ESF2_YARLI
ID ESF2_YARLI Reviewed; 324 AA.
AC Q6CFT1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Pre-rRNA-processing protein ESF2;
DE AltName: Full=18S rRNA factor 2;
GN Name=ESF2; OrderedLocusNames=YALI0B04136g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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: Involved in the small subunit (SSU) processome assembly and
CC function, and in the 18S rRNA synthesis. Required for the early
CC cleavages at sites A0, A1 and A2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ESF2/ABP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382128; CAG82708.1; -; Genomic_DNA.
DR RefSeq; XP_500481.1; XM_500481.1.
DR AlphaFoldDB; Q6CFT1; -.
DR SMR; Q6CFT1; -.
DR STRING; 4952.CAG82708; -.
DR EnsemblFungi; CAG82708; CAG82708; YALI0_B04136g.
DR GeneID; 2907052; -.
DR KEGG; yli:YALI0B04136g; -.
DR VEuPathDB; FungiDB:YALI0_B04136g; -.
DR HOGENOM; CLU_054086_0_0_1; -.
DR InParanoid; Q6CFT1; -.
DR OMA; TRKHNDF; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR GO; GO:0001671; F:ATPase activator activity; IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0034462; P:small-subunit processome assembly; IBA:GO_Central.
DR CDD; cd12263; RRM_ABT1_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR039119; ABT1/Esf2.
DR InterPro; IPR034353; ABT1/ESF2_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR PANTHER; PTHR12311; PTHR12311; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..324
FT /note="Pre-rRNA-processing protein ESF2"
FT /id="PRO_0000285381"
FT DOMAIN 126..216
FT /note="RRM"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..91
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 36936 MW; 33593DB700704514 CRC64;
MARAKAVDFF STKNNSSDSE EEEDKPAVDP RFVLADSDSE GEEEQEDGDE DEEEKGRTSK
KKTKDFFELA GKTDDGDDEE EDEEDEEEEE EEKEKKPVKT SSTKAKTKPM TKEEIEKHNK
KIAKTGVVYF SRIPPLMDPG KLRMLLQRFG IVDRIYLVPE DPKAQAVRIR HGGNRALAYT
EGWAEFTKKR YAKTCASTLN GNTIGGKKGS QHYDDIMNAK YLPKFKWSDL SEQLAQETHN
RQARLRTEIS QATRENQTYI QSLEKSKAAE RRRQRQEEEG GETEEKPAKK VHRDFYQGKT
HSARAKEGKK ELDGSVGSIL GSVM