ID A0A316YXY4_9BASI Unreviewed; 1561 AA.
AC A0A316YXY4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JUN-2023, entry version 14.
DE SubName: Full=CNH-domain-containing protein {ECO:0000313|EMBL:PWN93488.1};
GN ORFNames=FA10DRAFT_283131 {ECO:0000313|EMBL:PWN93488.1};
OS Acaromyces ingoldii.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Exobasidiales; Cryptobasidiaceae; Acaromyces.
OX NCBI_TaxID=215250 {ECO:0000313|EMBL:PWN93488.1, ECO:0000313|Proteomes:UP000245768};
RN [1] {ECO:0000313|EMBL:PWN93488.1, ECO:0000313|Proteomes:UP000245768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4198 {ECO:0000313|EMBL:PWN93488.1,
RC ECO:0000313|Proteomes:UP000245768};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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DR EMBL; KZ819634; PWN93488.1; -; Genomic_DNA.
DR STRING; 215250.A0A316YXY4; -.
DR InParanoid; A0A316YXY4; -.
DR OrthoDB; 5100844at2759; -.
DR Proteomes; UP000245768; Unassembled WGS sequence.
DR GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd04435; DEP_fRom2; 1.
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; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041675; PH_5.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR46572; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR46572:SF2; RHO1 GDP-GTP EXCHANGE PROTEIN 1-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF15405; PH_5; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000245768}.
FT DOMAIN 723..910
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1107..1402
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 20..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1561 AA; 171276 MW; AD92CEA38AE164B1 CRC64;
MPAGNADGPD KRTTAYENIF GRPTAKPKGP VPSAQPSMPP HVQQWVHQQA YGAQPAPRWN
GAPAGPYPPR VYGAQPYPQQ GPPMMAAGPA YGYGPNDAID RRASVTPSIS SQDPRMSAHY
PQSVGIGGGL ASGGSSAVDP YGSHNNIYQQ PSGSNNGYAP QRRPLSRGGG GGGSYSDVPP
GYRQSSAAAA APAASSDEQG MLSSPQHEPP RLPSIELGAG SGSADDHWFT NGSNGNARHS
KSSAASKAQD SVDDSETPLS PTPKQSAILS QPVHESETTE VIGENGGVDP YQLNDYQEYQ
RQTASKSGAS SLYDGNGRRR GSFESDRQSI ANSIYTLPGA VGNSSRMVYN QGGQGSYFQP
HPQQQQQQGI SALTPYNSSD ANLTWGRQAR MRTTSSATQA AQGVYAPGYA DQNTEWRKSV
ESASARQGGD NIRSLSVGQQ QIRNPANSPH GSTGSAMQQN QTSGRRGPLV YPALLSRVAE
AFKQRVTLSE RQKDGLSYTD AFDGREAVDR IAYIIKTTDR NLALLLGRAL DAQKFFHDVT
YDHRLRDSPN ELYQFRVRLT SPFGSEGDDQ YEDASDQLYK ASATPGRLSI PSSKGPTRDN
STSSVQQQDP SSPAPEVSTP ATSIPGGQGR QAIDEDVEDA LPTGVFTLLT DCYSPTCTRD
RLCYSIACPR RLEQQARLNM KPQPGLKRSI SKESLGDVKE QGALWADSVS EEVLKSLSDS
ERKRQELINE VIYTERDFVR DLEYLRDSWI KPLRSRDVVP EAKRDDFVTQ VFWNVLEIHA
VNSKLAELLS KRQKQQAVVD RIGDILLEMV PHFQPFVKYG AHQLYGKYEF EKEKSSNPAF
SKFVEETERM PESRKLELNG YLTKPTTRLA RYPLLLEAVV KATPDDNPDK QALPKVIKIV
KEFLSKVNTE SGKSENRFNL AQLDQQLVFK QGEAVDLRLR DEQRELVFKG PLKKRGGTQS
ESAELQVFLF DHAVLMVKAK TVHKNDLYKV FRKPIPLELL IVTVYDDVPT GKGNATRPKS
VMSKTSTGSR LSGGVPTGSA PKQDPKTGYA LTFTYLGRKG YSQTLWSSTF VSRKKWFEHI
ESRQEILRQR SNIFDTMTLS EGFFQGPSRV TCSVPFDFGR RIIYGADDGV YLSDLREKAR
PPTKVLPLPG VTQIDVLEEY QILIILAERS VHTFTLDALD PSDPMGSLKR GRRISSHTSF
FRAGQCLGRT LVCVVKSSSL SSTIKTLEPI EQNVRGKKQP TFRKLLQGGQ ETLRVFKEFY
IPTESSSIHF LKSKLCVGCT KGFEIVDLET LDTQGLLDPA DSNLDFVQRK ETVKPIAIYR
IDGEFLLCYD EFAFYVNKNG WRAKGNWIIH WEGNPTSFAL HYPYVLAFEP SFVEVRHVQT
GALHQVITGY NLRCLFADVP PATSGSSSGS SISSSASAHS SHSNLHSMTP YGARPGMPPG
YPSGSPYGPP GALSRQQSFN MMGGPVGPHG SPFATPRPLG TMSPYGVPPP QQQQQQQMMY
PGRPGMPYAF TQAQAPRPPP PQRNPVWESV AASRNQIVFI GDTSVFCIRP AGSSASSPAP
T
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