ID E3QW04_COLGM Unreviewed; 1268 AA.
AC E3QW04;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=GTPase-activator protein for Ras-like GTPase {ECO:0000313|EMBL:EFQ35042.1};
GN ORFNames=GLRG_10186 {ECO:0000313|EMBL:EFQ35042.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(2012).
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DR EMBL; GG697387; EFQ35042.1; -; Genomic_DNA.
DR RefSeq; XP_008099062.1; XM_008100871.1.
DR AlphaFoldDB; E3QW04; -.
DR STRING; 645133.E3QW04; -.
DR EnsemblFungi; EFQ35042; EFQ35042; GLRG_10186.
DR GeneID; 24415551; -.
DR VEuPathDB; FungiDB:GLRG_10186; -.
DR eggNOG; KOG3508; Eukaryota.
DR HOGENOM; CLU_003244_1_0_1; -.
DR OrthoDB; 22721at2759; -.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR CDD; cd05137; RasGAP_CLA2_BUD2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194:SF60; GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782}.
FT DOMAIN 547..702
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 757..992
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..101
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 141335 MW; 2531CDF041AB89FE CRC64;
MAPPGMDGRT YHNGGHNATP RLDWPHSQNQ TLSADPSSRS MERTSITNLR TSLRSNHPSN
PTIRAVTPEY HHPDLSPVSP ANTAFDPPVP LQLPPRGLTP SSPQTSPRSI PGDFSRRQGM
VFNDTYGDSY DNSTSPPSRQ TSSFRPRTHT MDGALRQQFI SATLRDGRQR LGSFSSSGSQ
PLYDDARSPP PQIESQGFPS VVPARHSEIP LGASTSLREK KLSTKRLIKR HSSRPTSPPT
ASTPSVDSLP IPVPTENANN ILLMMKNLCG RMRGEIEVRS EPAGAWRVGI AYVDEEKGSL
MFDSGQDGPF HVPLVSDLRG CRIAPVELPE GKRCLEVSCP TQPPLDLLLR PILAEERDLW
LAALLCWQQL RPPKVRLSSG NRSPTPTSLR PVVRRRGSEN GTKTTNALIK VGQVRLWDKG
LASSPRAIVK RSSTRDLRSP TTSWRLVSCL LQENGEIRLT TNDGDAVIAV VELSQLSRCA
IQQLDRSVLD EEYCIGIFPH YSPISTQLSI FRPVYIALEN RLLFEVWFVL LRAFALPDIF
RLDPHLSGGA IEVTDLESEL PGEIFRIEKT ISLRVTEAKL KPRNSSPDAG FVDRQPKDAD
PLVGNYLAEV ILDGEVRARS TVKAGTKNPF WREDYQFSDL PPAMPLLSIV LKRLDGNLEC
LNHQLQASLG SSKTSGLTEV LCGSVDIPLD HVEPGKDFER WLDIYDERQQ VMGTMLVKLH
HEELVVLHSK EYQALSSLLH SFPSGVTAKI AEALPGNLRR LSEIFLNIFQ VSGHANEWLQ
TLVEDEIDGI GSTQNQLKKY RFSSRLKSNE SMESSSDREQ ILRDMGKSLA GEANLLFRGN
TLLTQALEFH MRRSGKEYLE QMLQAKIAEI NETNPNCEVD PSKLKPGENI QEHWNRLIQL
TTEVWQCICK EPTKCPPELR SILKYIRAVA EDRYGDWLRT VTYTSVSGFL FLRFICPAIL
SPKLFGLLRD HPRPRAQRTL TLVAKALQAL GNLSTFGKKE EWMEPMNKFL GSNRQSVKDY
IDIICSIPVE RNKVALGPSY STPIAILGRL SPMAREGFPA LPHLIDHAYN FAALVKMWTE
ANPIGNGELA KPMTGEEDIL IFNEMCLGLQ ERADLCYSRM DSSLHETASL PTSEYADAME
HNAALLESMS ISTYHTENSA TNSANNSMVW AEQDQYQPPG SAGSDITVDA PSRRSREHRR
GRDFNSLRQM SGHSETSSSH LATLKRNGRA TRQILSGIMK PFARSDSPES SPSTSRGKNV
ERSWNTGF
//
