ID A0A163CVR3_DIDRA Unreviewed; 1185 AA.
AC A0A163CVR3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Rho-type gtpase-activating protein {ECO:0000313|EMBL:UPX10093.1};
DE SubName: Full=Zinc ion binding {ECO:0000313|EMBL:KZM22725.1};
GN ORFNames=EKO05_0000765 {ECO:0000313|EMBL:UPX10093.1}, ST47_g6136
GN {ECO:0000313|EMBL:KZM22725.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM22725.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM22725.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM22725.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:UPX10093.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX10093.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [3] {ECO:0000313|EMBL:UPX10093.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX10093.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; JYNV01000211; KZM22725.1; -; Genomic_DNA.
DR EMBL; CP095288; UPX10093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163CVR3; -.
DR STRING; 5454.A0A163CVR3; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 1.
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; cd00890; Prefoldin; 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:UP000076837};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 23..85
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 995..1182
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 140..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 754..816
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 164..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 129600 MW; 3E26429CF73FFD74 CRC64;
MDSPGGYPES LLDQDGDQDD VVYPCKGCGE ILEEGKAFEL AGNRWHIDCF RCNTCGTLLD
SDANLLLLGD GSLICNDCTY SCNHCGNKIE DLAILTGDQA FCANCFRCRN CKRKIENLRY
ARTSQGIFCM ACHESLMARR RKKSKKPPVP AAPKVDKSLP ALPPQFEDQQ SQRGAFTPDV
ETPSEVFSEP TTAEASPRPP QPRRGDSSSN FRRDASPAAA DLSRRDNILL PATTYNKDHK
HSESDAGDDG ILLPFALDPN PAPGPSPLSR ASRQFPDRSM GSASTTGEGK SSRNDYFNRP
TADPRDKLKE NNSRSGSAER PAPASPHIAF QEKGRQPSDH IVSTLRKQRD VSSESPSSNE
RSRSQHASPA PSSATDAFKL QEVPKNKKAD ARNRDSESSD SSPRQGSPGA EMSSRLSRPM
MEPTFTSTPP VGIQDSPETV SGSSFSSTQR VERPARGDSL RPTSSVQFGD RPAHSPTTPT
VEHPQRTSST HGAHAHLSAG LGISSPVESS RTFSDVPVPP ARSAGRPAPP AADTFTSPRA
PPQPPSTHKT SESISSLPSE SSRDAYAPGS GLPRYSAQGD FSMDEDFARL LGGQDKEDKD
SGVFRRVSNA VHKHGRSLSE RGSVTSRGHK KWPTNGSVDI SSPTIASPDS KEESASLRNE
LRRAQQRIAE LEAEKNGLQE SMHSAADIRQ ANTVLREKRN TMAVLDTQRE MVIRELEIMT
EHLKHAKESN GSMDINQLKS DILKDFANSL HKLKDQLGGQ IEDLISKRAE LTEEISNLIQ
MKDKGFQEYE SLTAQNAKLS AMNRELVENI QKTMNNKKGA PPFDVAANGL GIYNTQHKGG
KSELSLDAHS LPHEPSFPHI HEGDSEATLA QPQVVNIRKS GKATKFSKLK KGGQAFTTNV
TKGFKGAFGS EQKPEEYNSI KVIGTPYGSV HQQPDIASMS SSIKSKDEQT PKGWFGGGNA
KGGPSKQPND RFKPMQMNNS STNLAADAST VLFGSDLSAR CEFEKRMIPG VVSRCIEEVE
LRGMDVEGVY RKSGGSSQVN QVRSGFESKA DYDISDPDLD IHSVTSALKN YFRRLPVPLI
TFDVYDQFLE AGQLEDPEAQ SKALTTAINE IPRAHRDTLQ FLVFHLSRVI QHQDENLMTP
LNVAVVFAPT IMRPMDIQRE LSDVQQQRVA VQALLENYKT VFGEE
//
