ID   SQS1_PODAS              Reviewed;         718 AA.
AC   Q875B6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Protein SQS1;
GN   Name=SQS1;
OS   Podospora anserina (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX   NCBI_TaxID=2587412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=s;
RX   PubMed=12892638; DOI=10.1016/s1087-1845(03)00025-2;
RA   Silar P., Barreau C., Debuchy R., Kicka S., Turcq B., Sainsard-Chanet A.,
RA   Sellem C.H., Billault A., Cattolico L., Duprat S., Weissenbach J.;
RT   "Characterization of the genomic organization of the region bordering the
RT   centromere of chromosome V of Podospora anserina by direct sequencing.";
RL   Fungal Genet. Biol. 39:250-263(2003).
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; BX088700; CAD60695.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q875B6; -.
DR   SMR; Q875B6; -.
DR   VEuPathDB; FungiDB:PODANS_5_5420; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd02646; R3H_G-patch; 1.
DR   Gene3D; 3.30.1370.50; -; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   InterPro; IPR034082; R3H_G-patch.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00393; R3H; 1.
DR   SUPFAM; SSF82708; SSF82708; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus.
FT   CHAIN           1..718
FT                   /note="Protein SQS1"
FT                   /id="PRO_0000325000"
FT   DOMAIN          537..599
FT                   /note="R3H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT   DOMAIN          673..718
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   REGION          247..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          341..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..398
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   718 AA;  78868 MW;  F9CABA64C60EEC3F CRC64;
     MQSPTLLTFD LPPESRAMSV PFPQRRFSRV SRTQMVRFPD SALAWLQDLA HLTPTDFSLK
     DEVRNTQSHH LDSAWTSGTV KLRQKPVSFV SAGYSEPLKL LEDIEQDKVP PGEATESKAD
     DMDITTVDVN LNVSAEAVIE KTTLVELDSA AKGKMVLSNS TSQDNPSSET PQEQAQDLFF
     FDVSGDKAIR DKHRAVHPPP LVPIRKPSLA ESDSSEEVIL FRGRAGNAKT VPQSNFVVRN
     GVATNTTTAI TPTGDKTKPT AAEETSLRDD PEVIPVAREK RAGRQRSRSK ASKIPKTDED
     DEEDAILADY IANMSANPED DFISDQLRSF NNRRDLGGDN FALNLGSGDE NDMPVVEDLS
     GDEQQAESSG SGLSDADEDN GDENDEADED DDMDADMDDE GLARLLAKQE ELGLGSDELV
     LIPESFGVSK RGAKKGGQKR ATPSSFAKSA NASSVADAFD DLDLADWTVP VPRKRRSKQP
     PNFNISDSEI EAKLKLDWSR DRERKKERKL ARESLRGQGL LDKNASPDDL RVKYPVGLRL
     EDFKTELVAF LISSDERLEF PPLDKHGRMV LHQLALKFNV KSQSTGKGTT RRPVLYRSKR
     TITFKPHQIT EATRQVDGAA RRVGRKYFPR ADVAGPRGDT PRDGFRGSAH VSVKALVLRE
     GEVVGASAPE LGQENKGRAM LEKMGWSKGM ALGALENKGI LEPVAQVVKK SKAGLGRT