ID   SQS1_KLULA              Reviewed;         740 AA.
AC   Q6CQ59;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protein SQS1;
GN   Name=SQS1; OrderedLocusNames=KLLA0D19558g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: 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; CR382124; CAH01026.1; -; Genomic_DNA.
DR   RefSeq; XP_453930.1; XM_453930.1.
DR   AlphaFoldDB; Q6CQ59; -.
DR   STRING; 28985.XP_453930.1; -.
DR   EnsemblFungi; CAH01026; CAH01026; KLLA0_D19558g.
DR   GeneID; 2893211; -.
DR   KEGG; kla:KLLA0_D19558g; -.
DR   eggNOG; KOG0154; Eukaryota.
DR   HOGENOM; CLU_021974_1_0_1; -.
DR   InParanoid; Q6CQ59; -.
DR   OMA; PVFMRID; -.
DR   Proteomes; UP000000598; Chromosome D.
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..740
FT                   /note="Protein SQS1"
FT                   /id="PRO_0000324997"
FT   DOMAIN          561..623
FT                   /note="R3H"
FT   DOMAIN          690..737
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..37
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..464
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  83920 MW;  4BF9CC7187267DA3 CRC64;
     MAKRHKHYNA RGGGKSKSKK SKPHGESRQR KNHRGGTSIN RNRSELLLGG GDLMNPHQVE
     DYYFGSTAKK SSLRSGGFRP GRLTEADELD TGRLPSRKRP VEFIKAKELY DPSHDLILKL
     VKKNQHFDEP NSDGYNSSQS VSLREEEQDG EDEQQDVDTQ EIPSKNTTVK IRSDNVVSEN
     GDSESNSSAN DAELFYVDME GEEKTADNYI KTVDVDVQER SLKLNDCTEF QPTLRVGNVE
     LNLKDGGSGS IEVDKPKSSY HPFHSYIQNV MENVQNYDSD DDFDENGNDV EQSFSISSDY
     EFESSEELIT TGGTIEQFDS SMKSLTIEEI PGKTITASLT TKDISQGNSD NSSGDESFGF
     CEDDFEGSIG KVFVSNIRIG AGTHSYHVSC HEIYGDSEPR WVDDEMMNEI IAEMGLPEHR
     FRAYYKHLHK SFIEEEEEPE EYADIPFDDD DSDDSTADQC EPFAEDDLGE DLDDLVSYAL
     KYNKQRKIEY HTTSLDIRGK GRNKHLIFDQ TAGMDEDIKL MLQNKFATRQ INKTKKRRAK
     EDFLSQSHAS STDLLMKYPY GLHIQNIKDE FDAFYRNDRQ SITFPPLDPH GNKIIGKFAY
     NYFMKASNIG KGKSTKVYVE KTKKTRFNKP AYHIISQLLR KRPVFMRIDQ KAPTDTQSTF
     NRTVRLKVSK ENFNISEGQI VGEDAPEIGI DNIGRRMLEK LGWNIGQGLG AHGNQGINEP
     ILAKVKKNKS GLRHTSENQQ