ID B0E6W9_ENTDS Unreviewed; 935 AA.
AC B0E6W9;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=T-cell activation Rho GTPase activating protein, putative {ECO:0000313|EMBL:EDR29710.1};
DE EC=2.7.11.1 {ECO:0000313|EMBL:EDR29710.1};
GN ORFNames=EDI_251460 {ECO:0000313|EMBL:EDR29710.1};
OS Entamoeba dispar (strain ATCC PRA-260 / SAW760).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370354 {ECO:0000313|Proteomes:UP000008076};
RN [1] {ECO:0000313|Proteomes:UP000008076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PRA-260 / SAW760 {ECO:0000313|Proteomes:UP000008076};
RA Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.;
RT "Annotation of Entamoeba dispar SAW760.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS547933; EDR29710.1; -; Genomic_DNA.
DR RefSeq; XP_001734129.1; XM_001734077.1.
DR AlphaFoldDB; B0E6W9; -.
DR EnsemblProtists; EDR29710; EDR29710; EDI_251460.
DR GeneID; 5879026; -.
DR KEGG; edi:EDI_251460; -.
DR VEuPathDB; AmoebaDB:EDI_251460; -.
DR eggNOG; KOG4724; Eukaryota.
DR OMA; SNMSCHL; -.
DR OrthoDB; 11483at2759; -.
DR Proteomes; UP000008076; Unassembled WGS sequence.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) 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; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23179:SF3; RHO GTPASE ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR23179; T-CELL ACTIVATION RHO GTPASE ACTIVATING PROTEIN-RELATED; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Transferase {ECO:0000313|EMBL:EDR29710.1}.
FT DOMAIN 311..499
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 615..791
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 45..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 935 AA; 108132 MW; CBF29FA9A6906E21 CRC64;
MSSHNQSPGV DQLLVTAVRR PKPMQHNNNS VKQLSEDILL ELRKKKGEKT PRTRRRTLAV
DKKSVASEND QSESEESIIQ NIANEIEALQ NEIKVARDKC LKIMEGQQQF KILIDSLSNQ
RKVVLDMKEN LRDITIRDVG SRSDVEECSE FMGELYLKCF DQFNEQIRST EGFYETIKKY
IDSCSNFTRA RNDFDKLISS YATVDMKLQK MNKEKRPDIN KVGQLQQQKE ETFNSIKSEG
EKVTDFYVDL YNEFLTIMLH TSVDLSDKVS KGLTSTKRMF KDKGEKLNLW KTLNIGEAVK
NADVEYPQWM DDDPLFINIF EAENHLVEKM EYCVVKYAKS LLCNPTLATT GMSMADVNLI
FTEIESIHSL HHSIFTELKN STIDSFIDAF AKRASQLYDV YKRRCAHFKD SMKKYNKCLQ
IEAFKDAIES IDNSNLSQPR LEELLHLPFI HLTQLVPLFN SLKDDFSEET DKTEKLEELC
FIFTSLSLLS EQAEKENDVE TQLSKINGLK GISFSPKRKY LDRQQCTYNK TQGTMFLFND
IFIFTKPERN EYIFGSVIDV SQMVSFRVKN KKVVALEIKN ETCDIGFKDT QTAEKCAKYL
NSIKYEMDRK KIFGTEIKSS VIAREEENTL IPSVIHKIFD KLEKEAPDTE GIFRISVSVK
DLEETMTKID LDVNIDVSNM SCHLLGNVLK KYLNLMPNKL PISLQTVDVD NIKAIQDILE
PVGKSYLLLM ERLFRLLQMI DKNSGVNKMT ADNLAKVICP NIYEEDDDFG MNIEKLTRTA
IVMIQRYDEI FGDFRSAIEK KIQEGMQEIN HQKELEAKIQ SEDGFKEIPV SKLVEGHQDD
KTVVLTLKDI IKQGDVEMLE GKKWGKKWVV MKKNCLMIFR NIGEGQTLMV LPFKNMIVAT
ETKMNRECII LRVEKQSVTL YFEDPNEWLQ LFSSF
//