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BEM3_ASHGO
ID   BEM3_ASHGO              Reviewed;        1013 AA.
AC   Q74ZH7; Q9HF64;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=GTPase-activating protein BEM3;
GN   Name=BEM3; OrderedLocusNames=AGR230W;
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].
RA   Wendland J., Philippsen P.;
RT   "Isolation and characterization of the Ashbya gossypii BEM3 homolog.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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, AND SEQUENCE REVISION TO 61.
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 CDC42 and less
CC       efficiently for RHO1. Negative regulator of the pheromone-response
CC       pathway through the STE20 protein kinase (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AF210624; AAG41239.1; -; Genomic_DNA.
DR   EMBL; AE016820; AAS54720.2; -; Genomic_DNA.
DR   RefSeq; NP_986896.2; NM_211958.2.
DR   AlphaFoldDB; Q74ZH7; -.
DR   SMR; Q74ZH7; -.
DR   STRING; 33169.AAS54720; -.
DR   EnsemblFungi; AAS54720; AAS54720; AGOS_AGR230W.
DR   GeneID; 4623198; -.
DR   KEGG; ago:AGOS_AGR230W; -.
DR   eggNOG; KOG4269; Eukaryota.
DR   HOGENOM; CLU_010436_0_0_1; -.
DR   InParanoid; Q74ZH7; -.
DR   OMA; NNHIHSP; -.
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:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:EnsemblFungi.
DR   GO; GO:0030010; P:establishment of cell polarity; IEA:EnsemblFungi.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IEA:EnsemblFungi.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:EnsemblFungi.
DR   GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0031106; P:septin ring organization; IEA:EnsemblFungi.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 3.30.1520.10; -; 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF64268; SSF64268; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTPase activation; Reference proteome.
FT   CHAIN           1..1013
FT                   /note="GTPase-activating protein BEM3"
FT                   /id="PRO_0000056727"
FT   DOMAIN          555..662
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   DOMAIN          799..1013
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   REGION          90..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          282..301
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          307..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..421
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1013 AA;  111660 MW;  4D24D96D01262083 CRC64;
     MGDGSDAERS GGTSSSSALE LLAQYEQHIM ERGRTLEAIE GHGGERLGPT YEELVEENVQ
     LRRELQGQRE EIEHLRKTIS LLASGRSGAT VVEQQVRPEP SPSVRELALP PRSADRRKNT
     KNLSLAPVGH EVPSTDRLRV SPQEATSGAQ QVPLLTSSKS AEILVSKSPD EDRHLMSPRK
     TISRSSSSYS NTLGSPATSV LYKNSRISIT SPCKSNSTSK AASVLSLPEN NTSTENAPHS
     PHRIDNELDL LTVEPQDGSR YDTERAGGPG PLSPESIVYS DSDLQEHQPS DLSSTTRTDL
     GKFRDMVDTT FNAEDNPTGS RDKETGTEME IATLQNTPSR QHESSLVTSP QASRSSITTP
     VVDPTNTSEP SSLSAAKFGS MSTATSSNKR SKGMGTPSVE HSAKSYSQHS GSPHSNSHQS
     KKADIPLFVQ PEELGTIRIE VISTLYHEPG NAASILFSVV DKKSSKEMFK FAKTFTRIAE
     FDTFIRNNME SLAVPPLPDK HMFASNVPVK VDSRREKLND YFASLLYLSP LPFNPALKLA
     QFISTDPVMN PITGEFAKEG MLLVRKSKTL GSTTTWRIRY CTVEGSIMHL HDHMIDTDTI
     KLTHSTIELQ ANLPDDKYGT KNGFILNEHK KSGLSSSTKY YFCAETPKER EQWISVLTTL
     CDGPGGTAAI PSINSKSEAS SLFEQTSISD SSYLGPIANL EAMDATSPTR PNDPNPVSLT
     SEEEKEVKRR RMKSFFPFKK LATTPTPYAA GNDNASIFSQ DDDSPVNATN ESGISRSLQS
     MNLQAQYNAV FGADLRSCLQ LSSHPYQGKY EIPSVVFRTL EFLYKNRGIQ EEGIFRLSGS
     SSLIKSLQEQ FDKEYDVDLC NYNDKVSVTP GNENQGGLYV DVNTVSGLLK LYLRKLPHMI
     FGDAAYMDFK RIVERNGDDS KLIALEFRAL VNSGRIAKEY VALMYALFEL LVKITENSKY
     NKMNLRNLCI VFSPTLNIPV NILHPFITDF GCIFQDKAPM ENGPPVNIHI PQI
 
 
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