BEM2_ASHGO
ID BEM2_ASHGO Reviewed; 2071 AA.
AC Q9HF75;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=GTPase-activating protein BEM2;
GN Name=BEM2; OrderedLocusNames=AGR144C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=10751152; DOI=10.1242/jcs.113.9.1611;
RA Wendland J., Philippsen P.;
RT "Determination of cell polarity in germinated spores and hyphal tips of the
RT filamentous ascomycete Ashbya gossypii requires a rhoGAP homolog.";
RL J. Cell Sci. 113:1611-1621(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: GTPase-activating protein (GAP) for RHO proteins. Required
CC for polarized growth and maintenance of cell polarity.
CC {ECO:0000269|PubMed:10751152}.
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DR EMBL; AF195007; AAG43463.1; -; Genomic_DNA.
DR EMBL; AE016820; AAS54634.1; -; Genomic_DNA.
DR RefSeq; NP_986810.1; NM_211872.1.
DR AlphaFoldDB; Q9HF75; -.
DR SMR; Q9HF75; -.
DR STRING; 33169.AAS54634; -.
DR EnsemblFungi; AAS54634; AAS54634; AGOS_AGR144C.
DR GeneID; 4623112; -.
DR KEGG; ago:AGOS_AGR144C; -.
DR eggNOG; KOG1450; Eukaryota.
DR HOGENOM; CLU_002085_0_0_1; -.
DR InParanoid; Q9HF75; -.
DR OMA; LEDDRWF; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0005938; C:cell cortex; IEA:EnsemblFungi.
DR GO; GO:0005934; C:cellular bud tip; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:EnsemblFungi.
DR GO; GO:0044879; P:mitotic morphogenesis checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:EnsemblFungi.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR Gene3D; 2.30.29.30; -; 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 Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF48366; SSF48366; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation; Reference proteome.
FT CHAIN 1..2071
FT /note="GTPase-activating protein BEM2"
FT /id="PRO_0000068857"
FT DOMAIN 471..738
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 1751..1853
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1872..2070
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1702..1738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2071 AA; 232152 MW; 1CBA152E9AB8A148 CRC64;
MPLKWAARNK KPPSAPQSCA SKPSSASQSS CVDERISATP RSSISSNSSP NSKNNMSRHS
HSNGSVYSDE TTLKTAQTHY TQQGQQAKPQ QHTQQQQQQP QTPMQLQVPT GQAHKRTLTC
EDMKAGARCE EQVSPCSQPA GSPVRRGGGL NGETYDGTVF RLGWVNKAQG AAPAREGRYS
HQPTASLSSI GSERPHFTGG GTSGYQYVAT AYRLHRAQLK GCILNLYKSG LTNVKYFDPA
LEPSAAALQM HQERQEMPLL QPPLPSEAVP APSILEASME SGELRLEYLS EAYPHPDLQL
DKKDGKILSG SLESLCHAVL FMPTTDAKRV TDILLLLPLL DDFTRVLNYF NLFGKVFSKH
HPAGAAGADD LNQNYNISNE TDRQLTLRLA TVVQTVLDMF PGFLLDDKIF QSLVILLDTI
SFHDEDTSQE LKVAIAEKQT VLVKLTGFAN EPIQSAKLDV LIKVQSFLKL DTEKVANQIH
KINLTFNRVW SPQADYSLLY DSQYTQKHVE LNPLVFFNDK NVQYLSRLMV SHIFCEETGF
TPKKRAEVLT KWVQLGCKFE RLGDMVSWLA IATVICSIPV LRLTRTWQYV PDSYLKIIFK
DWVPTIVQLD RRQMSSKSMN SVFILAPPNL NDAFVRDNVI PYFGDLVIHS DDLPRDSKYK
YLEKKIRRTK NAFYKWQQRL DQAFAQDRDS ASSFTDSLHL DEEEHDVADF YQYWRFHMNL
PPMNIETIME MSLKMEPPSI NQQTYSKTYS TRSALISGAY LPTLFTTLLP SYSLFPQELL
IAAASTPSTK NNNSSQASNR ISQLSVNSTP HSNASSSSAA SAVTGIDNID VPITKEISSK
LSNKQVLLKF IRDMFNVDIN VFHISDDVIF KSIRDYEAKS RPTSVVIESP KRLSLLSSVS
PDVSAVSSAL ENLDLFKNFN SSSDDIAEFT VQVVLKCASL EKIFDILVLT SRVFSNLVTT
TDLVSYFNSE KARREKSGAQ HNGQHSIGLL DFALISLIMD NELFAETFFN NYKSFTTTLC
VLENLAKRFI GAKSSAISIS LINKLRNSES SRQIPPSTTS NQFSASGIFK PSYDELKFPV
WDLKVTSVEG CPLDYLAKIQ IGVLESLYHL IREHYADFTD DLANNKTFLD ILKIINQEVY
DEWDKRLDDL RNNNNSSQKR KNSCDDNSSA KITFHVNDAR PENSNENKRG AATNLGDSSL
AALEKLQCTL QDLYVKIKSS YQRQLYRPLG VTRNCRKVHD MLCQFQPQTS MSALIMNGSS
DTLDKMVTEF QALKHTDYDD IINWIYKLDH FITSKLKLVS NQDWIQVSQI LESLSNDSLV
ALFNYPLHAE SNNVIASGSS QLDDLQILDI FTWLSTLESG SAHIIDKFPA SVQLIVRLHL
SLTKFFTVHI AHLHSTYEAR VNTCSLILEI LNFVHVKNAN VNLFHSDDAG EGSMATISPH
VPSFIETAIE NAIISPESRF FEVSWKQAYK TISEKDEKLT FIGSVLTGLD KSTAHFLDAD
NRQPVRPKNF SPCPGWFISR LLEITGLVPN MSIENSKMIN FDKRRFINNI VINYQDLIPN
TEQLPSHDDE KSAHQFGSIL FHYGTESSIK AFRKASKEAA SNEARKLKFQ AMGLFNDILV
TEVYKVQRDQ KKQEQLTVQE HEAKRSVLIQ HPNKVSVSSA SSSVSGSSSG STARTSNPAH
AAYALNMAGS LSISAARHGR SSVSSRSSVI SNTATATSPA SGASPNQTST SHHGGMGKKI
GGFLRRPFSI SGFTSSSSQY TTTSVVLSGV QANGSISPYE LPELTSEIQD TKIVTVIKTF
EIKSCIQINN YRQDPDMMHC FKIVMEDGTQ HTLQCMDDAD MHEWMKAITL SKRYSFHSKR
FKGKTSNKIF GVPVEDVCER EGALIPNIIV KLLDEIELRG LDEVGLYRVP GSVGSINALK
NAFDDEGAVH NTFTLEDDRW FEINTIAGCF KLYLRELPES LFTNEKVDEF VNIMTAYKNH
EVDLSQFQNG IKTLLSTLPV FNYHILKRLF LHLNRVHQHV ENNRMDASNL AIVFSMSFIN
QDDLASTMGP TLGLLQMLLQ HLIRNPEHYF T