ID   ESF1_ASHGO              Reviewed;         619 AA.
AC   Q756J5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Pre-rRNA-processing protein ESF1;
DE   AltName: Full=18S rRNA factor 1;
GN   Name=ESF1; OrderedLocusNames=AER259W;
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, AND SEQUENCE REVISION TO 327.
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 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 ESF1 family. {ECO:0000305}.
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DR   EMBL; AE016818; AAS52940.2; -; Genomic_DNA.
DR   RefSeq; NP_985116.2; NM_210470.2.
DR   AlphaFoldDB; Q756J5; -.
DR   STRING; 33169.AAS52940; -.
DR   EnsemblFungi; AAS52940; AAS52940; AGOS_AER259W.
DR   GeneID; 4621326; -.
DR   KEGG; ago:AGOS_AER259W; -.
DR   eggNOG; KOG2318; Eukaryota.
DR   HOGENOM; CLU_010564_0_1_1; -.
DR   InParanoid; Q756J5; -.
DR   OMA; LTWDETA; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032040; C:small-subunit processome; IEA:EnsemblFungi.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR   InterPro; IPR039754; Esf1.
DR   InterPro; IPR012580; NUC153.
DR   PANTHER; PTHR12202; PTHR12202; 1.
DR   Pfam; PF08159; NUC153; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Nucleus; Reference proteome; Ribosome biogenesis; RNA-binding;
KW   rRNA processing.
FT   CHAIN           1..619
FT                   /note="Pre-rRNA-processing protein ESF1"
FT                   /id="PRO_0000228157"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          395..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          418..476
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        8..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..143
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..490
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..509
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..597
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   619 AA;  70969 MW;  74AB087102DCB13E CRC64;
     MAKNNEGTGK DSIDKRFARI ESDPKFRAPK QKNLKIKLDD RFSKQDLEYK RKAKVDKYGR
     RIGTAPGKEE KDFEKYFTKE SSESAAEESD KEDSSVAKLD RARGEVPADY VSSSDEESSS
     ESEADSDDAT AESDEEVEIE EEKPESGDPS KVLAVVNLDW DHVKCADLLV AFNSFVPEGG
     KIERVAIYPS EFGKERMQRE EVEGPPREVF KSKKDKKAKQ DDDDEIGLKD LYEQGDAEKD
     YDSKALRRYQ LERLRYYYAV VYCNNVATAE AIYQNCDGTE YESTANMFDL RYVPEGVTFD
     DEPREECASV PKDYKPVQFS TSALQHSQVK LTWDETPADR VEMAKRAFSQ KEIEDMDFKA
     YLASDSEESE ADDNSEAKNK LRSLVSSVKV ADKPLFADES DEEEADVQIT FTPGLEGGEA
     KEEDAEEENI LEKLKRKEKE RRKKRKERVK ELKKQAEEEK KSSKKEKHAS KSESEQKSEN
     DKRAELELLM MEDDENSQSI NSSAHFNMND ILRSEKERGK KSKYQKKDKI VEDDFKPDLN
     DPRFKEVFED RDFAIDPSQP EFKETAAMKQ ILQERRKRSS KSASKKRKTD EQSDSAMDSA
     GDLKGLVAKL KRKGKKPKL