NEP1_CANAX
ID NEP1_CANAX Reviewed; 267 AA.
AC Q9P8P7;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase NEP1 {ECO:0000250|UniProtKB:Q06287};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q06287};
DE AltName: Full=18S rRNA (pseudouridine-N1)-methyltransferase {ECO:0000250|UniProtKB:Q06287};
GN Name=NEP1 {ECO:0000250|UniProtKB:Q06287};
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=11935223; DOI=10.1007/s00294-001-0269-4;
RA Eschrich D., Buchhaupt M., Koetter P., Entian K.-D.;
RT "Nep1p (Emg1p), a novel protein conserved in eukaryotes and archaea, is
RT involved in ribosome biogenesis.";
RL Curr. Genet. 40:326-338(2002).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent pseudouridine N(1)-
CC methyltransferase that methylates the pseudouridine corresponding to
CC position 1189 (Psi1189) in S.cerevisiae 18S rRNA. Involved the
CC biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-
CC carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S
CC rRNA. Has also an essential role in 40S ribosomal subunit biogenesis
CC independent on its methyltransferase activity, facilitating the
CC incorporation of ribosomal protein S19 during the formation of pre-
CC ribosomes. {ECO:0000250|UniProtKB:Q06287}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q06287};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q06287}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11935223}.
CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase NEP1 family. {ECO:0000305}.
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DR EMBL; AF222909; AAF35325.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9P8P7; -.
DR SMR; Q9P8P7; -.
DR CGD; CAL0000197320; NEP1.
DR VEuPathDB; FungiDB:C1_11380W_A; -.
DR VEuPathDB; FungiDB:CAWG_00298; -.
DR BRENDA; 2.1.1.260; 1096.
DR GO; GO:0005730; C:nucleolus; IDA:CGD.
DR GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IGI:CGD.
DR GO; GO:0070475; P:rRNA base methylation; IEA:InterPro.
DR CDD; cd18088; Nep1-like; 1.
DR Gene3D; 3.40.1280.10; -; 1.
DR InterPro; IPR029028; Alpha/beta_knot_MTases.
DR InterPro; IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1.
DR InterPro; IPR029026; tRNA_m1G_MTases_N.
DR PANTHER; PTHR12636; PTHR12636; 1.
DR Pfam; PF03587; EMG1; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Nucleus; Ribosome biogenesis; RNA-binding;
KW rRNA processing; rRNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..267
FT /note="Ribosomal RNA small subunit methyltransferase NEP1"
FT /id="PRO_0000158610"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 222
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 227..229
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 242..247
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 103
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 105
FT /note="Stabilizes Arg-103"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 144
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 147
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 151
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
SQ SEQUENCE 267 AA; 29547 MW; A5A25AA3097556AC CRC64;
MSELKNGTTE PKKNETTQSD SKSKSTSTNK SSVPPASLVP VQPTALTSRD KTTQRLIVVL
SQACLETYKM NSGGPGGDRF ALLNCDDHQG LLRKMGRDIA EARPDITHQC LLTLLDSPIN
KAGRLQVYIQ TARGVLIEVN PSVRIPRTFK RFSGLMVQLL HKLSIRSENS KEVLLKVIKN
PITDHLPTKC RKVTLSFDAE LKRVQDYVTT LDENESICVF VGAMARGKDN FADEFVDEKI
GLSDYPLSAS VACSKFCHGC EDVWGIY
