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Database: UniProt
Entry: A0A1V6PIB3_PENDC
LinkDB: A0A1V6PIB3_PENDC
Original site: A0A1V6PIB3_PENDC 
ID   A0A1V6PIB3_PENDC        Unreviewed;       885 AA.
AC   A0A1V6PIB3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PENDEC_c004G06162 {ECO:0000313|EMBL:OQD76603.1};
OS   Penicillium decumbens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69771 {ECO:0000313|EMBL:OQD76603.1, ECO:0000313|Proteomes:UP000191522};
RN   [1] {ECO:0000313|Proteomes:UP000191522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11843 {ECO:0000313|Proteomes:UP000191522};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD76603.1}.
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DR   EMBL; MDYL01000004; OQD76603.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PIB3; -.
DR   STRING; 69771.A0A1V6PIB3; -.
DR   OMA; RKTWIYE; -.
DR   OrthoDB; 1328399at2759; -.
DR   Proteomes; UP000191522; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd04399; RhoGAP_fRGD2; 1.
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   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR036388; WH-like_DNA-bd_sf.
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; 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:UP000191522}.
FT   DOMAIN          2..433
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          212..296
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          467..665
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          675..885
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..746
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        763..802
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  98597 MW;  646927EC4D8971C1 CRC64;
     MPGFSDSFWT PDYATGLGVL YGKLQQGVVE NRQILTMASM RADAEEQYGL RMGEIAPSVD
     RMTGAGFGKD DGASVRKAYE GVRTEMIEAS RNHQKIANNI RELVVAPFRR WSDQHDYRVQ
     ASHDNLQTRI KEHSKQVELV KKLRSVYFNK CRVLEDLEEE NKLAFQDPDM SPKIMPTPKI
     VLPAEEEQEE EPVELGDRIF PPEEIKKILA HMLHNIRIGE AKVPIIGTYQ NTSTGADIVE
     YVQTYMDATN LAQAERIGQD LVDNGFLRLV GNMGSVFANS SKMNYQWRSK VFKLTGIPEK
     KKPLMRVTSV ASSEDGNVSD SPISSVSEML AGWNPLNNPH PNETPSEKLR REALEADERY
     KNAVRRLDQI RCRLEEDVIE NLRFMEQCEL DRLKAIKAVV LDFSGAISNV IPNLQSTVDH
     MMLYQETIQP LGDLRYLLEN YRTGGFVPRV QAYENYYGSV EEQNFGVDLE ARARVDRKRV
     PILVTTLLTY LDNRYPELEG DEARRAIWLH NPPLAITHQL RSVLNNSKVD YREVLPKYQI
     PVVASVLKLY LLELPDSLVS SQVYEIVKTI YSTTAHETTE EGRIKVLQST LGQLRLVNIA
     TLDAIMTHFT RLIDLTSADE QYIASLAQIM SPCVLRPRTE SSLTMDERHS YRLIRDLFAH
     KDAIFNELKR QSSALGISTS SRPRAISTDE SNRRAAMEAR QRAIVNRTRA TSPTGRQRHR
     RDRSSGASET GRFPINVSSP ADRRTTRGTS LDVPAEGSPT GAEHPTVDTQ ITDGSISNGA
     STESPASLPA SASSSEGSVS PPPPAETASD GSPTPTPTPA AISTEFEKRA SIPRSAGARY
     TRKPGLGSLS SFPTSAGSVG TDSKRSSIAE SEPKGVTLED KPMDD
//
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