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 323 AA; 33275 MW; 3EAE4626D51A556F CRC64;
MAAVAAVGAR PLAARLAAAS RRAATSTAVH AAAADTPAVS SPAQRPPRFY LPASLRDAGA
GAVLRLPPEE ARHATKTLRL REGDRLELCD GRGWVVQAEL AGADKAGAVV HTVAAPEQVA
LRGWQWEVAC ACGSLKGGRS DWLVEKAAEL GAASLTPLLT QRSPSIGSGG DDERPAAQGG
KRAGRRRGGG DDEDGEAAAS GREGRWARVA TAAMKQCLRP YALVIHPPTS VEQLCQRIQA
ADAALVGVGP DAPALQAVAA ALQAPPGRLG RGILCIGPEG DWTPEELEQL LAAGAQPVAL
GDLRLRAETA AIALLAYLRM QLP
//
