ID   SQS1_ASHGO              Reviewed;         679 AA.
AC   Q75E62;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Protein SQS1;
GN   Name=SQS1; OrderedLocusNames=ABL192C;
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: May be involved in splicing. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SQS1 family. {ECO:0000305}.
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DR   EMBL; AE016815; AAS50579.1; -; Genomic_DNA.
DR   RefSeq; NP_982755.1; NM_208108.1.
DR   AlphaFoldDB; Q75E62; -.
DR   STRING; 33169.AAS50579; -.
DR   PRIDE; Q75E62; -.
DR   EnsemblFungi; AAS50579; AAS50579; AGOS_ABL192C.
DR   GeneID; 4618834; -.
DR   KEGG; ago:AGOS_ABL192C; -.
DR   eggNOG; KOG0154; Eukaryota.
DR   HOGENOM; CLU_021974_1_0_1; -.
DR   InParanoid; Q75E62; -.
DR   OMA; PVFMRID; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0030686; C:90S preribosome; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0030688; C:preribosome, small subunit precursor; IEA:EnsemblFungi.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IEA:EnsemblFungi.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:EnsemblFungi.
DR   GO; GO:0051096; P:positive regulation of helicase activity; IEA:EnsemblFungi.
DR   CDD; cd02646; R3H_G-patch; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR034082; R3H_G-patch.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome.
FT   CHAIN           1..679
FT                   /note="Protein SQS1"
FT                   /id="PRO_0000324993"
FT   DOMAIN          514..576
FT                   /note="R3H"
FT   DOMAIN          633..679
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..419
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   679 AA;  76536 MW;  3185379DD37994D2 CRC64;
     MAKRHKHYEN RGSSGRGRRG GRAGHRGRGG RRRYAERNNS ERAAPVWAGS GDLGNPEMVD
     DYYFGRQADR RLWKKDSMRM GGFRPGDMGA SEQPQSHLPA RKRPVTFTLA RDVYDPSHNL
     NQLLNKQLDE GAEEEDSNSS SPSASGDDEP EGEYEPNPEP KMYRISELND DALFFVDEQG
     KLPTKIPAVE VAQQETPRSV EFNDTLTVGK VQLQLRQDSN GGTFVDAPHA KRIFRDDLYG
     DVSEEEDEPE TPKTEQLDNS KSVRTMQPPS PVPQLLSTNI GRLTLSELAS ESESDTEKPT
     AEAGAEPPKG EPGFGFLDED HLADMSEIQV TNIRLGAAAH SYFVASPRTF GDSVARWVDH
     DTMVDIALEL GLPEGRLHAY LRHVYEQLVP PEEPADDGAD DHYGDENYDD SEEDEQDDEY
     ENDGLIALVE HTLANDPYRN RDYNTKSLEY RGHGSRKRLI IDKESMIDET VRTLLEDKAA
     QRSAKRAAKR HAKEDYIAEE ARMSSDLFRK YPYGFHIENI IDELEAFLVS PRAALEFPPL
     DPHGRRTLKN LACAFALICK QVGQSTHTRV LVQKGGRYEP DYDAVNRIRR QRRVFMRVDV
     RRPRDDITPR EPRAKFHVRE GAIVGGDAPT IGQDNVGRRL LEKLGWTHGE GLGVHGNKGI
     SEPLMARVKK NRSGLRYTE