ID A0A0C7N8B7_9SACH Unreviewed; 1027 AA.
AC A0A0C7N8B7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=LALA0S10e02498g1_1 {ECO:0000313|EMBL:CEP64110.1};
GN ORFNames=LALA0_S10e02498g {ECO:0000313|EMBL:CEP64110.1};
OS Lachancea lanzarotensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1245769 {ECO:0000313|EMBL:CEP64110.1, ECO:0000313|Proteomes:UP000054304};
RN [1] {ECO:0000313|EMBL:CEP64110.1, ECO:0000313|Proteomes:UP000054304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 12615 {ECO:0000313|EMBL:CEP64110.1,
RC ECO:0000313|Proteomes:UP000054304};
RA Neuveglise Cecile;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LN736369; CEP64110.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C7N8B7; -.
DR STRING; 1245769.A0A0C7N8B7; -.
DR HOGENOM; CLU_010436_0_0_1; -.
DR OrthoDB; 25690at2759; -.
DR Proteomes; UP000054304; 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: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; 3.30.1520.10; Phox-like 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 Reference proteome {ECO:0000313|Proteomes:UP000054304}.
FT DOMAIN 571..678
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 811..1027
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 114180 MW; 2946B1EC932CECCA CRC64;
MGSGENAANS SATLELLSRY DNHVFERDET LAEVEREDWT ARSSGNLGAP GGPSYDELLK
ENVKLRLQLQ EHETEVVSLR KLVEVLKSDR SAQVDSVRQQ LIVEEEGKED KKDSEPVLPP
RSADRKRNAK NLSLNSVSDP TIPDLKFRSL LSPADVGLNR SVPYNHTTPT LREPGDNEHV
LSPTELDRIR RSSSSYSNFG AASPATSVAY TTSRISPSKS NKNFTAKEEE STNTVSNKSG
SSHQSVKVAT ASIHESFNSP LRQVSNSSGN QHSTENSARK EYPKSPVPNL LATEANAGEF
SPSSKRNLNN FADMLDSTFE SQSISSPQRV QASQQHGTRA LGSPVALNKP AASPKPGPSS
TSFIRYQNAS TEERSQISTV FSSTASYNIS GQDQQSPRSY STKSYPYGES DGITDTIQTS
QVTTTSSVPD SQSMVSDIPL FLQPNELNSI RIEILSTLHR DQDRSNDDNS ILFSVIDKKS
AKEMFRFAKT IDRIYELDVY LKCHMDTIML PPLPEKQYFD SGSPVKIDYR REKLNDYFSC
LYNSTNLSPL IALKMAKFIS TDTVINSFIG GYTKEGVLLM RKSKALGTPN TWRLTYGVLN
NGTLSLLDHG QVTENVKLQN AAIELQANLP DDRYGTRNGF IVTVPKKSGL SSGTKYYFCC
ESPKERESWV STITEFVESS VMSNSSYYAK SETSSMLDHT SVGDAVSDSA PSYIGPMVNL
QPTKVSTATN ADTTPTEDER ESKRSRMRSF FPFKKVNPSQ TPDSDLATEG GQTISAPGLD
ELTIAKTLQS MNLASEVLTD KVFGSDLNHC LSLSSQLYQG RFRIPSVVYR CLEYLYRNRG
LDEEGIFRIS GSTVLIKSLQ EQFDREYDVD LCNFNEKVVT EENQNSYSTG LVDVNTVTGL
LKLYLRQMPH SIFGDMMFSA FKNVIEASES SPSQIALEFR RLLNLQEMPF ENVSLMYVLF
ELLVKINQKS SINKMNLRNL CIVFSPTLNI PVNVIQPFVV DFSCIFENEE PVSDSLREQL
TLSLPHM
//
