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Database: UniProt
Entry: B6Q8L6_TALMQ
LinkDB: B6Q8L6_TALMQ
Original site: B6Q8L6_TALMQ 
ID   B6Q8L6_TALMQ            Unreviewed;       893 AA.
AC   B6Q8L6;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   13-SEP-2023, entry version 67.
DE   SubName: Full=RhoGAP and Fes/CIP4 domain protein {ECO:0000313|EMBL:EEA25820.1};
GN   ORFNames=PMAA_069130 {ECO:0000313|EMBL:EEA25820.1};
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA25820.1, ECO:0000313|Proteomes:UP000001294};
RN   [1] {ECO:0000313|Proteomes:UP000001294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC   {ECO:0000313|Proteomes:UP000001294};
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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DR   EMBL; DS995900; EEA25820.1; -; Genomic_DNA.
DR   RefSeq; XP_002146367.1; XM_002146331.1.
DR   AlphaFoldDB; B6Q8L6; -.
DR   STRING; 441960.B6Q8L6; -.
DR   VEuPathDB; FungiDB:PMAA_069130; -.
DR   HOGENOM; CLU_008201_1_0_1; -.
DR   OrthoDB; 1328399at2759; -.
DR   PhylomeDB; B6Q8L6; -.
DR   Proteomes; UP000001294; 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; SM00049; DEP; 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:UP000001294}.
FT   DOMAIN          2..434
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          230..298
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          468..666
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          165..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..788
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        820..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   893 AA;  98925 MW;  4594BD51E96A3D5D CRC64;
     MPGFADSFWT PDYASGLGIL YSKLQQGIAE NRQILTIASL RADAEEIYSS KLDDIIPAVD
     RINTGFSRDE GASVRKAYDG IRGEMIEASK NHQKISSNIR ELVVNPFSRW CDQHAARVQS
     SHDDLQARIK DHMKQAELVK KLRSQYFNKC RLVEDLEEEN KFAFQSLEAP SPKGKPPAPK
     IVLTDPQESD EPEIFDLGDK SYSEDEIKNI LSDMLNTIKI GEVKVPILGT YQNTSTGADI
     VDYLQKKLEA SSISYAERIG QDMVDLGFLR LIGNMGNTFA NSSRMNYQWR SKVFQLTGMP
     ENKKPLLRMT SLMSNDEATS SPTISSVSEM LSGWNPLNNP YPDETPAEKL HREAREADER
     YKTAVIKLDQ IRCILEEEIV DHLRFMERCE LDRLKAIKSV VLDFSGAISN VIPGLQSTVD
     HMMLYQETIQ PLGDLRYFLE NYRTGGFAPK VQPYENYYGS VGDQVFGVDL EARARADRKR
     VPVIVTNILT FLDNHYPDLE GDDARRAIWL HDVPLAATHH LRQALNNSAG DPRAILEKYE
     IPIVASVLKL YLLELPDSLV SSQVYEIIKT IYSTTANETS EEGRIKVLQS TLGQLRLNNI
     ATLDALMTHF TRLIDLTSAD ETYVAALAQA LAPCILRPRL ENTLTLNERH SYRLIRDLFD
     HKDAIFGELK RQSSASSTLG AGAGAARPRA ISTDESNRRA AVEARNRAIA SRSRATSPAP
     GARHRRDRST DGSQGSGRFP INVSSPHGPD RRNPRQSLDV PSSIDLQIVT DSSKLAEENA
     TPNGSSGEVS EKAAPEVSAT ITDFSDPAPV LAADVDAEEG QATNDNNESE GSPTPTASVA
     TIEKRDSLTR GRHVRRAGGS HPPADLASKR ANAVTDGELK GVTLEDKPMD DFA
//
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