ID A0A0A0HDR3_PARBD Unreviewed; 1988 AA.
AC A0A0A0HDR3;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=DH domain-containing protein {ECO:0000259|PROSITE:PS50010};
GN ORFNames=PADG_12531 {ECO:0000313|EMBL:KGM85837.1};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:KGM85837.1, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:KGM85837.1, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:KGM85837.1,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275998; KGM85837.1; -; Genomic_DNA.
DR RefSeq; XP_010764031.1; XM_010765729.1.
DR STRING; 502780.A0A0A0HDR3; -.
DR GeneID; 22588428; -.
DR KEGG; pbn:PADG_12531; -.
DR VEuPathDB; FungiDB:PADG_12531; -.
DR eggNOG; KOG3519; Eukaryota.
DR HOGENOM; CLU_001112_0_0_1; -.
DR InParanoid; A0A0A0HDR3; -.
DR OMA; DQVGWIW; -.
DR OrthoDB; 25601at2759; -.
DR Proteomes; UP000001628; 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; cd07589; BAR_DNMBP; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR PANTHER; PTHR22834; NUCLEAR FUSION PROTEIN FUS2; 1.
DR PANTHER; PTHR22834:SF20; NUCLEAR FUSION PROTEIN FUS2; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001628}.
FT DOMAIN 1202..1428
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT REGION 46..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1872..1915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..831
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1081..1097
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1872..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1988 AA; 220950 MW; 2C10800CCA8CE9DD CRC64;
MPANEVERNC DSLNHLVHSF HRQDQNPQFP SVSSLEAINS DQAFESNNDI SQSSSSLSSH
LPLLPATTYK PTGSPGSSRQ LSLTTNFTNQ HISRRHYPTS DETSPDPRDF YLQYNDPFSD
DGPAAVVNNM TSASYLRKSN VLSGCYPPNN PSLTSNNPPF SSRSHQYHSF SSFNPSRPSS
IDSSVARNPQ QRQSSLKELV DRFNQKLDPL PTKPPHSRSS SRDGSPVSCD SAYSRLSGTQ
QHTHKGDNER EDHRSPPLSR HPGRQSQRSL WLNNDSGRHS FGSPPAKQPL FGEIIPTRSQ
LRLCGQDTSS PRWRRGSDCS IHTPNPMVVN LPLDPDNTLS PTSPTAWYLG YSPSFEYFNH
TKAITHTPVA HRRFRSNLTP NLSIASSSAS KSFDSSDIKM GILVNEVTLQ PTPNTRTRII
CNSQSRIPVS TRRLSQTSDS GGSAHSTRAN SAMDRYIMHV GLPPKGSSAL PKHSSKHSPN
VKLPPTTLNI TSPSQHSWGH MPSHLTPEES PTLNTYISVP PPKKSPQLRS SRPRQPVSSA
TTSASRARVV DRISTLQNQS TTPLVDARPS KTKSRRLPEL GNVDFAARRR KIQQAFNKTV
EENAKREERA IKRRQLVEER EAGGDGSKNT QPSSLDESQV ESQLNKRNDL SRVSMESCPE
TPDICDGHDA FVTPDERRSP EVVNNVTERK ETGRHVTSFG QDNNNCSVME PVERPNENLD
VPRTRTPCSD IAPASAVTVD TDITTFDPEP QTDYHQPSSQ IHRTVLSQIM QMRESSPSSS
AYSDSFSERD DKESIQIMLG RSRYLDESQD NSRDNQDQCE AADDFRSNGD RHRWSTSSWS
SSFQDRQFIV APLEKIMKNP SDPDAHMPIS TDESSRTPQP LVSQPRADSP TTGEIEFQHC
DGDLLKQSTR PAHNVRYSTQ MMQQYPDLAK HGGWNSKRVT QLFLQELGFE GSHLLKSDFG
IATRVRTSRP PSSRGDDNQK TEVLSEDSII DPESVNVPNP EYVQYRASLN FREDWEKASP
SVAEWMHLAA SEESTGNSPS AIRDGTETPR LPVAVPKFAP TEPDEGFGLS INIQTPQDDD
SPTVRPPPLP DHSPPPIPGS RSVGAKQLHE PGVHPPVTSP PSISSNNPPS LIHPSVSVIS
TDQKLSTRCS EESSLHQSGL APSPQNLVLS ATPQDSSGVD RPSVETSVQK SFPSPEQRRL
KKRKHIIKEL VDTEHTFGQD MTVVVDIYKG TSSSCLDLSQ DDIKTLFGNS DQVVQFSMDF
QDCLKRAAKS VYVLPQSQRY KSKRGGSRLV QASGFMTYNQ ANPTSELSDG EKDSQTSIGQ
VFMENIERME KVYSEYLRNH DAANKTLEVL LRKKNVTIWL KECRDWAVDL TSAWNLDSLL
VKPVQRIVKY PLLLTELLGT TPPDHPDHAA LTNALRETTS ISVRINDMKK RADVVGQIIS
GRKRKESDVR AGLSKAFGRR TEKIKAHIGI TDMFADKEFL VLSQQFGDNF FQLQLIMRDV
ELYTTEVQAS FKRFHEYVLA IESYINVSPS NYPELESKWC QFRIAVNDVL TVALVDHVST
VRKSVILPMI TLLKLHDGPQ RVMQKRNKRL MDYVRYKTLK DRGDKADKKT IEQGEQFIAL
NVTLKEELTK LFDLTGKLTE ACLNNFVEIQ KTWLGLIEKR LGYIIERIPQ DLEHIGADWS
ADFSFSDAQV LSLGICNGSI LAEVANFAGF SPPSASNRAD GSPSRRPSTV NSANIHTAYT
TTNSNSNQST SFEQSNSPKM SYESSIGSPG SLIQSFQADS FNETHNNGAQ AFSAGRVRTN
SGFSVRMTGV SDMLNGQHVP SMTALVNNTT NAGTTYASRP SNISPSLPLL SLDPPMLQDF
LADPLLAISN NRGTTPKPAL HPSSPPTTRS DGFFSSAMPM TESPPTATPM DESEQKKDPS
VLFLVASLFE FNIDRARREA GYPYLTYVAG EIFDVIGEKG DLWLARNQDD PTRQVGWIWT
KHFSKLSG
//
