ID C4XYJ3_CLAL4 Unreviewed; 892 AA.
AC C4XYJ3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Rho-GTPase-activating protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=CLUG_01016 {ECO:0000313|EMBL:EEQ36893.1};
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:EEQ36893.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ36893.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ36893.1,
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).
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DR EMBL; CH408076; EEQ36893.1; -; Genomic_DNA.
DR RefSeq; XP_002619857.1; XM_002619811.1.
DR AlphaFoldDB; C4XYJ3; -.
DR STRING; 306902.C4XYJ3; -.
DR GeneID; 8500690; -.
DR KEGG; clu:CLUG_01016; -.
DR VEuPathDB; FungiDB:CLUG_01016; -.
DR HOGENOM; CLU_008201_1_0_1; -.
DR InParanoid; C4XYJ3; -.
DR OMA; RKTWIYE; -.
DR OrthoDB; 1328399at2759; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000007703}.
FT DOMAIN 1..438
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 215..296
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 472..691
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 695..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 100385 MW; D759818C25491022 CRC64;
MSFADSFWTY DYHSGHEVLF DVLFEGVKEN EDFIQLFNRR MDSELQYGLS LENLPGQVRP
TSKRHTDDDY VSTIKNAFSK MNENFSRQGK YHIEVAQNIQ GMVLDPFSKW CKEHESRVAF
SEATIAEKFK AYKSKKTALE KLQKKYFNKC RVLEEFRSRY TDEELAEIPQ EDTSFDNSAD
NENISETENE LNENTYTFAG AVYDYKNARK LLSDIISNIE LTSHKVPILG TYHNVSSGSA
ITQWLLDNMP EYKGNIAKAE SFGQDLIENN FIRLIGSMNA SKSFINSSQF LYQWKPLAFE
FTKLYERDGS RANVAEPTTV LTKTNQFTNY FEDVKQAIGV ASVDFNDKSQ YPKLVKQVES
LDIAYFESTK DLDMTRCKFE ETVMDHLAFM QKCELDRLRA VKKVMFDFLS IFSNKWAALK
GVSDELFVVE ETIHPSSDLK FLIENYGTGR FEPRVTLYDN YYNSNIKQTF GVDLNVKARL
ERKAVPSIIQ ATLSFLDNAY PDLENDTERM NLWTEPVHLS KVHELRFKLN ELTDAAEMKD
ILKKSEPKVV TNVLKLYFME LPDSIVPHSY FDLIMTLYQN YPAESQDKNV NKSRLTGLQN
TLSELPVCSL ATLDAILTHL NRLVNIISSA NEDLGSSLRL RLCKEFGALV LRPKRDNEGA
EGKNLHSNTV AVEIIQQEFV TDLFAHKDNI FGELRRRNSN KPSRASSAAS GTGPRNSDNQ
PRVSDSTTAS NGSDAAKLRL ETKLKRAVTK AAGKNNLSSK GDNMSGPGSS SKTSSSKSPP
TTPVKSKSDL SSKSSGTGLK RSSSPNKKKL SSLIEKQSKS TGASTSSQTG NDVENETHDS
ISHENDMPDV ARLTMESSTP KKGDEGASSE SSDLPPVPPK KSSSTKEVIV VD
//
