ID   A7TMN1_VANPO            Unreviewed;       678 AA.
AC   A7TMN1;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Kpol_1066p9 {ECO:0000313|EMBL:EDO16445.1};
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN   [1] {ECO:0000313|EMBL:EDO16445.1, ECO:0000313|Proteomes:UP000000267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC   NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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DR   EMBL; DS480424; EDO16445.1; -; Genomic_DNA.
DR   RefSeq; XP_001644303.1; XM_001644253.1.
DR   AlphaFoldDB; A7TMN1; -.
DR   STRING; 436907.A7TMN1; -.
DR   GeneID; 5544602; -.
DR   KEGG; vpo:Kpol_1066p9; -.
DR   eggNOG; KOG1450; Eukaryota.
DR   HOGENOM; CLU_010730_2_0_1; -.
DR   InParanoid; A7TMN1; -.
DR   OMA; DSGWQAR; -.
DR   OrthoDB; 5482027at2759; -.
DR   PhylomeDB; A7TMN1; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005933; C:cellular bud; IEA:UniProt.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23176:SF136; RHO GTPASE-ACTIVATING PROTEIN 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT   DOMAIN          34..296
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          484..675
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   678 AA;  76007 MW;  0A7EC0F37CBFF5E4 CRC64;
     MVDQDIASSQ STGISTGTSG MAETLSEGDL FERSEIKRIL DSDVAINTLL ARLKQSLLTC
     EEFTKYIKKK YMFEEENVEE LSKQYKHFFS STSATAPSLR RSIQQILQFD GKMAQVKQSY
     ISALVKMYEE LSALLLTMTK MRKSIKEKGR RLEKDVVDSI HIAEKAQARY NSLCQDWEKL
     RLTDPTKTKL TLRGSKTTKE QEEELQRKID AADLEYKQRV DHSTSLRNSF LNSERPKIVS
     ELRDLILEID TALTIQLQKY TIWTENLALN TGVTISPLEE SKSMRSIAAK VTNERDLYDY
     LNKYNKQSKD SILVNRNLIP VPYKKHPSMA KGQLINPTGS FTVNSSRNTN NFKNSTTSKS
     INTEGGFHSN SSSTYNSPAN SVNNLGSTKT SLANTAIASS MSGIGMNLLS HTDSTGNQSP
     IDNSSMFKPP SLNPGNGIGK PGRIPSLATT SSGVSGDSGR PLSHIQTNSS MPPGTQKNFK
     TFGVPLESLL EFEQEMVPAI VRQSIYVIDT YGLDLEGIYR KSANILEVSK LKEEIDRDPS
     NISMILPPKD YTEADIYVVG SLLKAFFSAL PDPLIPSSTV PELKICLSID DYNTRKNYIH
     GLIYKFPDAQ YWTLRSLMFH LKRVSEHESE NRMNIKGLSI IWGPCIVPQN DEDSNDINFQ
     IKIMEVLFDV ADQAFEPE
//