ID B5VNQ9_YEAS6 Unreviewed; 1355 AA.
AC B5VNQ9;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=YLR371Wp-like protein {ECO:0000313|EMBL:EDZ70432.1};
GN ORFNames=AWRI1631_123980 {ECO:0000313|EMBL:EDZ70432.1};
OS Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=545124 {ECO:0000313|EMBL:EDZ70432.1, ECO:0000313|Proteomes:UP000008988};
RN [1] {ECO:0000313|EMBL:EDZ70432.1, ECO:0000313|Proteomes:UP000008988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1631 {ECO:0000313|EMBL:EDZ70432.1,
RC ECO:0000313|Proteomes:UP000008988};
RX PubMed=18778279; DOI=10.1111/j.1567-1364.2008.00434.x;
RA Borneman A.R., Forgan A.H., Pretorius I.S., Chambers P.J.;
RT "Comparative genome analysis of a Saccharomyces cerevisiae wine strain.";
RL FEMS Yeast Res. 8:1185-1195(2008).
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:EDZ70432.1}.
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DR EMBL; ABSV01001688; EDZ70432.1; -; Genomic_DNA.
DR Proteomes; UP000008988; 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; 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; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
FT DOMAIN 658..845
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1033..1335
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 74..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1355 AA; 152497 MW; 794ED4000E7635FB CRC64;
MSETNVDSLG DRNDIYSQIF GVERRPDSFA TFDSDSHGDI SSQLLPNRIE NIQNLNVLLS
EDIANDIIIA KQRRRSGVEA AIDDSDIPNN EMKGKSSNYI LSQQTNIKEV PDTQSLSSAD
NTPVSSPKKA RDATSSHPIV HAKSMSHIYS TSNSASRQAK HYNDHPLPPM SPRNEVYQKN
KSTTAFVPKR KPSLPQLALA GLKKQSSFST GSASTTPTQA RKSPLQGFGF FSRPSSKDLH
EQHQHHQHIQ HNNINNHNNN NTNNNGAHYQ VGSSNSNYPQ HSHSISSRSM SLNSSTLKNI
ASSFQSKTSN SRKATQKYDI TSNPFSDPHH HHHHHSSNSH SSLNNVHGSG NSSSVMGSSS
NIGLGLKTRV SSTSLALKRY TSVSGTSLSS PRRSSMTPLS APRPVMSASS KKPQVYPALL
SRVATKFKSS IQLGEHKKDG LVYRDAFTGQ QAVDVICAII RTSDRNLALL FGRSLDAQKL
FHDVVYEHRL RDSPHEVYEF TDNSRFTGTG STNAHDPLML LPNSSSFNSG NHSYPNSGMV
PSSSTSSLNS DQATLTGSRL HMSSSLSQQK NPAAIHNVNG VFTLLAECYS PTCTRDALCY
SISCPRRLEQ QARLNLKPNG GLKRNISMAL DDDDEEKPSW TSSVSKEDWE NLPKKEIKRQ
EAIYEVYITE KNFVKSLEIT RDTFMKTLAE TNIISADIRK NFIKHVFAHI NDIYSVNRRF
LKALTDRQRS SPVVRGIGDI VLRFIPFFEP FVSYVASRPY AKYLIETQRS VNPYFARFDD
DMMSSSLRHG IDSFLSQGVS RPGRYMLLVK EIMKSTDPEK DKSDYEDLSK AMDALRDFMK
RIDQASGAAQ DRHDVKLLKQ KILFKNEYVN LGLNDERRKI KHEGILSRKE LSKSDGTVVG
DIQFYLLDNM LLFLKAKAVN KWHQHKVFQR PIPLPLLFAC PGEDMPALRK YIGDHPDCSG
TVIQPEYNTS NPKNAITFLY YGAKQRYQVT LYAAQYAGLQ TLLEKIRQGQ AAIISKTEMF
NVTKMSDRFF DYTNKINSVT SCDGGRKLLI ATNSGLYMSN IKRQQNKDHR HKSSAFFSTP
IQLVQRNNIT QIAVLEEFKS IILLIDKKLY SCPLSLIEAE GNGTSFFKKH HKELINHVSF
FAEGDCNGKR LIVTAHSSSH SIKYFEHEHP LLAEKNGSGS GNKKSLKKKI TEVIFDSEPV
SISFLKANLC IGCKKGFQIV SISQNAHESL LDPADTSLEF ALRDTLKPMA IYRVGNMFLL
CYTEFAFFVN NQGWRKKESH IIHWEGEPQK FAIWYPYILA FDSNFIEIRK IETGELIRCV
LADKIRLLQT STQEILYCYE DYRGYDTVAS LDFWG
//
