ID A0A395N7C1_TRIAR Unreviewed; 1487 AA.
AC A0A395N7C1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Rho gap domain-containing {ECO:0000313|EMBL:RFU72015.1};
GN ORFNames=TARUN_10247 {ECO:0000313|EMBL:RFU72015.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU72015.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU72015.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU72015.1,
RC ECO:0000313|Proteomes:UP000266272};
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:RFU72015.1}.
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DR EMBL; PXOA01001039; RFU72015.1; -; Genomic_DNA.
DR STRING; 490622.A0A395N7C1; -.
DR Proteomes; UP000266272; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd13277; PH_Bem3; 1.
DR CDD; cd04400; RhoGAP_fBEM3; 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; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23176:SF137; GTPASE ACTIVATOR (BEM3), PUTATIVE (AFU_ORTHOLOGUE AFUA_6G06400)-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00169; PH; 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 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:UP000266272}.
FT DOMAIN 831..948
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1123..1331
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 66..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 258..285
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 66..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..445
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..467
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1487 AA; 161421 MW; D12919C3B30C7A69 CRC64;
MSTSSPSSFS GRAPAQTSAT EYGITFLFGA AFVELLAISC FGSALHWRLL LLADAWLRSI
YRSSRPSIPS PLSSPSYTAS SLTSPSPSWP STATSQRRPP PIDTRSQGNT TPSSAGHTTF
FSDSSNPSSP ESPRPPPLVA PNDTRSVHQQ VKRKPVVGSS NKAPSSAMAS PTTSAAPSGS
ATGLPRNSSI DSAISAISST AHANSPTNNQ AKSEEIAKLI KTAGSPEAVI QYLLKEKQSQ
AQQNSQLWRL VDKQRAMILG LNKDLEAALK DKDKYRKKLK ELMASPLVVK SAAGQDDEQH
SETHSNALLL RQEVDSPRES AAPFPRSLRL GSEGQLDSPV DMKLAPYPIT PPADRAHAPP
SAVAELLNPS EEMPKPQEYA LDHYNHEAEE EAADKARKEK SNGQLKEIPF IASLPPSRSL
PNHPPMKPPP KPPTANAPPT VTVMEPTPQP DEGIGKFPSP PRKAPPAPLQ LRQEIRRQLD
SPTIDEDTDS EYDDILEVDE IIPEKRGRRR TREEDDRERE VIAIQEAEAR SVSKMGNPGV
AEAPSSGTPS SPSTLSPNSQ PAASMDAVLS SNRPRELTAP ILSPGLPASP RPFGNPKMSL
AKPPMSPRGG GPLSPRPPRQ LIPMPPGTPL IVPPTASLSD GNPLKKAMDA GDYSKGLSSP
VERTAIFRGL VTEEYPDLLL PPNALPSVAV RVASSRMKPS RASLLSLTQL EEDPVFTLAI
LSRADGGELW RVEKDSASLA KLDQRLKQCG AFTARTPDRS LFTGHAPAKI DARRVVLDQY
MDELLNTPLD NATALELCKY LSTHTLPPNA DETGQTFKPK DDNSSIRSDG RPTRNGYLTK
KGKNFGGWKS RFFVLNGPYL KYYETPGGAH LGTIKLQNAQ IGKQSQNNEA NAPANQNNDE
ELDSQYRHAF LVLEPKKKDS SNHVKHVLCA ESDRERDIWV ENLLQWIDYR DPEEDQPPAR
PTVHDRQTSG DQLNSANKSK KGSKAHQTSG SDTLIGVRYD STHAGDAPHQ GAPGGRPKTS
GSQSDHHASM DSHSKLISGP KDPQVISDAS MWGNRIGLSA PPPAPAPSHD EKKQRKRSFF
GFGPKARTSS DGQESLFGGS ENGSGATPPQ NGYHGPVRHV FGAPLAEAVR YNSPVDVDVP
LPSVVYRCIQ YLESQNAIFE EGIFRLSGSN VVIKGLRERF NNEGDINLVT DEQYYDIHAV
ASLLKLYLRE LPTSILTRDL HLEFMSITTE ITDKSEKMAA LNELSQRLPQ ANATLLKYLI
AFLIRIINNS DINKMTVRNV GIVFSPTLNI PAPVFATFLQ NYEAIFGVDP EEYELPSPVS
ESESNSRSDS TARFDPPPGR PSTSSGSASP RHHGWPESIR DPARSTPTPP LLMNLNAARG
SPTPSGTSRH SYEPSYLLHQ SPRAVSQPLH DTGSGSDGHV SQPPHRASPA YERSLLPVTV
EDQNGNLAAY DQGSVARRRE SAIMMGGSSG LQHQQGSKSR LREEAHY
//