ID K0KIA2_WICCF Unreviewed; 982 AA.
AC K0KIA2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 13-SEP-2023, entry version 53.
DE SubName: Full=GTPase-activating protein {ECO:0000313|EMBL:CCH41129.1};
GN Name=BEM3 {ECO:0000313|EMBL:CCH41129.1};
GN ORFNames=BN7_666 {ECO:0000313|EMBL:CCH41129.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH41129.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH41129.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(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:CCH41129.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CAIF01000011; CCH41129.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KIA2; -.
DR STRING; 1206466.K0KIA2; -.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_303312_0_0_1; -.
DR InParanoid; K0KIA2; -.
DR Proteomes; UP000009328; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328}.
FT DOMAIN 539..649
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 784..982
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 55..82
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..185
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 982 AA; 111061 MW; DFEF4FB55074DFB4 CRC64;
MAQSSKRGSV QSGFSEFSFE HNDDALRIST PRSERPQSPT PTTSPLKFDG LIKENKDLKL
KVLEQQQLIE NLRREIQELR GSTNKGNNIN IIEEQKPISL SSSLSASPID KNQDNSSNII
AQHILVSNQS LSSLAPPPRS ANRLKTSPLR DDLESQRTPI ITEPEPEKDE KTTLDEEDEN
DDTTQREETG DNTLTNIDED LLQTPDNTNV EDDSSRRSSA YSAPPDTKLE SPEKTALAPN
SYSSPYKGRI SSSSSPLRNP PTSASNNPSN SPSPSPISPE TTQLSQPLSV VTTTTTDDKS
IHNKLNFNES RSTFQGSPLP PKNFSSSDSP FMTPELSIPP SPLEGRFTPA ESIKSNLYDP
YEGDFQHQQI HQNHNGFGGV YNGENENHEL NQLDSTHKRF PSDVPLFVNP TELSTVKTEI
ITTICGNFSK KSDDPIVIIA VCDRQTGVEM WRFKKSLSSI VLLDTQIRPL INTFSLPPVP
EKSLFLSNIP VKVDIRRLRL RDYFSTLFTI PHIPLDAAYK ISRFMSQDVV NLLDESNTEA
LKDGFLLRRS KGLGNNWKAR FCEVDGPFLN VYENKDGSLL EILKLTGSQI GRQPDHIKHT
DDKSSYRHAF AIMEPKKNLK SSSFTKHIFC AETDQERDLW VNTLIQFVED PSSSISTYSG
DSSNLSSQTI INPEPQLIPS PNSISTQSPS KSSIHTKNDD TDELEELVKE SKRNKKRSFF
PFSKKNINEE LEVFKNQQQG GTEQSSDQET SPKKSNIEES LKNMNLLDTK INEKIFNNEI
SIAINLSNHE LYGYKVPSII YRCLKFLDDS DAVIQEGLFR LNGSASMIKQ LRENFDSKYD
FELDEFELKP DINTIAGLLK LYLRELPSVI LTKELYSNFR DSYNKIKDPQ LLSIEFKKLT
QKLPIENYSL IFVLFKFLNK VIQYQEMNKM NLRNLCIVFS PTLNISSEVI IPFFVDFGCI
FENQEPIPNN QREVLDIHIP TF
//