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Database: UniProt
Entry: A0A165KXY2_9APHY
LinkDB: A0A165KXY2_9APHY
Original site: A0A165KXY2_9APHY 
ID   A0A165KXY2_9APHY        Unreviewed;       835 AA.
AC   A0A165KXY2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Protein SQS1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DAEQUDRAFT_770335 {ECO:0000313|EMBL:KZT63736.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT63736.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT63736.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT63736.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV429160; KZT63736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165KXY2; -.
DR   STRING; 1314783.A0A165KXY2; -.
DR   OrthoDB; 1333919at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1370.50; R3H-like domain; 1.
DR   InterPro; IPR000467; G_patch_dom.
DR   InterPro; IPR001374; R3H_dom.
DR   InterPro; IPR036867; R3H_dom_sf.
DR   PANTHER; PTHR14195; G PATCH DOMAIN CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR14195:SF2; GH10944P; 1.
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; R3H domain; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT   DOMAIN          670..734
FT                   /note="R3H"
FT                   /evidence="ECO:0000259|PROSITE:PS51061"
FT   DOMAIN          791..835
FT                   /note="G-patch"
FT                   /evidence="ECO:0000259|PROSITE:PS50174"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          303..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..435
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..468
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..499
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..536
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   835 AA;  91267 MW;  C24F29414CBBF5D8 CRC64;
     MDSPRGRGFF RGRGRGDYNE TTRGRGRPSR GQLNSRLRAG VPLSKLLNED RPLLKPIVFV
     RSVHTATLFQ QEEDILQPLV EPVAENEKSH VPTAEQVSRV FNGQAESDHN LSGAEEEIKE
     IDFADLGKLQ AEVDAIATTM AGEHTHTRVT TDTKVKEETF AGFFVDTTPA PVTARSAPTA
     MTDRMEGALG EDDEIIVYVA PHPRLSRAPT PATLAETITT TSILTGRELT NTQQINTSAV
     PALPSIPEAS ASPGTNIPPV PNDVDEAPAP TAVAPQISEP PSIPEPPSFE SISFSFETSV
     RKKQTRRLFP VGGPRSLLPR SKKARRRRPR HLGAFGAAVS EAQARREGRE RDPREAEQRR
     GDSDVNFGES SEDDAGVEEV SNGVGAMDLD VDAGISLDAM KSFVKSMSAE GSRHVTMDDI
     ADGERMRAED AQEEGEDSSR GSDEESEESD GEEEADEDDE EDKELEETLD AEERALVGEV
     SEDDEEQEED EDEDDSSDEN DTPKTGFQAR LARMRARDKG RNNGKGKARQ MDDSSDEDME
     TNVAWADEDE DFIAEIEEML DANAYLLSSG DRKARKKLFK AVEDGVFDDD EFATMRTPAP
     RKKDTHVPQG LQEQWDKDRQ KKAENKRRHA EARIAVAADP LAVHKGGKKG RKAMLAAAKL
     DSHVEVENRV VGFVSLEAQI RRFLADISGK GTMALPPCDK DTRKKIHELA SAFNLKSESK
     GKGTGRYTTL VKTSRSGIAI NEKKIRGILK RNQDSIWDAP GRGKGKGRAG QSLAKHREGE
     EVGKAAPKIS QSNIGFRMLA AMGWAEGDRI GLSGGLDAPL TAKMKKTKLG LGATM
//
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