ID W7LJ76_GIBM7 Unreviewed; 1236 AA.
AC W7LJ76;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Rho1 guanine nucleotide exchange factor 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FVEG_02258 {ECO:0000313|EMBL:EWG39428.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG39428.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG39428.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7600 {ECO:0000313|EMBL:EWG39428.1}, and M3125 / FGSC 7600
RC {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [2] {ECO:0000313|EMBL:EWG39428.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=7600 {ECO:0000313|EMBL:EWG39428.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS022243; EWG39428.1; -; Genomic_DNA.
DR EMBL; DS022243; EWG39429.1; -; Genomic_DNA.
DR RefSeq; XP_018745619.1; XM_018889468.1.
DR RefSeq; XP_018745620.1; XM_018889469.1.
DR AlphaFoldDB; W7LJ76; -.
DR STRING; 334819.W7LJ76; -.
DR GeneID; 30060480; -.
DR KEGG; fvr:FVEG_02258; -.
DR VEuPathDB; FungiDB:FVEG_02258; -.
DR eggNOG; KOG4305; Eukaryota.
DR OrthoDB; 5100844at2759; -.
DR Proteomes; UP000009096; Chromosome 6.
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; IPR001849; PH_domain.
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; PS50186; DEP; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009096}.
FT DOMAIN 367..442
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 538..729
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 674..891
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 913..1206
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 140269 MW; 6C8A09D4B151955D CRC64;
MSNYGYDPRG APQRPPQRGY GDDNNYGQRD AAFSNIFGAA PPPGRSQTMT SSSSMPQNMM
DPGRTQTMSS MSSGMQRQPP PRAPPGHYGD PAAGRTRTMD SNSMMGNGYY PSQRSASGGQ
MPSHYMQQQQ QHQQQRRPYP GPGGPPPPRM EQRGPPPPQA PGARTPAQRF YQGGPAPSMN
NDPYRSQSLA SAPRQPMYHP PPSAYQQAPA NHLRQAPYAQ QNSARTTAQG RIVPERHEDR
TMSLTGNYQP QSMDAHQTMS GRVIPNRRAP TELPTTNGYP NSMPHAPGAQ TRTSSMVSSN
GAGDYSRTMS MASTVAPTIT PSESDASTLV QRPTRSKSIE SERPPTATKI RPPLVYPALL
SRVGECFRRK IIVGDRTKNE LTYKNAFSGS EAVDVLSYII RTTDRNLALL LGRALDAQKF
FHDVTYEHRL RDSQSEMYQF RETLMDEPED KPAVNGVFVL LSECYSPTCT RDQLCYSIAC
PRRLEQVSRL NLKINPGLRK EDAVNAVDDE GDQTDEQKLW INSVPKEVAE KVDEREKKRQ
EVISEICYTE RDFVKDLEYL RDFWILPLRS KASPVPVQRR EKVVKTIFSN IIDHPSIHTV
SSRFASGLTT RQQKEPIVHN IGDIFLEYVP QFEPFILYGS KQLEGKFEFE NERSVNPYFG
KFVDEIERRK ESRKLELNGY LTKPTTRLAR YPLLLENVLK YTEDGNPDKE DIPKVLVMIR
DILGRVNAES GKAENRFNLR RLHEQLRFRP NERVDLRLTE EGREMVFKCQ FKKSPTDPAE
ITAFLFDHAV LLVRIKQTGK TEEIKAYRRP IPLELLAIRE MDEVIPKDGN MKRTSSSLIP
SIRNNANDPA RKEGWPITFR HLGKAGYELT LYASNQAARQ KWLEFIHTAQ ERLRSRADFF
NTTVISSKFF AGTNRVNCVT PFDGGRKLLY GTDNGVYLSD RKVKDQVPRR VLETASVTQI
DILEEYQLLL VLSNKTLQSY PVSALNPDEP ALSRRPKKIQ NHCSFFKTGI CLGRHLVCCV
KSSALSTTIK VFEPNDAMTK AKKQKGIGKF MSGGHDELKP FKEFYIPTES SSVHFLKSKL
CVACARGFEV VSLETLETQS LLDQADTSLD FVARKEGVRP IHIERLNGEF LLNYSEFSFF
VNRNGWRARP EWRIDWEGTP QSFALSYPWI LAFEPNFIEL RNMENGAVHI VPRKNIRMLH
SSTHEILFAH EDDKGDDVVE AIDFWKSNRK SELLGS
//
