ID A0A165P303_9APHY Unreviewed; 1068 AA.
AC A0A165P303;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Dbl homology domain-containing protein {ECO:0000313|EMBL:KZT67698.1};
GN ORFNames=DAEQUDRAFT_766865 {ECO:0000313|EMBL:KZT67698.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT67698.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT67698.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT67698.1,
RC ECO:0000313|Proteomes:UP000076727};
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 {ECO:0000256|ARBA:ARBA00004496}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KV429073; KZT67698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165P303; -.
DR STRING; 1314783.A0A165P303; -.
DR OrthoDB; 1423507at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR PANTHER; PTHR46006:SF7; DH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46006; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR AT 64C, ISOFORM A; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076727}.
FT DOMAIN 280..683
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 1..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..751
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1045
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1068 AA; 115987 MW; 01E9379BD51D5AB8 CRC64;
MKAFFNRIGF TKERDRDRTD VLREKIPQLP PLPDWPPQRS TATPTTLDSS KPLPELSDRN
LPPPPLDEPD ASTSTESSAT PTPTATMNHL HPVDPPLEDV SNILGKHESV GSSGTARQDP
DSAGRSSRKT TNGSMSNGTT SDIQKKVAFL SPPPTPAPAL GSLPETDSSA GLSAAPAKST
VSRFQATHAK DTRGSTSTAA SSKTDVASTA RSTRQASTRP APSPFTHRSY NDGASIHQSL
RSGTPYSQMT NASSRILLAQ SWSEVAEEDL VSNIGQRERT RQEVLWEIVA SEERYVNELL
KLKETFIDPL LHPYSASSPI ASPTPLDYEE YPRSDTPRES LDHLPIAARF LSPTGSRTDS
PTPQVNASPP RKDDGHPTID GESMNSEEEG EADDQMGATY MSRGKNVSGM SQTAKHNHPR
SPYNSRSTGG KFGTSLPFPS RSHQSLPPPT RGQNGAASTH SLGRQSLMAE RDRDHSGESS
AHSTRAPTTT SGGNVLRRFK RSQSTAPETV VNGAVPPREL PEDLRKCLEV IEGGILDGHM
KLSENLRKRY EEQYPLVRSL ADVFVSNSHI LHGYATYVLH LERALEQVDN ALSTACASKK
PKKQDADQWV KVCQSLQRLE VTASDKGETG LAISLSKPFQ RLLKYPLLFQ NLLYHTDPST
FEYESTLGMV AEVEMIVRSI EDEKIQKEER DKTRDVFARI EGLDKVKQLM VPKPSRVLME
ERPVGGLHSS ADASVKPSSS PPTSSKGVKG KTSFKRLSDV LQPSGGGIGG KKDQWLVVFN
DVVLRCQRTG TTSLPLVAST NSRTNSLPEL QGKAKYATTG RRNVHTKPRN LYKFLKIETW
AIGDVVQPRE GVVSMEDVVR SRAQVHSGVQ PRLVPMPDDN DEPANDSDDS DRKSKMSFSY
WGADKVTVQK PIKPRQLAAS VARRGAAGSP TAYGRESSAN AKFGTRMMAA ESPSGGARPA
SRRTQGTPAG GRRQAHSEED HTVRATVTKA TVTKERPAWV GNARATTTTP VQKRPRNTSQ
TSAATRTTTA TTTAAPKQLS SPAPSEDSGV GLYRQIIAQN PSLNALNA
//