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Database: UniProt
Entry: H0GFG0_SACCK
LinkDB: H0GFG0_SACCK
Original site: H0GFG0_SACCK 
ID   H0GFG0_SACCK            Unreviewed;      2167 AA.
AC   H0GFG0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Bem2p {ECO:0000313|EMBL:EHN07438.1};
GN   ORFNames=VIN7_1435 {ECO:0000313|EMBL:EHN07438.1};
OS   Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS   (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN07438.1, ECO:0000313|Proteomes:UP000009009};
RN   [1] {ECO:0000313|EMBL:EHN07438.1, ECO:0000313|Proteomes:UP000009009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN7 {ECO:0000313|EMBL:EHN07438.1,
RC   ECO:0000313|Proteomes:UP000009009};
RX   PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT   genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT   origins.";
RL   FEMS Yeast Res. 12:88-96(2012).
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:EHN07438.1}.
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DR   EMBL; AGVY01000019; EHN07438.1; -; Genomic_DNA.
DR   HOGENOM; CLU_002085_0_0_1; -.
DR   PhylomeDB; H0GFG0; -.
DR   Proteomes; UP000009009; Unassembled WGS sequence.
DR   GO; GO:0005933; C:cellular bud; IEA:UniProt.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   CDD; cd00159; RhoGAP; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23176:SF96; GTPASE-ACTIVATING PROTEIN BEM2_IPL2; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF48366; Ras GEF; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Guanine-nucleotide releasing factor {ECO:0000256|PROSITE-ProRule:PRU00168}.
FT   DOMAIN          592..859
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000259|PROSITE:PS50009"
FT   DOMAIN          1914..1948
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          1967..2165
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          934..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1771..1827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1724..1751
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        7..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..955
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2167 AA;  245363 MW;  4D41D6BE5ADD8F29 CRC64;
     MKGLLWSKNR KSSTASASSS STSTSHKTTT ASTASSSSPS SSSQTIRNST SGASPYMHSH
     HHHGQGHSHH RGEDNNRDKR KSSVFPPSKQ YXSTSSSQVN LGMYXSDTNT RSSRSIASTL
     KDDSPSVCSE DEISNSSSQK SNAQDETPIA YKKSAHSKDS LLPSRSSSLS PPQSRCSTGT
     TLEKSLNTSG ISNNSGTNNN NSNNNNDNEQ KQRNVIHLNS ENYDTTVFKT GWVNKSHGQT
     VATNYNSSMT APSSSSSSSS QNLRNDAYSR NRESRFYGND GSSLKNDDSS STTATNSGND
     VASARSSMAI DPQMLVPDYR LYRAQLKGCV LNLYKSGLNS NIKFFDPTLP ASNSSIANEN
     HRQKKQQTNS QAQAEALHQK QSFGQMGEPI TLDLKYLSEV YPHPDLRQDS DGKIISGTIE
     SLCHTVLFYP GPKQSDVPNE KSLSKTHRAV INLLLMFPLL DHFIKFLKVF NQFGLSFTKN
     KSRLTNNSTQ FYNISPAVDD SMTQRLALTA KTILDVFPGF LLDEPMLKTI ISLLDTISSH
     NDEISNNLKI KIANKHNELM KLTAFTRSLP MATSSTHELE IILDPSHFLS LDITTLADEV
     HHINLKFDKV WAPKFDYSLL YDSKFINRRI VSLNPLVFNN DQNIHFLGRL LILHLFPTNP
     EFSKKVTPKV RAELLDKWVQ IGCRFEHLGD MVSWLAVATI ICSIPVLRSS SWKYVPDQSL
     KTILKDWVPT IIQLERRQRT SKSTSSVFIL APPNLDDDFT RANVISYFGD LLIHADDLPS
     DTKFKYLEKK INRTKNAFHK WQQRLQAIDS TRHKTSSTEN VRDNDSPNNV VYQLWKFHLS
     QPPLNIEGIM KLSVQHEPPI IDQKAYSTIG SQRSALVTGS YLPILFNELF PNYSLFPKNT
     LVGAASDAKL PPPRSSARLS KSLSISEPIP IASKSHTTGS LTDDAMSSKN DNNKVTGVGK
     IDGPVIKEMS SKQSNKQRLL KSVRDVFNID MDVFHISDEL VFKSVYDNDG KSRPASMVIE
     TPKRFSQHSS MLINNPATPN QKMRDSLDTT GRLSKTLENM DFFNNIGQVS DSLKESIIRV
     VLKSSSLEKI FDLLVLTSNI FSKLVDTKDL ENYYYHQRQR GHSTRGLSDD NIGLLDYAFV
     KLTMDNDIFT ETFFNTYKSF TTTTTVLENM AKRYVGAKSC SVSISKILDR SDDSKMKINE
     DTNLVSSSLY DQNFPVWDMK VTDDENINLI YMAKIQIGAA EAILHLVKNH YSDFTDDLCN
     NSTLLDIIKI MEQEVSTEWP TRIANSKLQK SLPENFVIET ENLLTTLTDL FHGIKSAYQK
     QLYRPIGVNR TQKRITDILN SFNTFSFTDL NNIIDDPSFS DDMIRSFQKL HSTNYEDILE
     WIYQLDNFIS KKFNLVSKKD WIVLFQELEL LSKESLVSFF NYPLHFKSSK LINPGYLQLH
     EFEISNLFTW ISTLILKDDN GTESLFFEKL PQSIKLLIKL HTSLTTFFVM EISNVNKSSS
     ERLTTCKVIL QILNYIRWKN GSLDLFDSEE DESPHAICPH IPAFIETAIA HAIISPESRN
     YELSWIKASE KLSDPTKGTQ NLRSISNVLE KIDDIHIKRF IEIDDVFSKN CKNLCPCPGW
     FISRLLEISQ FVPNMSITNS KLINFDKRRF VNNIISNVLD LIPNEREFPL DIEMSDENPS
     KRTTFGRILF NNFEDVNKVY RKKTKKVSES EAISERFQEQ GVFNEILVNE IEKIKREARK
     LEVLLDQEKI LKNSAALHQA VPKKNRKSVI ISGTHSDNDH SYNIXKNTGQ TPSLGSVMES
     NNSARNRRDS RASFSTNRSS VVSNSSHNGV SKKIGGFFRR PFSIGGFNTS SSNYSLNSIL
     SQEVSSNKSI LPSILPEVDS MQLHDLKPSY SLKTFEIKSI MEIINHRNIP AYYYAFKIVM
     QNGHEYLIQT ASSSDLTEWI KMIKASKRFS FHSKKYKGKT HNKIFGVPLE DVCERENTLI
     PTIVVKLLEE IELRGLDEVG LYRIPGSIGS INALKNAFDE EGATDNSFTL EDDRWFEVNA
     IAGCFKMYLR ELPDSLFSHA MVNDFTDLAI KYKAHAMVNE EYKRMMNELL QKLPTCYYQT
     LKRIVFHLNK VHQHVVNNKM DASNLAIVFS MSFINQEDLA NSMGSRLGAV QTILQDFIKN
     PNDYFKQ
//
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