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Database: UniProt
Entry: A0A316YXY4_9BASI
LinkDB: A0A316YXY4_9BASI
Original site: A0A316YXY4_9BASI 
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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