ESF2_ASHGO
ID ESF2_ASHGO Reviewed; 314 AA.
AC Q75DA3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Pre-rRNA-processing protein ESF2;
DE AltName: Full=18S rRNA factor 2;
GN Name=ESF2; OrderedLocusNames=ABR121C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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}.
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DR EMBL; AE016815; AAS50892.1; -; Genomic_DNA.
DR RefSeq; NP_983068.1; NM_208421.1.
DR AlphaFoldDB; Q75DA3; -.
DR STRING; 33169.AAS50892; -.
DR EnsemblFungi; AAS50892; AAS50892; AGOS_ABR121C.
DR GeneID; 4619176; -.
DR KEGG; ago:AGOS_ABR121C; -.
DR eggNOG; KOG3152; Eukaryota.
DR HOGENOM; CLU_054086_0_0_1; -.
DR InParanoid; Q75DA3; -.
DR OMA; TRKHNDF; -.
DR Proteomes; UP000000591; Chromosome II.
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..314
FT /note="Pre-rRNA-processing protein ESF2"
FT /id="PRO_0000285361"
FT DOMAIN 116..206
FT /note="RRM"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 314 AA; 35749 MW; 9FA17C699809DF1E CRC64;
MSDNDSDVQD FSSEEEDHGL LIDRKKQQTL DFAQDGSDSE GGSDLDDDDI AEEESPIQNE
TKAATGEEPA TADGDNIAPQ SADELRPEER ADQLKQERLR RLKKLKASKK SNHKTGVVYL
SKIPPYMKPA KMRQILSRFG DLDRLFLKRE DEHSHRQRVK GGGNKKVMFR EGWAEFIRKK
DAKLCAETLN GNIIGGKKGN FYHDDVMNVK YLSGFKWADL TEQIARENDV RQSKLQLEIS
QANKLNAEFI RNVEKSKMLN NIRAKKHKDE DSSERTESHL PVKQRKVTSN RASAPESQKQ
PASEKLSNVL HNLF
