ID   G7XM31_ASPKW            Unreviewed;      1255 AA.
AC   G7XM31;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=GTPase activating protein (BUD2/CLA2) {ECO:0000313|EMBL:GAA87990.1};
GN   ORFNames=AKAW_06104 {ECO:0000313|EMBL:GAA87990.1};
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:GAA87990.1};
RN   [1] {ECO:0000313|EMBL:GAA87990.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA87990.1};
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).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DF126461; GAA87990.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XM31; -.
DR   STRING; 1033177.G7XM31; -.
DR   VEuPathDB; FungiDB:AKAW_06104; -.
DR   eggNOG; KOG3508; Eukaryota.
DR   InParanoid; G7XM31; -.
DR   Proteomes; UP000006812; 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; 2.
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}.
FT   DOMAIN          505..670
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          725..959
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          1..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1112..1255
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..125
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1164..1178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1230..1255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1255 AA;  140753 MW;  B12857FF80AE366C CRC64;
     MEPEGSSGFK RNSVHQGIYS RPVERRPSKK SSSKDRHGMV YPDSFRDTGI RTVTPDSEAG
     NHSPSSEAEY LASSAAASPR PATRTRASDR ESRRDYHSYH SAGDEEDTHV EMKSQRARSR
     TTTLDDQRSE ISPNTFFRAR NRLGSINTAV PQPKTPDESS SIGFPSIQSP TYFSHSLGRQ
     RSSKPPGGSS LVTSVSANQT PSALSTTDAS KILQLMKTTC GRMHGILSFR TASTTAWSSG
     YCAINVATGS LIYQAKGEPA LAKTLIPDLR GCQVRSLVDP ELRTNYLSVS TFTSGLGVEL
     RPHVSETFDS WLAALLCWQP IRPKGVQNKM TKPQSVAIGD RRLVERRRNS ESTVQKEAAI
     IKVGKMLLWD RPSASGVRPS SGRRVSTYRQ QRALSSSWLR VSCTLQENGA FKLYTESDIT
     LVTCIQLSQL SRCSVQQLHS SVLEDEFCIA IYPQYAVHSA SGITRPVYLA LESRVLFEVW
     FVLLRAFTIP ELYGPETCAE DDPKSPSDAA ASSMADMFRI ERMLNVRVTE AKLLRNKAAE
     KAPRSRKQSR SHSNSTPTSA VSDYYTEVLL DGEIRAKTAV KYRTANPFWR EDFNFSDLPP
     VLSQVSILVK TISPTQKDWT LIAHGSYGQD HSNPARLLDD VELSSQDATF GRVDLKLDDL
     QPGVETEKWW PILDDKDQPV GEMLMRARME ETVVLMSHEY TPMSEILHSF TNGLTINMSQ
     VMSSELNQLS EALLNIYQVS GTTVEWISAL VEDEIDGLHK ESTANRLRYT TRIHSNDSRE
     SGQEREVLVR DMGRTATVEA NLLFRGNSLL TKALDYHMRR LGKEYLEETI GERLRDIDET
     DPECEVDPSR VHRSDDLERN WRNLVSLSTG VWKSIASSAS RCPAELRLIF RHIRACAEDR
     YGDFLRSVTY SSVSGFLFLR FFCPAILNPK LFGLLKDHPR PRAQRTLTLI AKALQGLANM
     TTFGSKEPWM EPMNKFLVSN RADFKQFVDS ICAIPADRPA PIVTPSYATP IQILGRLPPT
     SREGFPSLPF LIDHARSFAN LISIWLEIAP ERLAEMEEID PAVSKFHEMA VRLHQRTKEC
     LSRAEQAERP NGGLEVKWEE LVDAMERSVT FYEDSSKPTS PATEAAIAGS TSLTGSHRNS
     IGYFASRPSL PRRSTDYAPE AEDDTPPSSS SATWDQSRVP FSIPRWADPR DSTGSSKNSS
     TYSLEYPEPS KSRRSSITRE TTSKYRFFDF VPPSRRKAKD REQAQHSREE QRNEL
//