ID A0A165BJR9_9APHY Unreviewed; 894 AA.
AC A0A165BJR9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Dbl homology domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LAESUDRAFT_731561 {ECO:0000313|EMBL:KZT01190.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT01190.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT01190.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT01190.1,
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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DR EMBL; KV427669; KZT01190.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165BJR9; -.
DR STRING; 1314785.A0A165BJR9; -.
DR InParanoid; A0A165BJR9; -.
DR OrthoDB; 53554at2759; -.
DR Proteomes; UP000076871; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12673; FACIOGENITAL DYSPLASIA PROTEIN; 1.
DR PANTHER; PTHR12673:SF159; LD03170P; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 123..316
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 346..506
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 564..630
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 894 AA; 98788 MW; 5421A37542FD69DE CRC64;
MAAVSTPPPA SMVDFPSSSE SHLSSSLSNS DVHHSRLPHL PFRRISLPSA PNLLHRQSIV
STASFDSLPE EGVKPVAPVP AFTPAVIRNA TKPPRHRPSS LDIARKAPRR SQMRPVNERR
EAKRKKVINE LHETEKSYVD GLELIYSHFL TPIIASLDTP EQLLDRSELT SIFSNFIDIW
NLHRSFYTTL TTFLETSASA HPDEPPPLSP VLLAHFPYLS LYTPFVTSFS DALTAYSYLL
STHHTFAEFI SRQEADPRCG KLKFRDWLLT IVQRCPRYLL LLKDLISCTD PDDPEYAQLT
AVHTLVAKIT SSLDTSLHTH AQILSLLALQ RNTAHLPFPL ISPGRTFLKR APLLQLEGST
PKEREFLLFS DCIMWLASAD GDGLLDKLEA VSGHPPLMRT RSKSDADMPL AAEALKHKES
MLGFRIHYHH HHPRRKVRRA SSAADERWVY KGHVDLVDVD VVVTTPREPG EERRFEILSP
QQSFAVYAGS EEERDEWSTA IRNAKSSLLV SLNVMQPNST LTSSSSTNHL RRTLQALPYS
PDEDARRPKR GRVDHFVPAI WIPDGKSQSC MRCGRTFGWR RRRHHCRLCG RCVCGSCSSK
EFFIIDETTK DTREQHKPAR ACDACYESVF PLLEPAREAS TASGTTHSHL TLSGLKSMPS
LVFDRTPSAL MAIDVDSPRS AKRVLARIDD EHGMADSADA GPSVSAIRVK PSARPRSYIH
ILEDFHEFGE TSAPPSASTS FSRYSSMIGG RDGHCEEEEV AAVESAFTEM ESPSRTTTGT
GTTTESSFPP TPKRENTVRR HKRFSLPAIA LQTNPVHARS NLVGEGSARR ISLVLGKGEP
LGHARADGDG DVGADGDGDG SGDGGGEERG RRASGHGIAA GMLTELLGRV RGSS
//