ID   A0A165GE67_9APHY        Unreviewed;       477 AA.
AC   A0A165GE67;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   RecName: Full=DH domain-containing protein {ECO:0000259|PROSITE:PS50010};
GN   ORFNames=LAESUDRAFT_416371 {ECO:0000313|EMBL:KZT10223.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT10223.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT10223.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT10223.1,
RC   ECO:0000313|Proteomes:UP000076871};
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; KV427609; KZT10223.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165GE67; -.
DR   STRING; 1314785.A0A165GE67; -.
DR   InParanoid; A0A165GE67; -.
DR   Proteomes; UP000076871; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   PANTHER; PTHR47339; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   PANTHER; PTHR47339:SF1; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   Pfam; PF15411; PH_10; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871}.
FT   DOMAIN          1..71
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   REGION          308..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          438..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..327
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  52756 MW;  C81BF0FDFF752112 CRC64;
     MHKMKMINDV HDIKVADLPM LLVKPLHRIH AYPALLKSLS EAVVGTAYAH YPELQAGLRA
     AERISDRLHK VYRSAKNTLI LGTLPRRLIK WEESEVSQLG SLLLSDFFTM PGDKDDGLHA
     FLFEKGILLC KELPGFLLGS KRTRKRAWTL TKPKSPTQLP DMDTRLIVET HISLQTEFHV
     APYSQGQHSL FIWWNGDDGS DDGHKVLCCQ DVTQLREWEG ELKLFAARKD AQPPTSDIVH
     PQEIQGTDDQ LYFDDLSLTE EARIPEIVTT AAGPSADHHA VRTRSGSWST LRRKFSSAAL
     STKVASGKYP SYDGAASHTT SSLRPRSGSF PYARPDPHIG LNRARATPSP LSRSVDLPLT
     GENNRGEQLR TQTPSVYDET ANLLAAATDS GTPAQTTAVD IIVHPSPANT DPFQDGRSSI
     FPFSIWDRLR HKLSSSSFRA SDDADDLPTS PPNAGLLVPP RNRVRSASDP IASSRRT
//