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Database: UniProt
Entry: A0A395N7C1_TRIAR
LinkDB: A0A395N7C1_TRIAR
Original site: A0A395N7C1_TRIAR 
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
//
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