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Database: UniProt
Entry: A0A168MF57_ABSGL
LinkDB: A0A168MF57_ABSGL
Original site: A0A168MF57_ABSGL 
ID   A0A168MF57_ABSGL        Unreviewed;       997 AA.
AC   A0A168MF57;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=DH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=ABSGL_03945.1 scaffold 4693 {ECO:0000313|EMBL:SAL98416.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL98416.1};
RN   [1] {ECO:0000313|EMBL:SAL98416.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98416.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT552071; SAL98416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168MF57; -.
DR   STRING; 4829.A0A168MF57; -.
DR   InParanoid; A0A168MF57; -.
DR   OrthoDB; 23973at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; 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; 1.10.418.10; Calponin-like domain; 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; IPR036872; CH_dom_sf.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
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; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT   DOMAIN          257..430
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          454..576
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          913..994
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..907
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..653
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        835..854
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   997 AA;  112485 MW;  3AFFD7D1EFBCEEC2 CRC64;
     MATPALKRRT PSLGATPTIS SPPTHSPFNS PTTTAPATTA TEASITSTIT NTSSTSSTIS
     STSSKTPPPG SSLYHTCRLV LDKLALVDGM SYWLDLEEDN LSPSLSPINS SSPPLMPLST
     SSPSLAAVNT DASSTAGSNN DPLSKLCYLC RRGTPLFTLF NALNTHQPLK MDPNPKLNQV
     NSCKANVYHF LVACRKQLLF PEEELFTVSD LYVDDTNGFV KVVNTVLKLL QLLEDKGIIS
     SHCANQDSCP MVPPKDIRDQ VVLELLSTER KYVQDLETLQ TYMRELQQQR ILSQDTVHYL
     FGNLNALVDF QRRFLIQMEK TAENQPQDQH FGLLFSQMED AFSVYEPYCS NFYSAQDLVV
     QEAPKLQKLN IMNPTHQLTS LLIKPIQRIC KYPLLLNELI KSTNKEWLTV PEMATGLDTM
     RRVADKVNET QRKHENLQMV VELKRRVDDW KGISIDKCGQ LLLQDKMVVT AYDNEREMHV
     FFFENRLLLC KENKDNTKNR LTKANTITMK KRRRGTLEPK GKIETSRIVS LQNVSSNGEW
     ALMIEWKEHQ VEQFTLKFRN EEQYKLWEST LNKQKDRRAV AAASSLVYST SNIDLHSNDS
     NVPTVASSSS NISIFNHPNY LTTLPLNPHV NDNWSFIDPD DEEDEVDSVE DDGEESSSGS
     RSRSNSFSAQ ILNTFSTRPK FGRNNSTDIS GLKPLSTPAT TMTSGRSNTP GLNLQPLPRS
     NNSNLYHHEQ PVPGDYFFYP SSPPPSNPSS PTSSSRVSPN NSSSGRTFRD HPSSQMLHHH
     YLQHHQKQKP TVLPTPSEPM TPSMDYFATP TMDAFDSSLL TGRPGPSLSE QQHYDRHHHH
     HHHHHHHHHQ RPPPAQSRSR AQSSPSISRR HDNRPDGYYP VQQQRQYSLS TTLPKVSSDK
     KSASLSDQLA PGLRKVKLIY NDGVYSIIIV SQHISCEELM DRVEQKLQVV GDLPYYCGFR
     LKYRDEDGDL ITINSTEDIQ MAFESDSTSS SHFYVCM
//
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