ID A0A2K1QFP7_9PEZI Unreviewed; 765 AA.
AC A0A2K1QFP7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE SubName: Full=Rho GTPase-activating protein 1 {ECO:0000313|EMBL:PNS13974.1};
GN ORFNames=CAC42_6487 {ECO:0000313|EMBL:PNS13974.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS13974.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS13974.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS13974.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNS13974.1}.
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DR EMBL; NKHZ01000088; PNS13974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1QFP7; -.
DR STRING; 2082308.A0A2K1QFP7; -.
DR InParanoid; A0A2K1QFP7; -.
DR OrthoDB; 3030820at2759; -.
DR Proteomes; UP000243797; 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 CDD; cd00170; SEC14; 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 PANTHER; PTHR45808; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR PANTHER; PTHR45808:SF2; RHO GTPASE-ACTIVATING PROTEIN 68F; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000243797}.
FT DOMAIN 30..190
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 219..436
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 10..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 84187 MW; AB3D9F1654957275 CRC64;
MKSAFVQRAA RMRSGSSSAN LQTIPPPESS EDYSQDYASI AASILYQSPL PSQSGLPVFI
LNAAAFPDSH EVDYDSLLPY VLNRLPGEDD LIAGTEYEVV FFAGGQPESV TGEKKAGPGI
AWFIQVYQVL GRALRKRLQK IYIVHERSWV RVLTEVFGTI VSPKFKKKVA HVSTLSALAL
HIPIETLLIP PPVYLHDRKL SPDIYVPYAT GQRAFTANDP LPQDSTGSRR LPRVLREATT
FLLNETNVKT EGIFRIPPHS TMLGVVREAY DRGQHFIVWK ESGVSSVDPG MSPQTLAEVH
ESDAYGVHLA AGLIKVWYRE LRTPIVPERC YEDLRQAFGS PETEVTRESL VQLLSPSSEK
SVLPLNSRLV LTWHLLPLLS LVSDHEPRNK MTPENLAVCF APALICGEDQ LQDAKMTTVI
RKIFTEAIVE WSDGLAEACE TSQRDFWNAL KAPTRAEDYE DPLPDMQREN AIAMDERIKR
ISLSDNDTPE PVPTLPPRSS SLPRGRDGQR TPPSPFPKRK PAPTVASLPR YSTLIPNPSQ
PPTYQNGDHG FQADSKQRLH DEQNGFPAKE SARLQSIRAD QSSNDSAPLI DISPVKRAAT
ISVPTRNEAP SPLLSPSLAE IQGAQTMLRS VSGESAKSDR SDDGVFIKPT WAASSRQTSV
SSQKSVTRKP TPPLSVTRNG DRVDSGTHAP SYAPKPRTPS PGLMQRMQSW EREAGTSDTG
VGKAEVGGRK QSVDDLKRLY EERATTVKGL ARTKSGSSQR SQGSA
//
