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Database: UniProt
Entry: A0A1Y2W192_9PEZI
LinkDB: A0A1Y2W192_9PEZI
Original site: A0A1Y2W192_9PEZI 
ID   A0A1Y2W192_9PEZI        Unreviewed;      1005 AA.
AC   A0A1Y2W192;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   RecName: Full=DH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=M426DRAFT_12621 {ECO:0000313|EMBL:OTB03475.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB03475.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB03475.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB03475.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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DR   EMBL; KZ111559; OTB03475.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2W192; -.
DR   STRING; 1001833.A0A1Y2W192; -.
DR   InParanoid; A0A1Y2W192; -.
DR   OrthoDB; 23973at2759; -.
DR   Proteomes; UP000242955; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   CDD; cd00014; CH_SF; 1.
DR   CDD; cd05992; PB1; 1.
DR   CDD; cd13246; PH_Scd1; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR010481; Cdc24/Scd1_N.
DR   InterPro; IPR033511; Cdc24/Scd1_PH_dom.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR47339; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   PANTHER; PTHR47339:SF1; CELL DIVISION CONTROL PROTEIN 24; 1.
DR   Pfam; PF06395; CDC24; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF15411; PH_10; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS51745; PB1; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000242955}.
FT   DOMAIN          227..401
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          905..1000
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          581..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        597..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        656..701
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        746..786
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..875
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1005 AA;  110491 MW;  1FA9AA2EE6A9BCDB CRC64;
     MAHAPALLRT NTAPVFPADN KYGSMTASTM SSLRTSQLSG STVLNSSNSS LTSMSASTGN
     VVATANIINQ KADASRSLYQ ICIALKQRLA RVPNFETHLE ALEANRGDDG PVESLWNLLR
     TGLPLLTIYN TLQPESQLEI DPTANDTKRS KLAIFKFVEA CMKQLKFPPS ESFVISDLMG
     NDTTGFVKVT QVVNRVLDRA EQQGLLLQVD PYLEVVGPVA PGSQMSYRDH IIQELVDTER
     KYVQDLENLH DLKKTLEQKG VIPGDIIHQI FLNINSILDF QRRFLIRVET ANSMTEEAQR
     WGAPFAIYED AFDIYQPFIA NQRKAGQIAN QVFDKIQLAD HPVTYDFNTL DGFLLKPMQR
     LVKYPLLLKS LLKKCENEEV RADLTAGIEA SERVLSKANE AVDRDLLDEA LEDLIRRVDD
     WKNHRVDQFG RLLLHGVYTV ITGRSEQEKD YEIYLFECIL LCCKEVIPNK SKEKKDKNKT
     GPRIPNKNNK LQLKGRIFMT NVTDVLSYAK PGSYTVQIWW KGDPGVENFI IKFSNEETMK
     KWETGLVAQR KENAPNTAAT PDQTTPNFAW MQNQSNIENP YAQQEEDDEE EDEVQQPPQV
     SPPNMGFGGN STGGVMARNA SDTSLRARSA TAGSTQSLAS IARAPPPRFP LPAPPGQLSL
     QTQGNAQSPG PHAGESYFSP TAESPASSRT STASTMFGGQ FPFPRTGTPQ GGWEDSNRYT
     APAMPRAPSR DGPSPMNGRN PRGPSLPVMA SSQSQTLTQQ QRSRSYSTPD INGQPNGRRT
     NNSTPVPAVP GIPPHLHPAH DANIPRSQTG SPRQDVPIRA NTQSPGVQRD GRSTQQSGQY
     GGTMAQFPTQ PVYSRQTTPA PATAAPTGSL PPPLNINNQQ PVSPALGTAT QHNPLASPDM
     SIPAQLKVKV NCDNGAYITL VAPFNIAYQS LRDRIDAKLG RFTSSSIAKG NLKLRYRDED
     GDSVTIESDD DIQIAFSEWR EGARNTSNGV GEIELFCVGE VGETG
//
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