ID I1BL75_RHIO9 Unreviewed; 966 AA.
AC I1BL75;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=RhoGAP-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=RO3G_01659 {ECO:0000313|EMBL:EIE76955.1};
OS Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE76955.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE76955.1, ECO:0000313|Proteomes:UP000009138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC {ECO:0000313|Proteomes:UP000009138};
RX PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT whole-genome duplication.";
RL PLoS Genet. 5:E1000549-E1000549(2009).
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DR EMBL; CH476732; EIE76955.1; -; Genomic_DNA.
DR AlphaFoldDB; I1BL75; -.
DR STRING; 246409.I1BL75; -.
DR VEuPathDB; FungiDB:RO3G_01659; -.
DR eggNOG; KOG4269; Eukaryota.
DR InParanoid; I1BL75; -.
DR OMA; MANIHIK; -.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000009138; 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; cd13277; PH_Bem3; 1.
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:SF140; ATYPICAL_BCR PROTEIN KINASE; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT DOMAIN 226..345
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 351..461
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 699..897
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 81..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..59
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 463..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 108013 MW; 8C7D084990FCC703 CRC64;
MSSVNFGQDE ITHLRSQNDQ LWKIIEKQRV MIQNLQKENA RLSADRDGLV DKVTSLEKEI
TRKQRVTSLL ISPQTLQEIA EADDNLSTPS DVELPLSPMP PPRSPYRPLK EKNDVMEEDL
SSPASPAPGP VRKDSAPLPA KSPVVVPTAS KSSSSLDNKS RRRESALPPA SPPLPSPAVR
GRPTKRESAF LNRNEIHQAI KNMSSPNLTY HQEKSTEDNF MGNMANLHIK VVGSTIKPND
KGKEVVSFIL SIGSHHDEFE EKWRVEKLYS DFLTLDSKLK AQLNNRSMTA RMGKLPDKAL
FSNNAPSKVD QRKIALEQYL QHIISLPLED TSDICEFLST GILDTANHQP SGQKEGYLTK
RGKNFGGWKT RYFVLNDYTL DYYESKEGNQ LGSIRLTNAQ IGRQMPGSTP AVEEYNSIYR
HAFLIVEQHK TGSSHYARHI LCASSDDERD EWVHALLQNI QMEDDDKKKS KKSGEKPRKL
SKGEIRAISA QPMSQVKLEN AADIEKFNAM VPSVNVEDSN LSIPPGHPTP SISSESSDSL
TLNGGDIPRA SLDQTNRGLH APRPPIVRRS SMGNLVSEQP SPFDHHQQSR PQRAASPTII
TSTVDDADQE KKARNKAHRM TFWGKKMFSS SNNANDLQQL PKFSTESDTK ASMSSSTSSS
TNTSSGGLRG FLSRSSHEQA ERQKAKQEET KPTKQVFGVA LDEAVRLSRI SEGYELPAVV
FRCIEYLDAK DAVLEEGLYR LSGSNSTMKA LKEQFNQEGD VNLLAAKNEY DVHVVAGLLK
MWLRELPTSV LTREHRMDFL HVIDRKDRVN ELGRLVSLLP LANYTLLRAL TAHLIRVVKH
SDVNKMTMRN VSIVFSPTLG IPATIFNLFM SEFEYIFWTT ENGDAAPRMI EDKEESVAVP
PATGLSRKTT LRLVREEHGR SNRNSVNYMD GAPNAIVDLE KNMDGPPVLD EDEDEVDDLT
LNDSSY
//
