ID A0A087RXI0_9ARCH Unreviewed; 222 AA.
AC A0A087RXI0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase Nep1 {ECO:0000256|HAMAP-Rule:MF_00554};
DE EC=2.1.1.- {ECO:0000256|HAMAP-Rule:MF_00554};
DE AltName: Full=16S rRNA (pseudouridine-N1-)-methyltransferase Nep1 {ECO:0000256|HAMAP-Rule:MF_00554};
GN Name=nep1 {ECO:0000256|HAMAP-Rule:MF_00554,
GN ECO:0000313|EMBL:KFM18184.1};
GN ORFNames=AAA799P11_01215 {ECO:0000313|EMBL:KFM18184.1};
OS Marine Group I thaumarchaeote SCGC AAA799-P11.
OC Archaea; Nitrososphaerota; Marine Group I.
OX NCBI_TaxID=1502295 {ECO:0000313|EMBL:KFM18184.1, ECO:0000313|Proteomes:UP000029387};
RN [1] {ECO:0000313|EMBL:KFM18184.1, ECO:0000313|Proteomes:UP000029387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AAA799-P11 {ECO:0000313|EMBL:KFM18184.1};
RA Ngugi D.K., Blom J., Alam I., Rashid M., Baalawi W., Zhang G., Hikmawan T.,
RA Guan Y., Antunes A., Siam R., El-Dorry H., Bajic V., Stingl U.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Methyltransferase involved in ribosomal biogenesis.
CC Specifically catalyzes the N1-methylation of the pseudouridine
CC corresponding to position 914 in M.jannaschii 16S rRNA.
CC {ECO:0000256|HAMAP-Rule:MF_00554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pseudouridine in 16S/18S rRNA + S-adenosyl-L-methionine = an
CC N(1)-methylpseudouridine in 16S/18S rRNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:46696, Rhea:RHEA-COMP:11633, Rhea:RHEA-
CC COMP:11634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:74890; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00554};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00554}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase NEP1 family.
CC {ECO:0000256|ARBA:ARBA00008115, ECO:0000256|HAMAP-Rule:MF_00554}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00554}.
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:KFM18184.1}.
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DR EMBL; JOSZ01000021; KFM18184.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087RXI0; -.
DR PATRIC; fig|1502295.3.peg.1168; -.
DR Proteomes; UP000029387; Unassembled WGS sequence.
DR GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070475; P:rRNA base methylation; IEA:InterPro.
DR CDD; cd18088; Nep1-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR HAMAP; MF_00554; NEP1; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1.
DR InterPro; IPR023503; Ribosome_NEP1_arc.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR12636; NEP1/MRA1; 1.
DR PANTHER; PTHR12636:SF5; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE NEP1; 1.
DR Pfam; PF03587; EMG1; 1.
DR SUPFAM; SSF75217; alpha/beta knot; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_00554}; Reference proteome {ECO:0000313|Proteomes:UP000029387};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW Rule:MF_00554};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00554};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00554};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW Rule:MF_00554};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00554};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00554}.
FT BINDING 177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00554"
FT BINDING 182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00554"
FT BINDING 198..203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00554"
FT SITE 60
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00554"
FT SITE 62
FT /note="Stabilizes Arg-xx"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00554"
FT SITE 104
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00554"
FT SITE 108
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00554"
SQ SEQUENCE 222 AA; 25307 MW; 0DE46A4B453FE08E CRC64;
MISIVLAESA LELVPSDLKH HPSVVSHARK LGKLSSEILL DNSWHFAAMK GINNELKRGR
PDLVHFSILE ATTLPLYLKN KIKLYVHTID DKVIYFGQNV HVPKSYHRFA GLIEKLYKEK
KITANDDTLL EIKNKTFSEL IDEIHPSKII GLSTKGTKNS YEKIAGEIND DYCLVFGGFQ
KGHFSDSIEK QFAQMYSIGD ESFEGHTVVA RMLYEYEKTI FM
//
