ID A0A371DXT9_9APHY Unreviewed; 962 AA.
AC A0A371DXT9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Dbl homology domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=OH76DRAFT_1476727 {ECO:0000313|EMBL:RDX57314.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX57314.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX57314.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX57314.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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DR EMBL; KZ857379; RDX57314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DXT9; -.
DR STRING; 139420.A0A371DXT9; -.
DR Proteomes; UP000256964; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; 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 InterPro; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46572:SF1; RHO1 GUANINE NUCLEOTIDE EXCHANGE FACTOR TUS1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000256964}.
FT DOMAIN 202..391
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 426..561
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 602..912
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 962 AA; 109352 MW; 97094AE5E1653CAA CRC64;
MAHRSRPHVT IPAGAAPPLN PSPSAHDQSL SPINLWADRR NPVYTVHTPS SPSLLSSSHP
GPRISLDVPG RPPSRAASAY EYETSRLSFP EPQLHRSSSQ RTPYRSTSTN FTHRTSRSES
VLTPDGLLTP TQYSISGESS RPPSFFENTP ESISRDLSTE LTELSNVEEA LRKFQAGELP
DAEWYRLVSP SVREVLDKKE VQRQSILFEI IKSEKDYVAD LELVKEVFID PLMNTLAVPS
SRVKNFIREV FFNFDEILQH HQKMLTALFA RQREQHPWVM TVADIILDNC LEFLAGYEEY
IKHYPIAEMR HRSEMRRNTK YQYLVQQCSL DPRVRKRDII TFISRPVTRL PRLQLLLDNA
RKFTEPESQD AEDIPVILGI LNEFIRSTQP GIEAAEEKVK FWSLCESLVY QKGEIIDLDL
YDDTRSLQYQ GRLSRKYKSE MNYHWADLHV ALLDNYLLLL KPDVRSNDGR ANPPTRHHVV
SRPIPIDYLR LGMFDGPPEN RKEKAEDGGL GLLDRVRPKY RQMFPFTIYH ASSKMNRRYT
LYAQSEQVRD RWLTAFNTAL DIRRYRQEGN MFFVTHVIND GFFKQASSYT SGNFNGAGAH
FTGRINAAIK FSSTAHKFVA VASSSGVFVA QKGEPAFRKV LSVYNPTCLV ALPDVNKFFV
LHDQGLYAYS LDLVARATLG ISSTENAEAS KERIAGDVLF FRAGRVGSRP MVLYVAKSFL
QYNLYALEVV NSSDLHINPR RNTNGLFSFR AFGEPVSIPK DTLDIIMFRQ RIVICSDKGL
SLVDPTNLSL SAKSTLIPDF SDADFNNNLP MMTLKSRCAS SKPLGIVRCD SSDELLVIYD
ELGCYTNKYG VPSRSSGYLR WETKATSYSW RGEHILLFSP EFIEIRTVQT GKLVQVIEGA
DMRRVDVGLL TSDKDLTTLV AMKGREEQGL VVDTLQELVE TTEIRTTRSS EVPGMFDDFE
VM
//