ID G7XU88_ASPKW Unreviewed; 1217 AA.
AC G7XU88;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Rho GTPase activator {ECO:0000313|EMBL:GAA90504.1};
GN ORFNames=AKAW_08618 {ECO:0000313|EMBL:GAA90504.1};
OS Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS awamori var. kawachi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA90504.1};
RN [1] {ECO:0000313|EMBL:GAA90504.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA90504.1};
RX PubMed=22045919; DOI=10.1128/EC.05224-11;
RA Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT for brewing the Japanese distilled spirit shochu.";
RL Eukaryot. Cell 10:1586-1587(2011).
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DR EMBL; DF126474; GAA90504.1; -; Genomic_DNA.
DR AlphaFoldDB; G7XU88; -.
DR STRING; 1033177.G7XU88; -.
DR VEuPathDB; FungiDB:AKAW_08618; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR InParanoid; G7XU88; -.
DR Proteomes; UP000006812; Unassembled WGS sequence.
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; cd04397; RhoGAP_fLRG1; 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; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 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; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
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 125..186
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 189..249
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 863..1065
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1217 AA; 134925 MW; 1650DF2A5F302AAF CRC64;
MPPGDVPLPD SLVPGNGAVR PKLNTSGYGG GSYQSQTPTS PADSNIIFDS PRTRTGGWNG
STNSPVEGPQ GSDSRMSRRL ESGHPGPRDP STPRDRNGYW DRSTPRERSR PNGRPPTKSP
GSSSRICKKC GEPLTGQFVR ALQATYHLEC FKCEDCGQIV ASKFFPVDAE DGTGQYPLCE
TDYFRRLDLL CHECGGALRG SYITALERKY HIEHFTCSVC PTVFGAQDSY YEHEGKVYCH
FHYSTQFAQR CHGCHTAILK QFVEIFRNGQ NQHWHPECYM IHKFWNVRLA PTGQPLEPPE
VETDATDEER NRVREEEDIM EEKVYKIWSI LSSFEESSAA CISDMLLHVS NGTYLDGVLV
AKRFIGHVDI LFSAIDQLAG HIKEQGMKDL AYGREAKLLC KKIVAFFALL SKTQETGVRK
LGVTQELLSL VTGLAHYLKL LIRIGLQGAL KLEREQQASQ GLHHFLDHLG DLETLRPPEE
EETLADLMTG VDTLADQLSD CCTACKEPID DECVMLGDSR WHIKPPHLTC ASCQKELSHT
LQDALWNPKE KRSFCTDCVS QNGLMHDVQG GFTHITKLQQ FVFLLKVALA RLLAVLRAGG
SLGSGDASPP QDGNESGRIP PGGEMRRSAT RSKSYANATR NAPEGSSLEQ TVGEMRRLRS
IRNERTLSTT YKKARASRII DGPEGRSVRP GSSGGEGSDP RGHGFQIVEE RDANGETVTE
LTFGNQDALT LDDIPRIVAA EQAKEQRPNA YKHAGTKLVG TTEPLPKYNY GHQRGVSGAG
LDQHIIEQGG RTKKYFSELS ALEYFIVRHV AVLSMEPLLS EYFTLEELLS LIESRKPTIW
NIFGRAFNKE GKKVGKKKGV FGVNLDFLVE REGTESSHGV GPGQLRIPAL VDDAVSAMRQ
MDMSVEGVFR KNGNIRRLKD ISEMIDNKYE QVDMTKENPV QIAALLKKFL REMPDPLLTF
KLHRLFVVSQ KLPDPEKQKR VLHLTCCLLP KAHRDTMEVL FAFLNWTSSF SHVDEESGSK
MDIHNLATVM TPNILYPNAK NSTVDESFLA IEAVNCLITY NDTMCEIPED LQSVLSDTTF
FKENTEVTTK EILRRYGDIA RGSFSPKASN GGETVTITNS NRAANIPTSA RIETDPSQDT
AWQMQSSVRH VQSPGGHQHS TSGTPQAGTE LAPTASNDYR ERSTSNGSQQ NPMQAEGQSQ
PMPYRARPGA GPMGVAG
//
