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Database: UniProt
Entry: A0A010S2M1_9PEZI
LinkDB: A0A010S2M1_9PEZI
Original site: A0A010S2M1_9PEZI 
ID   A0A010S2M1_9PEZI        Unreviewed;       775 AA.
AC   A0A010S2M1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Beta-chimaerin {ECO:0000313|EMBL:EXF78818.1};
GN   ORFNames=CFIO01_01657 {ECO:0000313|EMBL:EXF78818.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF78818.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF78818.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF78818.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) 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:EXF78818.1}.
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DR   EMBL; JARH01000609; EXF78818.1; -; Genomic_DNA.
DR   RefSeq; XP_007597601.1; XM_007597539.1.
DR   AlphaFoldDB; A0A010S2M1; -.
DR   STRING; 1445577.A0A010S2M1; -.
DR   KEGG; cfj:CFIO01_01657; -.
DR   eggNOG; KOG1450; Eukaryota.
DR   HOGENOM; CLU_010730_3_0_1; -.
DR   OrthoDB; 5482027at2759; -.
DR   Proteomes; UP000020467; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07652; F-BAR_Rgd1; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23176:SF138; RHO GTPASE ACTIVATOR; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 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:UP000020467};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          64..337
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          580..772
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..66
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..435
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..550
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   775 AA;  84394 MW;  DBEC933B29DF7C81 CRC64;
     MADLRSPSDD NLPSHNEQRD RASSMSLGNT ETAAPSQNGG ATTANGGPPA GNDTGSAPTS
     EVSRQVQEVL SSDIGVATML NQLKASIASA KEFALFLKKR SHIEESHASS LKKLSRISQE
     TMHQPDHRQG SFAQAYSEMM YIHERMAENG TQFALSLQQM HDDLLELAAV AERSRKGWKA
     NGLAAEHRVA ELEAAMRKSK AKYDSLAEEY DRARTGDTSR NSGKMFSLKS KSGPQHEEDL
     LRKAQGADQD YQAKVQTLQS EKAELIARTR PEAISALQDL VKETDSGLAL QMQKFASFNE
     KLLLSNGLSI SPIKGQGSGG GPRSLREAVL AINNEKDLHD YLTSHHSKVA NNNGEVKYEK
     NPILATARQQ AMGHQPNASV SNVPQAAPSG SFSGPPGGPN QQQQRDMPPP ARPGNLQPPS
     DSPQSFAPPN MPAAQQPRPS SQQQHPPPQA QQHGRSFSTN NMLNQPSQQQ QFQSNRNSGV
     VAPTYNSGGM SSQGPPQLGA LPFQTSQSPP PPQQQPQQRA PPPQSQYQPP QQHQPPPAQQ
     YPPQGPPPGA GGYPQQNRQS PPLGGPSGPS PNAARPTFGL SLPRLYERDG LPVPMVVYQC
     IQAVDLYGLG VEGIYRQSGS LTHINKLKTM FDTDSSNPAL DFRNPENFYH DVNSVTGLLK
     QFLRDLPNPL LTTEHHSELI EAAKQEDDIV RRDSLHAIIN SLPDPNYATL RSLTLHLHRV
     MENSHVNRMN SHNLSVIFGP TVMGTDPATS IADAGWQIKV VDTILQNTYE IFDDE
//
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