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Database: UniProt
Entry: A0A165BJR9_9APHY
LinkDB: A0A165BJR9_9APHY
Original site: A0A165BJR9_9APHY 
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
//
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