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Database: UniProt
Entry: A0A168NKY6_ABSGL
LinkDB: A0A168NKY6_ABSGL
Original site: A0A168NKY6_ABSGL 
ID   A0A168NKY6_ABSGL        Unreviewed;      1270 AA.
AC   A0A168NKY6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=DH domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=ABSGL_06464.1 scaffold 8356 {ECO:0000313|EMBL:SAM00741.1};
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:SAM00741.1};
RN   [1] {ECO:0000313|EMBL:SAM00741.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM00741.1};
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; LT553414; SAM00741.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168NKY6; -.
DR   STRING; 4829.A0A168NKY6; -.
DR   InParanoid; A0A168NKY6; -.
DR   OMA; FAHVNDI; -.
DR   OrthoDB; 5100844at2759; -.
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; 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   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR041675; PH_5.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR46572:SF2; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF15405; PH_5; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50010; DH_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561}.
FT   DOMAIN          512..700
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          904..1247
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          23..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          122..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1017
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        980..1016
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1270 AA;  142943 MW;  80E12B25DE748D88 CRC64;
     MTTQSTTTRL TPSASIREQY YRKHGIQQRS TSNLNPSSNQ VDNVTSQQQQ QLRDEGEDSD
     NLFDYRPEGA IAFAPLKLPD FPSINADDIS LLSRQTEYDD TEDDEAATRS IISLQTMDSL
     AIGNNDSGHS TLASSSGTNS GHPLAAPAPA PAPPRSLFGQ PKSSRNFLRR QQSSQTLFAS
     SSSAMDPQWP PQQQVTSSKA STNEKASLLS RLSKTTAPMR ARLSAMSRTS NYLKSEMVAS
     ISIPLRRSAE SVYNFPTSTA MRITGRKTQA ERAQSFTFEK SVRPSRDLIS PNQSTSTSSK
     DGAPVLYPAM LSEVAVAFKE RVTVGTKIKN SIKYKDTFDG VEAVDKLAFL TKTKDRNLAL
     LLGRALDAQK FFHDVNYEHR LRDSRQELYR FTEHINVRHS QLLPSPPQND SSIAEEDDVS
     EFNYPTPTND NNHPNGVFTL LLTCYSPTCS REKLCYSVFC PRRLEQQARS ANHRNQIHRS
     SSKSSLVEKK DRLWTTTVPK AIVEKLSKED RKRQENIFEF IYTEKDFVDD LGYLKTYWIE
     PLLTGDIIQP PERRESLVRD IFWNIMEVHE ANGRFVEALQ KRQKQNPVVD QVGDIILEYV
     AHFTPFVQYG AHQIIGKSIF ETEKSTNPDF AAFVQTTERL PVSRKLELNA YLTKPTTRLG
     RYSLLLREIL KHTAKDHPDQ ETIPKATKII AEHLTNVNHE TGKTENRFNL QLLAEKMQDS
     SHLSDMDLDL LDENRQIVMK GPLKRKGTGS ESLALQVYLL DHCLIITKQK FVDDVEHIKL
     YKKPIPIGLL AISLPDQTKR ASVILPYGQH KTSGSISSID LTSLASASNP NGTSSSGTTG
     TKSGYPISFV HLGRHGANPT TLYASTFTSR RQWVDKIESY RYSVMEKQKV FEVVPINSDF
     FNGFNKVNCA ATFGDSIIIG SDQGVYLSSG TKNQRKVTRL LSMDKVSQID ILENKFILVL
     ADKTLYTYAM DSLLNKEGQQ QGSDDDDGGY TKTNDFDDND TTHRQTEGDG STHSRRGRKI
     SSHVSFFKVG TVMDKSEGQA VERSLVCYVR YNAMTSTIRA LEVHDSSAAK NKKKKQQSIR
     RKTKQLGTLL RHQHEGLRVF KDLYIPGEAT SIQYFKNVLC IGSAKGFQMV DVGSAGVLSV
     LDPNDTSHAV MASKYDLRPI SMFRHPEKNI LLCYNDLAFY IDKKGQRARP DWIMRWEGNP
     TAFAFRYPYI VAFDSSFIEI RHIDTGHIVQ VIPGNNIRCL KPDPLDAIHC VMEDGVSGNE
     LVFQLKFIEK
//
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