NEP1_CANGA
ID NEP1_CANGA Reviewed; 229 AA.
AC Q96UP2;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
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; Synonyms=EMG1; OrderedLocusNames=CAGL0B01232g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=12620120; DOI=10.1186/gb-2003-4-2-r10;
RA Wong S., Fares M.A., Zimmermann W., Butler G., Wolfe K.H.;
RT "Evidence from comparative genomics for a complete sexual cycle in the
RT 'asexual' pathogenic yeast Candida glabrata.";
RL Genome Biol. 4:R10.1-R10.9(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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
CC {ECO:0000250|UniProtKB:Q06287}.
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; AY034788; AAK61538.1; -; Genomic_DNA.
DR EMBL; AY181247; AAO25590.1; -; Genomic_DNA.
DR EMBL; CR380948; CAG57923.1; -; Genomic_DNA.
DR RefSeq; XP_445023.1; XM_445023.1.
DR AlphaFoldDB; Q96UP2; -.
DR SMR; Q96UP2; -.
DR STRING; 5478.XP_445023.1; -.
DR EnsemblFungi; CAG57923; CAG57923; CAGL0B01232g.
DR GeneID; 2886681; -.
DR KEGG; cgr:CAGL0B01232g; -.
DR CGD; CAL0127832; EMG1.
DR VEuPathDB; FungiDB:CAGL0B01232g; -.
DR eggNOG; KOG3073; Eukaryota.
DR HOGENOM; CLU_055846_1_1_1; -.
DR InParanoid; Q96UP2; -.
DR OMA; CAKICSA; -.
DR BRENDA; 2.1.1.260; 1113.
DR Proteomes; UP000002428; Chromosome B.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
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; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA processing; rRNA-binding; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..229
FT /note="Ribosomal RNA small subunit methyltransferase NEP1"
FT /id="PRO_0000158611"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 184
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 189..191
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT BINDING 204..209
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 67
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 69
FT /note="Stabilizes Arg-67"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 108
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 111
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
FT SITE 115
FT /note="Interaction with substrate rRNA"
FT /evidence="ECO:0000250|UniProtKB:Q06287"
SQ SEQUENCE 229 AA; 25596 MW; E4BED261436D0314 CRC64;
MVEDSKARIG GPNNSSVTKK QEPRLYVVLC EASLETYTSN DHRTSLLNCD DHQGILRKMG
RDIAEARPDI THQCLLTLLD SPINKAGLLQ VYILTKKNVL IEVNPSVRIP RTFKRFSGLM
VQLLHKLSIR SMESSNTHLL RVVKNPVTKY LPADCRKVTL SFDAEVMRPQ EYLGDKQSVC
VFVGAMARGH DSFADEYVDD KIAISNYPLS ASVACSKFCH GAEDAWAII
