ID A0A0A2V9K0_BEABA Unreviewed; 1193 AA.
AC A0A0A2V9K0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Rho-type GTPase-activating protein 1 {ECO:0000313|EMBL:KGQ03032.1};
GN ORFNames=BBAD15_g11755 {ECO:0000313|EMBL:KGQ03032.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ03032.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ03032.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ03032.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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:KGQ03032.1}.
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DR EMBL; ANFO01001295; KGQ03032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2V9K0; -.
DR STRING; 1245745.A0A0A2V9K0; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_0_0_1; -.
DR Proteomes; UP000030106; 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 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; PTHR24215; RHO-GTPASE-ACTIVATING PROTEIN LRG1; 1.
DR PANTHER; PTHR24215:SF10; RHO-GTPASE-ACTIVATING PROTEIN LRG1; 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; 3.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000030106};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 93..154
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 157..217
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 476..539
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 818..1022
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 135068 MW; 56CF54FF8BB5B0F6 CRC64;
MAFDSSNGLP PDLAHGDNNH PTSDAADKSW QSAGRQTPDN DHKLRLTNSN PGPASLPGSL
PAEPPWNDEP PRKSSERNRS RQRNGRSASG QIRTCKKCGE PLTGQFVRAL DGTFHLDCFK
CRDCGEIVAS KFFPADDDDG QGQYPLCETD YFRRLGLLCY QCGGALRGSY ITALDRKYHV
DHFTCSMCDT VFGAQDSYYE HDGNVYCHYH YSTRFAQRCN GCQTAILKQF VEIFRNGQNQ
HWHPECYMIH KFWNVRLGQP SDHPQLPLDL TDPADRELIR ADEERMEDKV YRIWSVLSTF
EESSAACISD MLLHVSNGSY VDGVLVAKRF IWHVEILFRS ADRLDQLITQ KSEKGKLLTT
CLQASMLTTL GMSYGREAKL LCKKIVSFFS LLSKTQDADA RKLGVTQELL SLVTGLAHYL
KLLIRICLQG ALRFERDTQD SDGLHQFLDD LNDFESFKND ETANMIDSRL AAKDSDHCGV
CRRSVEDECA TTGDYRWHLP CMRCSRCGRD LGRALYEATY NTADRKLACT NCASSQHPAI
SLPLEHVSKL QQYAFLLKVA LARLLDILRN NGTIPPAPGE KPANGLTADR PSFGADNRSK
SYSAAGDREH QRESTYENTL NEVRRLRSTR LDRHLSSSVR HARTSRVMNS DGRGPRAESP
AQGDSKHAPQ NSTDMMFGQN DAITLDDIPR IVAVEQSKEQ QQRELAQEAG RTGLADTGIS
NRHQRTLSAS QNQDVRAPDP LQTRLVRKFF PELSALEYCN VRHLAVLTMQ PMLESEFSLD
ELSSFIETRK QVTFWKNLGK AFKNDKNRNM KKKGVFGVPL EVIIERDGAE STDGVGPGTL
RIPAIIDDII SSMRQMDLSV EGVFRKNGNI KKQQEMVDRV NNEGCDQINF MEQPVIQLAA
ILKRYLRDLP DPLMTHKLYR LWVTAAKLSD PAKRKQCLHL VCCLLPKSHR DCMEILFTFL
KWAGTFHQLD EDVGSKMDVR NLATVIAPNI LTNATKAPAL DSEAIYVIDA VEIIIANIEE
MCHVPDELLT LLNDPYLFSS SSEITTKEIQ KRIQDRRGQI PIADVAEVYN RPDVTSRAPP
KRVETDPSLW QGERTVRPVQ DPPGHYSHSN QGTPPQRWRN PDDPSPYHNN NYNRSEGHLA
RTDHNPREWR NSGWQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQHPGGLGVG NSF
//