ID Q0CEM6_ASPTN Unreviewed; 1201 AA.
AC Q0CEM6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Rho-type GTPase-activating protein 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ATEG_07858 {ECO:0000313|EMBL:EAU32120.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU32120.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CH476604; EAU32120.1; -; Genomic_DNA.
DR RefSeq; XP_001216479.1; XM_001216479.1.
DR AlphaFoldDB; Q0CEM6; -.
DR STRING; 341663.Q0CEM6; -.
DR EnsemblFungi; EAU32120; EAU32120; ATEG_07858.
DR GeneID; 4322813; -.
DR VEuPathDB; FungiDB:ATEG_07858; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_1_0_1; -.
DR OMA; WQMQSSV; -.
DR OrthoDB; 1329523at2759; -.
DR Proteomes; UP000007963; 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 Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 115..176
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 179..239
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 852..1054
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1162..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1201 AA; 132397 MW; 525BF9AA3E0E16EA CRC64;
MPPGDVPLPD SLVPGNGAVR PTLNTSGYGG SYQKQTPTSP ADSNVPFDSP RALSAGGRNG
SANSPIDGGY SPVTPVTRDP TTPHDQLGYW DRPAPRENSR SNGRSHTKSP GSTTRICKKC
GDPLTGQFVR ALSATYHLEC FKCEDCGQIV ASKFFPVDAE DGSGQYPLCE TDYFRRLDLL
CHECGGALRG SYITALERKY HIEHFTCSVC PTVFGAQDSY YEHEGRVYCH FHYSTQFAQR
CHGCHTAILK QFVEIFRNGQ NQHWHPECYM IHKFWNVRLA PTGQPLEPPQ LDLDATDEER
NRVREEEEVM EEKVYRIWSI LSSFEESSAA CISDMLLHVS NGTYIDGVIV AKRFIGHVDV
LFSAIDELAG AIRTQGMKDL SFGREAKLLC KKIVAFFALL SKTQEAGVRK LGVTQELLSL
VTGLAHYLKL LIRIGLQGAL KLEREKGTAD GLHNFLDHLG DLEALRPPEE EEATSDLMAG
VEVLADQLSD CCIACKEPID DECVMLGDNR WHVKPPHLTC VACQKDLTAT LQDALWSPKD
QRSFCTDCAS SKGLTPETQA GFIRVTKLQQ FVFLLRVALA RLLTVLRAGG SLTSASGDMN
ARPQDGNDDQ KTSPGGPIRR SATRGKGYPR QGSEESSLEQ TMGEMRRLRS IRNERTLSTT
YKKARASRII DGPEGRSVRP GSPGGEGSDP RGPGFQIVEE RDANGETVTD LTFGNQDALT
LDDIPRIVAA EQAKEQRPNA YRHAGTKLVG TTEPLPRYNR GHQRDVSGAG IEGPLEQPGR
TKKYFSELSA LEYFIVRHVA VLSMEPLLEG HFTLEELLSL IESRKPTIWN IFGRAFNKEG
KKVGKKKGVF GVNLDVLVER EGTESSHGVG PGALRIPALI DDAVSAMRQM DMSVEGVFRK
NGNIRRLKDL SELIDNKYEQ VDLTKENPVQ IAALLKKFLR EMPDPLLTFK LHRLFVVSQK
IPDPEKQKRL LHLTCCLLPK AHRDTMEVLF AFLNWTSSFS HVDEESGSKM DIHNLATVMT
PNILYPNAKN GTVDESFLAI EAVNALITYN DTMCEIPDDL QMVLSDTSLL KENSEVTTKE
ILKRYGDIAR GSFSQKPSNG GETVTITNAT RGANAPTSAR IETDPSQDGA WQSQSSVRQV
QASGSHGPPP GGMELGPAPT NDYRERSTSS GSQHNPMQPE GQSQQLPYRA RPNAGPMGVA
S
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