ID C4YA35_CLAL4 Unreviewed; 1019 AA.
AC C4YA35;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=GTPase-activating protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CLUG_04973 {ECO:0000313|EMBL:EEQ40845.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ40845.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ40845.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ40845.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408081; EEQ40845.1; -; Genomic_DNA.
DR RefSeq; XP_002614958.1; XM_002614912.1.
DR AlphaFoldDB; C4YA35; -.
DR STRING; 306902.C4YA35; -.
DR GeneID; 8495357; -.
DR KEGG; clu:CLUG_04973; -.
DR VEuPathDB; FungiDB:CLUG_04973; -.
DR HOGENOM; CLU_006138_0_0_1; -.
DR InParanoid; C4YA35; -.
DR OMA; DSAKHEY; -.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000007703; 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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like 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; IPR001683; PX_dom.
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; PF00787; PX; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00312; PX; 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; PS50195; PX; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007703}.
FT DOMAIN 455..575
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 577..686
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 809..1019
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 113741 MW; E1396B9667103991 CRC64;
MRPNITVNDE DQSQKSFKGR QRSQRMRSNI RPSDPQFDRS RFSDEEYIDL LLSEIKELHA
TISDFTTKSL KLETLLKEHD ILIPTDSEIL TPAAELKPTV SVDEDDVPQR SARRKVSCHE
ISENPNETNV TPDRAFSNSN EDLTIDGASS ITFNGRVEDG VPLSSTMKNE LSATLSNSSR
SRFQTTDSDI ISSNGTRSVL GDDVTAADES LQKKKDVPEI LLSPLARHSS MTSTISDVSQ
SSTKFGSAST IISHKSGQQA SINTSQSKFS REKLREGAHG VIARNYASLK STESFANSTL
SPQKNITGTK SSDDSRNQTQ STPLALTSER SSLMKESSQE VKIPSTPDAF SSNFSSNTHN
GSLKSDFRTQ GSYDFQNGLD FSSFTSPSKS SYSARSNSNL DVAKTPISHV FGSTDSFSSP
KKSSRTPGSS FNVLHTPKVE EEIPLFIQPE EFYNINIKVV STIPTNSKKL DDPNCTFAIT
DKESGKEMWR VRKTYSQIAG FDSEIRPIVE FFGLPPIPER SLFSSTTPSK VAMRKQALQE
YYNTIFLMPS IPQVVLQRFC RYISLDFVNP LDDFKSGARK EGYLIRRYKS LGTAWKIRWC
QVDGPSLEIY DSPGGTLLEE IGLTGAQIGR QSPDTVAEER GYRHAFLILG KSKGNKLSSS
TPKHFLCAES DEERDEWIAA MVEFTENDPL KSDPSQVENE YHSRSLEPIS VEGDTPTQLM
SPTSKFGTQD TLGFNGGLED WNAKDHKELK RAKMRSIFSF KHRNPVQLDD SNESETQGPP
NANTADTSMN AYLSQMSLLE EPTRRIFGRD LAEAYKLSNH SLNGHSIPSI CYRCVDYLNK
TGAIYEEGIF RLSGSASTIR QLKETFNSSY DLDLFSSPLK PDMHTVAGLL KTFLRELPEP
ILGEKAYNEF QVYVTNEGSN LSKSALALKM QEFLRDPVNI DSIHYDSSFT IFKLLKSVVD
QSSMNKMSLK NMCIVFVPTL NISVEVLSVC LTDFDCIFGE ALPIPDKDRE RMDLQIPFY
//
