ID A0A3F3PXB4_9EURO Unreviewed; 672 AA.
AC A0A3F3PXB4;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 02-APR-2025, entry version 24.
DE RecName: Full=Rho GTPase activator {ECO:0008006|Google:ProtNLM};
GN ORFNames=BDQ94DRAFT_60928 {ECO:0000313|EMBL:RDH31402.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH31402.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH31402.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH31402.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ852055; RDH31402.1; -; Genomic_DNA.
DR RefSeq; XP_026624424.1; XM_026776162.1.
DR AlphaFoldDB; A0A3F3PXB4; -.
DR STRING; 1341132.A0A3F3PXB4; -.
DR GeneID; 38144518; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-ARBA.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-ARBA.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07652; F-BAR_Rgd1; 1.
DR FunFam; 1.20.1270.60:FF:000063; Rho GTPase activator; 1.
DR FunFam; 1.10.555.10:FF:000041; Rho GTPase activator (Rgd1); 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR050729; Rho-GAP.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF136; RHO GTPASE ACTIVATOR (RGD1); 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 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 PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729}.
FT DOMAIN 37..318
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 479..669
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 138..197
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..390
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 672 AA; 73445 MW; 7AC1858F72266296 CRC64;
MADSALHDSP AHDPDAPPSS AGSTGHPGAL EPRPGPAPMS EELKGRLDKV VYSDIGVTTL
LTRLKQSVSS AKDFSTFLKK RSSLEEEHAQ GLRKLSRSLH DSAYRNENRQ GTYSQNYNEL
NRFHDRMADH GLQFSVSLQQ MADDLNELAS NIERGRKQWK QTGLSAEKRV LEAETSAEKA
KAKYESLAEQ YDRVKTGDKQ GGKFGLKGHK SAAQHEEELL RKVQNADSDY ASKVQAAQSA
RQELVSTLRP QAVQNIQKLI AECDSGLTLQ LQKFATFNEK LLLGQGLAIS PLKDGSANPA
LAPKSLYEVV SQIDNEKDFN EYVLSHERNP AAVTSDQIQY KRHPTLGGSS GPVVPASQPS
TQNKRQSMFL PQSFSQSNLL SSTPASSQPS APAPVSAPAP APAPAPALAS PPATESLPYP
QNPDSYSSPP FQPPYPTSSS EQHHLNQAPA LPAKTPLGPA GNGFQPSPNL PPLKPVFGVS
LDDLYTRDGT AVPMIVYQCF QAIELFGLDM EGIYRLSGSA THISHMKALF DNDSSQVDFT
NPENFYHDVN SVAGLLKQFF RDLPDPLFTS HFYTDFINAA RIDDDIQRRD SLHALVNNLP
DAHYATLRAL VLHLNKIQEH YTQNRMNAGN IAICFGPTLM GANSGGNIAD AGWQVRVIET
ILVNTFQIFD DD
//
