ID A0A395RYI1_FUSSP Unreviewed; 1182 AA.
AC A0A395RYI1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=GTPase-activating beta-chimerin {ECO:0000313|EMBL:RGP65216.1};
GN ORFNames=FSPOR_7429 {ECO:0000313|EMBL:RGP65216.1};
OS Fusarium sporotrichioides.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP65216.1, ECO:0000313|Proteomes:UP000266152};
RN [1] {ECO:0000313|EMBL:RGP65216.1, ECO:0000313|Proteomes:UP000266152}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP65216.1,
RC ECO:0000313|Proteomes:UP000266152};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP65216.1}.
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DR EMBL; PXOF01000106; RGP65216.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395RYI1; -.
DR STRING; 5514.A0A395RYI1; -.
DR Proteomes; UP000266152; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09394; LIM1_Rga; 1.
DR CDD; cd09395; LIM2_Rga; 1.
DR CDD; cd00159; RhoGAP; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
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; PF00412; LIM; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 22..84
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 992..1179
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 142..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 650..677
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 185..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1182 AA; 130375 MW; 02174E2894590DD4 CRC64;
MASIVEDYLE SPGMEQETDD VFPCKGCGDI LEEGKAFELA GNRWHLDCFR CNTCGTLLDS
DANLLLLGDG SLICNNCTYS CSACGNKIED LAILTGEQAF CATCFRCRNC KRKIENLRYA
RTSQGIFCMG CHETLMARRR KKSKAAAAAK AREKEHSPMI TEKSLPALPA NAIPPNAFSN
DRVDPDSDTA TELSPRPRNH TRHESSSRSS SRPARSPERK PDGLNLPATT YRSNRNSAMM
SRTENSNDDG FLISVALDPS PHPTPKSTSD NMTEGKSKDR DYFGAAKPPS EKRSDSRTST
PHIAFQEKGR QASASEHDTP PKLPDRKHSK PPRPESMKPS PVIDEKTQKT SGRRPPTEDF
KLQEAPKSKK LLSRSSSQSS SIPAETSSVR TSNGQPGKAG HSGLPHSDSN ATTPASRSSL
ESRYLDEEEL RASMDSSTRT SSRPENAKPL ARKDVPSSSS RTGNYSSESR KSSQALTERI
VNGSSRQQSR QESPEDSTPT RQTPSRSISE QKKTDTYMQP RSAPAPPNNR GHAAGKEPSK
DDGSSPKVSP KLPRWSSGGD LNMDEDMARI LGTDEGSSSI LRRVSNAVRH GRTGSVESPH
QMHPGNRHTR SISETTRATG SPRWPRTPVA DDYHAQDISS PMSLTAGDDP AFLKRQLRNS
EQRVAELERQ FTTEKDLKSL NKKLVEKRKT VSVLDTQTEI MIRQLEVLAG YVERAKETKT
PVDPRDLEES AIKEFVQKLD KVKSAMSATI EQLHEERDLL CEEKDQAIAD RDRALLEFEQ
LSSKNAQLAD MNNDLTHQIQ ERFKSQIGGD VKSPGALGIY AGKGLNASSI NLDAASLSTG
ATLVPADEDT IVEAGPTVVQ VRKGQAKKFN WKKGSKGLAQ GVAKGVNRAV VAFQNDRERM
QQQGGLSGEN IGMPYNMTVA QVEAPAGPPS NGHVSHEKHG AAGAQARRQE ERERERQGFG
FFGKKNAMPK SGSAGTMNNA EAAEPPTVLF GSDLAERADH ERRQIPSVVT RCIEEVELRG
MDQEGIYRKT GGNSQVNMIK DGFSKDENFD ISDPDLDITA VTSVLKQYFR KLPIPLLTFD
VYERVLESNA IVDEDERSDH LRKTFASMPQ RHRDCLEFLM FHLARVAQRE PENLMSPKNL
AVVFAPTIMR DTSLEREMTD MHAKNLAIQF VIENSNTIFE DA
//
