ID A1CU76_ASPCL Unreviewed; 1267 AA.
AC A1CU76;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=GTPase activating protein (BUD2/CLA2), putative {ECO:0000313|EMBL:EAW06863.1};
GN ORFNames=ACLA_085590 {ECO:0000313|EMBL:EAW06863.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW06863.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW06863.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027060; EAW06863.1; -; Genomic_DNA.
DR RefSeq; XP_001268289.1; XM_001268288.1.
DR AlphaFoldDB; A1CU76; -.
DR STRING; 344612.A1CU76; -.
DR EnsemblFungi; EAW06863; EAW06863; ACLA_085590.
DR GeneID; 4700442; -.
DR KEGG; act:ACLA_085590; -.
DR VEuPathDB; FungiDB:ACLA_085590; -.
DR eggNOG; KOG3508; Eukaryota.
DR HOGENOM; CLU_003244_0_1_1; -.
DR OMA; QKDWTLI; -.
DR OrthoDB; 22721at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR CDD; cd00030; C2; 1.
DR CDD; cd05137; RasGAP_CLA2_BUD2; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194:SF60; GTPASE-ACTIVATING PROTEIN; 1.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 4: Predicted;
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701}.
FT DOMAIN 513..651
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 734..968
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1243..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 142463 MW; DA9FE41AE87A2915 CRC64;
MDSEGSSSNG FKRNSAHHSI YSRPVERRAS KKSSSKDRHG MVYPDSFRET SIRTVTPDSS
SETRNHSPSS EAENLSGSAA PSPRAAYKSR APDPESRRDF HPYYSAGDED DVQVESRSQR
ARSRTTTLDD QRSEISPNSF LTRTRTRLGS INTTSPQPKQ SEDQTSIGFP SIQPAPYFSQ
TFGRQRLSRN LGSSNSVTGL ATSPVSPSLS STDASKVLQL MKTTSGRMHG ILSFRTSSTT
AWTSGYCAIN VATGSLIYQA KGEPALAKTL IPDLRGCQVR SLVDAESRAN YLKVSTFTSG
LGIELKPHVS ETFDSWLAAL LCWQPIRPKG VQNKMTKPQS VAIGDRHLID RRRNSESTVQ
KEAAIIKVGK MLLWDRPSAS GVRPNSGRRV STYRQQRALS SSWQKVSCTL QENGAFKLFT
ESDITLVTCI QLSQLSRCSV QQLNESVLED EFCIAIFPQY AAHPASGLTR PVYLALESRV
LFEVWFVLLR AFTIPELYGP EIPVDENQAS NMDSGDSSFP PTRDLFRIER MLCVRVTEAK
LIRDRTSEET ARSRKQSRSH SNSLPAPAIS DYYTELLLDG EIRAKTAVKY RTSNPFWRED
FIFQDLPPVL SQVKILVKTI NPAQKDWTLI AHGSYALNQE TSGMHGLDDV ELSSHDPTYG
RVEIRLDDLE SGVETEKWWT IFDGRDQSVG EMLMRARMEE TVVLMSHEYM PMSEILHSFT
NGLTINMAQI ISSELNQLAE ALLNIYQVSG QTVEWISALV EDEIDGVHKE STTNRLRYTT
RIHSNDSRES AQDREVLVRD LGRTATVEAN LLFRGNSLLT KALDLHMRRL GKEYLEETIG
ERLREIDESD PDCEVDPSRV HRADDLERNW RSLIALTTSV WKSIASSASR CPPELRLIFR
HIRACAEDRY GDFLRTVTYS SVSGFLFLRF FCPAILNPKL FGLLKDHPRP RAQRTLTLIA
KALQGLANMT TFGSKEPWME PMNKFLVGSR LEFRQFVDSI CAIPADRPTP IVTPSYATPI
QILNRLPHTS REGFPSLPFL IDHGRSFANL IRIWLEGAPG KLAGLEEIDP AIQKFHEMAY
RLNQRTKDCL SKAEQAERPN GTLEVKWEEL VDSMERSATF YEESSKPTTP ATETAVPAPA
SVTGNHRNSI GYFVSRPSLP RRSTDHSPDA EAETPPSSSS ATWDQSRVPF SMPRWSDTRD
STGSSKNSST YSLEYSDMSK ARRASVTKET STSKYRFFDF VPASSRRKAK ERENTQQHSR
EELRNEL
//
