ID A7TFM8_VANPO Unreviewed; 729 AA.
AC A7TFM8;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Kpol_1023p5 {ECO:0000313|EMBL:EDO18836.1};
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:EDO18836.1, 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; DS480384; EDO18836.1; -; Genomic_DNA.
DR RefSeq; XP_001646694.1; XM_001646644.1.
DR AlphaFoldDB; A7TFM8; -.
DR STRING; 436907.A7TFM8; -.
DR GeneID; 5547157; -.
DR KEGG; vpo:Kpol_1023p5; -.
DR eggNOG; ENOG502QQWB; Eukaryota.
DR HOGENOM; CLU_008201_1_0_1; -.
DR InParanoid; A7TFM8; -.
DR OMA; RKTWIYE; -.
DR OrthoDB; 1328399at2759; -.
DR PhylomeDB; A7TFM8; -.
DR Proteomes; UP000000267; 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; cd04436; DEP_fRgd2; 1.
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 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 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; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 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:UP000000267}.
FT DOMAIN 2..437
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 216..296
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 471..714
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 592..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 84341 MW; C288A92E68169EAE CRC64;
MPGFVDNFWS EDLTTGLDVL FERLYHGCEQ CNSFIQLFAT RMQYEVAYGR QLYGVGGDID
NLDVTGRDPN VSIERALQTM VKSISEEGEA HLTIASNIES LILRPFSKWS NDHRERVKYS
EKLLKSNARN FQKSRTYVTK LEKDYFNKCR KIEDFKNSKF NEDELNKAME LLKLQKRYED
NLAREREFQK FATVGTIDFD YKTMRETLTL FLTKLPKSDY KLPLINYSLQ NTNSGSEITK
FILQNMSLKD MDHAELFGQD LLNLGFLKYC NGVGNTFVNS KKFQYQWKNY AYTFANLPLP
GEDGSNSGAE DNEESQYTNI KEINDSSTES ENKYEAVTEM PNISTDESTL FSYMKDVEVS
DKKYRKESFK MDTLRCSVEE LMIDHLSFME KCELDRIKAI KKATFDFCSI LGNKITSLKI
CVDKMINSED SIDPIESLLQ LISRYHTGVF QPKVISYNNY YNPGAYQIFG IDLETRARLD
KKVVPLIVSV ILSYMDQIYP DLANDKVRTS IWIAPVKLKL THELRALLNT QVFKDDADLL
EILKKANYDP STVSSVLKIY LLELPQPLIT DEVYDILKVL YEKYPPERTN FRKIQIDEKD
SDKKSEDEGN RNDDANTYKN TESENDTNRI RGLYTTLSSL SKPHIATLDA ISTHFYRLCK
ILRMGENGEQ MASDFALAIS QEFANCIIHV RLLDGNDLGC KIFYDLLTHK KQIFKVLKGQ
VSKQKRDKD
//