ID A0A1L9V515_ASPGL Unreviewed; 841 AA.
AC A0A1L9V515;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 22-FEB-2023, entry version 16.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0000259|PROSITE:PS50238};
GN ORFNames=ASPGLDRAFT_137830 {ECO:0000313|EMBL:OJJ78949.1};
OS Aspergillus glaucus CBS 516.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=1160497 {ECO:0000313|EMBL:OJJ78949.1, ECO:0000313|Proteomes:UP000184300};
RN [1] {ECO:0000313|Proteomes:UP000184300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 516.65 {ECO:0000313|Proteomes:UP000184300};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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DR EMBL; KV878924; OJJ78949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9V515; -.
DR STRING; 1160497.A0A1L9V515; -.
DR VEuPathDB; FungiDB:ASPGLDRAFT_137830; -.
DR OrthoDB; 25175at2759; -.
DR Proteomes; UP000184300; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd04396; RhoGAP_fSAC7_BAG7; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR15228; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR PANTHER; PTHR15228:SF25; SPERMATHECAL PHYSIOLOGY VARIANT; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000184300}.
FT DOMAIN 98..305
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 841 AA; 90786 MW; A9B3A4A155F89A76 CRC64;
MVTGKPEPFQ AFAPTSQPVA FSPPSKRDLT SWWRQFKRNT RKEEVKGTTT SIDSLESHHH
LFMAGANGSC VIKKKIDIPR GIFGIPLNVS IKYANVAISL TNDNGESFIY GYVPIVVAKC
GVFLKEKATD VEGIFRLNGS AKRIKDLQEI FDSPERYGKG LDWTGYTVHD AANVLRRYLN
QLPEPIVPLD FYEQFRQPLR TYQRQVQGLA PANEAEIFDH AKAVAAYQQL IRELPPLNKQ
LLLYILDLLA VFASKSEQNR MTSANLSAIF QPGLLSHPQH DMSPDEYKLS QDVLIFLIEN
QDHFLFGMNG TAADEETVKA VESGGIAPRA PTTTQTSIRR SVSSASGGAD SFRKYGSLRR
NVSVSSKNSR NSNAATSPGT PSSLSGVHRS NTLPSKMAPP MQRRAVQESA TGNTTGPAPS
AKPSPSPSRT PPSTEGNNHI RIQVPSGTDG ASVIGTSGMA YVHSATHGPI PKRFAGHVTV
PEPQPPREAS VSPPPPAVVT PTKERKLSNF FSKSPPPSGE QRQPNRLRKK RSPGSVCESA
QSSSQSLQGV TADNIPRTVP PENGVAANGA QDESHTNNQE NGTSQSENGQ TLTTDTSLKP
HSRTPSMRSR SSFTDQSDLE QLDETARAER KEHRQSWKFP RSSKRSSEQI GLVSPPLGAT
NPSATRSASS IGSWHQTSRS SPSDLQQFVN DPANQPLSLD AELNNNGSPK EIEPERRSLF
GKFKAKVGLS RDGKDTDSLR DRTRSPVNSD TEMSVSNLTL SPPPSKVSNG SKSAPEANGP
DESPVSPLPG SGLPHAIPEE PGSPESPVAS AFVEQKEPVT SAPESAPAQT EAAAGPPKEL
N
//