ID A0A428R6G5_9HYPO Unreviewed; 1700 AA.
AC A0A428R6G5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Rho1 guanine nucleotide exchange factor 3 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CEP54_000538 {ECO:0000313|EMBL:RSL73129.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL73129.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL73129.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL73129.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSL73129.1}.
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DR EMBL; NKCI01000002; RSL73129.1; -; Genomic_DNA.
DR STRING; 1325734.A0A428R6G5; -.
DR Proteomes; UP000288168; 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; IPR041675; PH_5.
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; PF15405; PH_5; 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:UP000288168}.
FT DOMAIN 878..1070
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1105..1269
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1337..1646
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1646..1672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1646..1671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1700 AA; 189154 MW; 689DC8CEDA69DA33 CRC64;
MSFRGDDQRR YGHVPPVQYP VASRGQDYQQ QQQQQQQQQQ SSYDVDVARR ASFNGGDDAA
YLQQPSTRPA NGEDELFLGG APAGRSSYGS TNNSALAGYQ HQYQDAGPPT PTYSYNPQSF
AQTSGFPRSQ STNTLPYRNS QPPTRFASTA GYTPHSTYDP SAYANTNSSL QRQSSYQGFN
NTYAQGYPPQ TSPGYGQSPN STYGNAYGQS ATSPALSPGY EQPLRSPSLN SSTSGAQASA
YDHSYNQYPG SLANGAASTP SYSGSSQPPY PTTTQIPVGP YYSPIEQHNS QYTRPSRSNS
QASPMGSPSN LPQSSSPGIQ RHPTNAPLPS RPSEDSSGRW GSGQQQYQDE HVNDNLMQEL
EMELGGSGQT YRPLPEPTNG QYNDEDGQHL SRYDSNATTI PNMASRTTST RTGTTAYEPE
EDDDDDDAYG EAGLMAMRQA ELDEQRFSSA FGYTDMPAMA NPEPPVSRPL PTHPEEQAQS
SDSDYAGMDL GAFAGGFVGG MSYGNVGSPP ASSGQEVAAR PLPTPNTANR NFEAEMNYGD
TGGLKPPTEK RMSFDDDDER VSLRSRQSGT ESPNKDQLQD LFYHPGLSSR PLPAIPGPGS
DSSSLLSVQT NNRQPYQHGY SRSVGSQLGQ VDNPEAYYSS GGAYNPQPER SISLSGHSHT
PQVQPPARSR TDAAADERRR LARQSHMPQS QVFPEYETAD FGGITLPSGR KKKFVPSKLN
AADFRRCPEP WALTCLEAWI REMAEGEADL RSKTVEEALI NLFTGKIPTM NVADAEVLSN
HVITLMLERA VLVPEEEWVK FGNGHISGVL WQLTGSGCYA PKLHDEEISG RCYSYHCTRS
LKKVDLEELP DTKPADEWHI FYGLKKEDWE SKPKKEVERQ NILHEIVTGE ENYIKQLDIF
RRYYRDRLRV MQPPILKPET RDRFLYDVFG KLDTVQDINK DHLLAQLKYR QQEQGPWITG
FSDLFREWIR KAKAIYVEYA SAYPNAVYTV RREADRNLYF KRFLDEMQRH KIASKQDWTH
YLIAPIQRLQ RYILLLESVE HKMKSDSEEK TNLIKAIQEI KVVAHECDGR VAEMNKKVQM
TDLNRMIVFR PGYHHALNLE AHNHELLFEG DLQRMGSKGV RWVDTHALLF DHYLILAKTV
TPKDGKGEKK YDVNKEPISM AFLFLESRND EPVQKQKGIT APLGRTTAAS ASGTQLNKVA
TNSGRPGLEH VATSSSIGSG LTPIASNDTE GKILYPFRIK HLGHEVYTLY ATSAKDRSDW
CDKIIEAKTT YAKGQFSQNA EPFRLRVLAD AAFHYDNAST WAKTPVVPQI KGTPLDRSIQ
ELESVLGPAQ GVAPVCRAQV NCATGFTAFG KSVIAIGTDY GIFISEPSNP RGWLRTVQAT
RVTQIAVLEE FSVCVLIADK NLISYPLDAV APVNEFSAPV LSDNPRRAPQ RLAKDVTYFA
TAKMKDRMLL FYKRKEGLHT SFKVLEPIFQ KSTEKKSRLF GGRRTGGGTT ETFREFDEFF
FPTECYSLSL FQTYIAVATA KGVEMLTLDK KQPMSIPDLK EPAIANIAAR IRDQRPLGMF
RLNENEFILT YEDCAVYVDK HGEVSRTLIM EYSGKRGKAR GATMYGSYLI IFNDDYVEVR
NAENGRVRQI IAGRGVRVLD LGVRGPTGQS TLNPQSNGYM QSSSGSEGSK GTVKISMCHP
ELPGRQIILE MLLNDGHTEK
//
