ID   A0A319AN30_ASPLB        Unreviewed;       780 AA.
AC   A0A319AN30;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Rho GTPase activation protein {ECO:0000313|EMBL:PYH61589.1};
GN   ORFNames=BO96DRAFT_100645 {ECO:0000313|EMBL:PYH61589.1};
OS   Aspergillus lacticoffeatus (strain CBS 101883).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH61589.1, ECO:0000313|Proteomes:UP000247441};
RN   [1] {ECO:0000313|EMBL:PYH61589.1, ECO:0000313|Proteomes:UP000247441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH61589.1,
RC   ECO:0000313|Proteomes:UP000247441};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ821339; PYH61589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A319AN30; -.
DR   OrthoDB; 24454at2759; -.
DR   Proteomes; UP000247441; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   CDD; cd05132; RasGAP_GAPA; 1.
DR   InterPro; IPR000593; RasGAP_C.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR001936; RasGAP_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   PANTHER; PTHR14149:SF17; GTPASE-ACTIVATING PROTEIN; 1.
DR   PANTHER; PTHR14149; RAS GTPASE-ACTIVATING PROTEIN WITH IQ MOTIF; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   Pfam; PF03836; RasGAP_C; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF143885; RGC domain-like; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   4: Predicted;
FT   DOMAIN          186..402
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   780 AA;  90290 MW;  E9244B3484A910B6 CRC64;
     MSVATMLQPA SRASTSSSSS FQPVTRQNTM SSHDTRSLRQ SKRLSVTALY MSMNAKDRDL
     DISDDLARAQ IYLRELKAKI STQSKKNFVL EKDVRYLDSR IALLIQNRMA LEEQNEVASH
     LDDAIDPQEG FFPNDERTQK YGNLLFLLQS EPRHIAHLCR LVSMSEIDSL LQTVMFTIYG
     NQYESREEHL LLTMFQSVLT YQFDNTPEYS SLLRQNTPVS RMMTTYTRRG PGQSYLKQVL
     ADQINALIEL RDVDLEINPL KVYETMVKQI EEEQGSLPES LQRSVTAEDA AANAQVQAII
     EPRLKMLTDY ANRFLNIIIE SVEETPYGIR WICKQIRSLS RRKYPDAQDQ TICTLIGGFF
     FLRFINPAIV TPRSYMLIES TPTEKPRRTL TLIAKMLQNL ANKPSYAKEP YMAKLQPFIQ
     QNKERVNKFM LDLCDVQDFY ESLEMDNYVA LSKRDLELQI TLNEMYATHA LLEKHSLALA
     QDQHSHLNEL LQELGAAPPQ VPRKENRTIT VPLFSRWETS LDDLTAALDI TQEEVFFMEA
     KSTFVQILRS LPPKHPAMRR PLRLYLIAES AATLKNDAVM VRKGIRTIEL LDQLMKLGVI
     ERANDFSLLR DEVEQELEYL GGLKENVLKE TKKLEEVFAT IRDHNAYLVG QLETYKSYLH
     NVRSQSEGKQ RKQQKHQELG PYKFTHQQLE KEGVIRKSNV PENRRANIYF MFKSPLPGTF
     VISLHYKGRA RGLLELDLKL DDLLEMQKDN QEDLDLEYVQ FNVSKVLLLL NKRFARKKGW
//