ID G2X1V4_VERDV Unreviewed; 1185 AA.
AC G2X1V4;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Rho-type GTPase-activating protein {ECO:0000313|EMBL:EGY22840.1};
GN ORFNames=VDAG_04278 {ECO:0000313|EMBL:EGY22840.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY22840.1};
RN [1] {ECO:0000313|EMBL:EGY22840.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY22840.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS572701; EGY22840.1; -; Genomic_DNA.
DR RefSeq; XP_009649020.1; XM_009650725.1.
DR AlphaFoldDB; G2X1V4; -.
DR STRING; 498257.G2X1V4; -.
DR EnsemblFungi; EGY22840; EGY22840; VDAG_04278.
DR GeneID; 20705741; -.
DR KEGG; vda:VDAG_04278; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_0_0_1; -.
DR InParanoid; G2X1V4; -.
DR OMA; WQMQSSV; -.
DR OrthoDB; 1329523at2759; -.
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; cd09391; LIM1_Lrg1p_like; 1.
DR CDD; cd09392; LIM2_Lrg1p_like; 1.
DR CDD; cd09393; LIM3_Lrg1p_like; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
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; PTHR24205; FOUR AND A HALF LIM DOMAINS PROTEIN; 1.
DR PANTHER; PTHR24205:SF4; LIM DOMAIN FAMILY; 1.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 102..163
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 166..226
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 472..535
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 826..1030
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..92
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 132026 MW; F8B5851E40FEE599 CRC64;
MASAHDNGSA DDRFHGHPPV MAPGYPMDNR SWQNGGRKTP DSTYRNHITE SPGPRTPGMN
DRPERTERTD RSRDRDDTRS RPSGERQRSR QRSGRSASGQ QRTCKKCGEP LTGQFVRALD
GTFHLDCFKC RDCGQIVASK FFPADEENGE GQYPLCETDY FRRLGLLCHQ CGGALRGSYI
TALDRKYHVD HFTCSLCPTV FGAQDSYYEH DGNVYCHYHY STQFAQQCNG CQTAILKQFV
EIFRNGQNQH WHPECYMIHK FWNVRLSSSS GKADVPVDTD DLVVRDNIRH REEQMEEKVY
RIWSVLSTFE ESSAACISDM LLHVSNGAYV DGVLVAKKFI CHVEVLFTAA DKLDLTMKQV
DIKGLSYGRE AKLLCKKIVS FFSLLSKTQD TGARKLGVTQ ELLSLVTGLA HYLKLLIRIC
LQGALRLERE SNSLDGIYQF LDDLSDLEAI KLDDKSLQVM TGTSKLSAKD SDHCALCGRS
VEDECAQNGD KRWHITCVKC TRCETDLGRK LGDARFNVFD QSVYCTNCTG ANSDDLLSFK
HVSKLQQYVF LLKVALARLL DILKTNGALP PQDDDTPMNG YTLGDGSLAP GSGDVPYLSS
DNRSKSYAGD AREHQRESSY ENTLNDVRRL RSTRLDKHLS NSIRKARTSR VMDADGNDMQ
ASNGGALGGP GGQIPEDMAV GDESTNERMF GHQDALTLDD IPRIVAAEQV KEQYQPGRQD
LYRSPATEPF MGHQRSQSTG RQADARAGDQ PRGGRRFFSE LSALEYFNVR HLAVLLMAPH
VESEFTMDEL LSFIDAKKPA TFWKNIGKAF KNDRSKAVKK KGIFGVPLEV IIEKDGAEST
DGVGPGALKI PAVVDDIIRA MKGMDLSVEG VFRKNGNIKK LTDLVERIDR DGCDSINLTE
QPVVQIAALL KRYLRELPDP LLTHKLYRLW LTISKITDDN KRINCLHLSC CLLPKAHRDC
MEILFCFLKW AGSFHQVDEE VGSRMDIKNL STVIAPNILY TNAKALALDS DPMFAIVGVE
DLISHIEEMC LVPDEVMGLM DDPFVIAGGN ADLSTKEILK RYQDRMGQKP AGFGGDMGEI
HNRQDNSSRP PPTRVDTDPG VYKQASSVRP VMDTPAPFNN TQMPGTPPQG WRGPGDSGHP
SPYGSQGNQY ETADAQLEQT EGGPKREWRN SGWGRPNGVG VGGNI
//
