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Database: UniProt
Entry: W7HPH8_9PEZI
LinkDB: W7HPH8_9PEZI
Original site: W7HPH8_9PEZI 
ID   W7HPH8_9PEZI            Unreviewed;      1114 AA.
AC   W7HPH8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Rho-type GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DRE_04804 {ECO:0000313|EMBL:EWC46011.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46011.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC46011.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC46011.1,
RC   ECO:0000313|Proteomes:UP000024837};
RA   Liu X., Zhang W., Liu K.;
RT   "Drechslerella stenobrocha genome reveals carnivorous origination and
RT   mechanical trapping mechanism of predatory fungi.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KI966422; EWC46011.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7HPH8; -.
DR   HOGENOM; CLU_001321_1_0_1; -.
DR   Proteomes; UP000024837; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd09391; LIM1_Lrg1p_like; 1.
DR   CDD; cd09392; LIM2_Lrg1p_like; 1.
DR   CDD; cd04397; RhoGAP_fLRG1; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR   PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 1.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00132; LIM; 3.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024837};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          59..120
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          123..183
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          410..473
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          753..955
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          658..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          990..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        992..1006
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1031..1048
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1081..1095
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1114 AA;  125307 MW;  47667F50750A5A14 CRC64;
     MASPYASEPQ IRGQPLPPSL VPGASNDTSP QRRPDDRLAP FPPTDSKQKS PPKPESARRI
     CKKCDQPLTG QFVRALGGTF HLDCFRCRDC GTIVAQKFFP VDADDGSGQY PLCETDYFKR
     LDLLCHDCGG ALRGSYITAL ERKYHIEHFT CCVCPTIFGP QDSYYEHDGE VYCHYHYSTK
     FAARCQGCQT AILKQFVEIF RNGFNQHWHP ECYMIHKFWN VKLAPSSEVP ELPRIVEEED
     QDPSDSRRSV VREAEERMEE KVYRIWSVLS TYEESSAANI SDMLLHVSNG AYVDGVFVAE
     KFIWHVELLF NSADNLDIEL CKASGEGLVY SREAKLLCKK IVAFFTLLSK TQETGAGKLG
     VTQELLSLER DYNNIDAFNR FLVELSDLDA AKDAKPTFEV NSTLADLNSD LCQNCRNTIE
     DECMQFGMPK WHISCFGCVS CSTSLKNDVD SAYYSALTSQ LLCANCASHV QDAQRGFEHV
     SRLRQYVYLL RVALARLLSM LKEGGALSYT PVDDPNFVGY DDTNPTGFGP GALNAENRSK
     THHGEGEGYN STVSDVRRLR STRLDQKLAS SGRKARQSRI IENENFNAEG SDQRERFRIV
     EDRDINGETI NELTFGEAGT LTLDDIPRIA AQEQAREQRP NAFKHRTSGF FAPVGMHQPK
     LMNGHQRDSK GEQVPPPRMR RYFSELSAID YFIIRHLACL AMLPLVSEHF SQEELLELIE
     RGSKQTLWTK FTKGFKQDGG KNKKQKKTGG FGVPLEQLVE RDHAESSLGI GPGPLRVPAF
     LDDAIAAMKQ LDMSVEGVFR KNGNIRRLKE LTALINAGNE NIDLVKEGPV QVAALLKKFL
     RELPDPLLTF KLYKLFIASQ RMPDEEKKRR VLHLTCCLLP KHHRDSIEIL FSFLNWVASF
     SHVDEESGSK MDVHNLATVI TPNILYTKGQ SPGMDDSFLA IEAIHNLIEC NERMCEVPED
     LMMILSDPNM MATPDMTTKE ILKRYGEVAK FSSNTGRGQG NRSPPSRNKD GRPPPPIYHK
     VADEPVTGGG ESWSGNGTVR QVQTPPAPDQ LQKGEFGYEN NDAPRLPEPM YAQENGNRSR
     HSHSFSFDRE TSPGGRRMDY PSSNHQNPNL SAHT
//
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