ID G8BXN2_TETPH Unreviewed; 1064 AA.
AC G8BXN2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=TPHA0I01540 {ECO:0000313|EMBL:CCE64660.1};
GN OrderedLocusNames=TPHA_0I01540 {ECO:0000313|EMBL:CCE64660.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE64660.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE64660.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE612864; CCE64660.1; -; Genomic_DNA.
DR RefSeq; XP_003687094.1; XM_003687046.1.
DR AlphaFoldDB; G8BXN2; -.
DR STRING; 1071381.G8BXN2; -.
DR GeneID; 11532825; -.
DR KEGG; tpf:TPHA_0I01540; -.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_010436_0_0_1; -.
DR OMA; QFISTDT; -.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000005666; Chromosome 9.
DR GO; GO:0005933; C:cellular bud; IEA:UniProt.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13277; PH_Bem3; 1.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF129; RHO GTPASE ACTIVATING PROTEIN AT 16F, ISOFORM E-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000005666}.
FT DOMAIN 565..674
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 851..1064
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 105..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 685..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 743..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 60..94
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 119624 MW; AEA1C485C8CF367A CRC64;
MSRRKIGGGS HAFDLLQAYD DHREIKDQLI KDIEQNTVPM EDERHGVETK TGDSEQDTQT
VKLLEEIKML RNTIEKKDAE ILKLNRVINE YEENKMLELL PPRSLSRSKR GVDESKSVTD
IEEGKPGLPS NDLDFHSPAT SVAYTTSRIT ITSPTKIKSD SKNTNALQSS SNNNNNNNSN
NRSNNNQHQH QHQHHDGTIE FTPTSKQQLT SFNDLLVKSF DGEVPAISKN VNDNNNDGME
IDEDISDAGT PDALPQPFFN RLQKTEQPPL PPQDEQMLLT PIRTSFKFDE PKYDGTNESV
ELSSPIVVGS DIKNELEDSI RSLEDSEGTT TINENYQIQI NDSNNINGNS TREPSLTSVL
SSSSNNIVTN GRINSVNSAN KYRNPSNEAT PNRNISNSRI NTALSNQINS PNSFVNTPIS
VIKSDIPLFI QPNDFHTIDP IVLTTLYFNE TNENFCLVSV VDKSSRKEMF KFKKTIEQIY
ELDSYLKSTI SVYSLQELPM LPEKHSFNNY IPAKVNGRLD TLNDYFKTLF QTNNLPNNAI
IKILQFISTD TFIPPLSVDD MNSSSLMKDG VLIVRKSKTL GTGINWRLRH AQLLKDMLLL
CNQRNSQVLE SIKLKQATIE LMPNLPDDKF GTKNGFIITE QKKSTLSNPN KYYLCTEKPK
ERETWVQVIN KLLMDVDSSG ASYNGNTIDN NNDNNNYTNS TNISAKSSMQ KVSNMRSITP
VSRTSENSSE HIYVTDLTLD NKTFNNKEND SNLVNTESSN GSPLENKKIV TELEICSHSK
KTAPNGNDDE NLNKPSTRNY PSDVKFSDSS INNALEAMTL GSLEKSDSGS NFNSSFGTRN
LVFGNSLDAC IALSSNTYQG QYVIPSVFFR CLEYLYKNRG LQEEGVFRLS GSSSLIKLLQ
EKFDKEYDVD LCNFDPSTIG DGTIATRNID VNTVTGILKL YLRSLPHLIF GDSNYQTFKN
IVDENYNKPS IIAQEFRNVI NSGSVPDTSI AMMYALFELL VRITQNNKIN KMNLKNLCIV
FSPTLNIPIN ILQPFIVDFG CIFKNEEPVP DSERSEVDIH IPQL
//
