ID A7TGU0_VANPO Unreviewed; 633 AA.
AC A7TGU0;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0000259|PROSITE:PS50238};
GN ORFNames=Kpol_2001p58 {ECO:0000313|EMBL:EDO18553.1};
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:EDO18553.1, 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; DS480388; EDO18553.1; -; Genomic_DNA.
DR RefSeq; XP_001646411.1; XM_001646361.1.
DR AlphaFoldDB; A7TGU0; -.
DR STRING; 436907.A7TGU0; -.
DR GeneID; 5546849; -.
DR KEGG; vpo:Kpol_2001p58; -.
DR eggNOG; KOG4406; Eukaryota.
DR HOGENOM; CLU_027718_0_0_1; -.
DR InParanoid; A7TGU0; -.
DR OMA; KKISWVY; -.
DR OrthoDB; 2055650at2759; -.
DR PhylomeDB; A7TGU0; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000000267}.
FT DOMAIN 188..365
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 372..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 71626 MW; 78B2ADE51A8B8E7F CRC64;
MLDINVNNIF FKSYSVDPNT GHSIYVFDST YLPSPEEVGD KQVFDLLIDE LMDTLMAKLP
SAPYSLVVFS SGFSNKKISW VYGIKMFSKL PQESRVFLQK TYIVHESFFI RTVYQVLSNA
MSIKFLGSSS NSTDSSSNEN TSASLIHVSD LTGLSHLIDI TRLRISLNVY MHDYELSEYI
DVPSEYFGRL TTLGNRQYRQ LIFDKVFKRL QLEGINYPMV FQKPGSYKKV NILLDIIERS
NYIDLSQWDI YSLASIFLHF LKNKSKPLIP IDFIALPIVD DFDYTYATFL RIIHYNEYYE
LLAAIFPLFT SFLDNEDHTK HNSKTLSKAL TPTLCKEKIS ILSSDRLSIG TRYIKNLLEH
FPSILNRIES STRSPRPVST IDSTKLKQRT ISAPITSPVA KQPVRVASQG LPPPALPKPR
KLSPTRSENR DTSPTRSISR STSPIRTLPP LPDKKKPTEN GNALSNIPVK LPPLNISNIP
SLKPETSNNE TRSEKTVRIS SDSSSILADE SLTDSVSNRR EPGSPTAPSE AIKEMVQDKP
ANDDDNDEIN NILKSASKLT LEHNEKILTF DKELKKKKKL EEINNTTNHS KFSDDGYSGI
KSGSKVGRLA ALYEERVQGI QMMNEMQKKM NNV
//
