ID A0A5N6ZV88_9EURO Unreviewed; 887 AA.
AC A0A5N6ZV88;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 02-APR-2025, entry version 16.
DE RecName: Full=Rho-GTPase-activating protein 8 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BDV27DRAFT_133078 {ECO:0000313|EMBL:KAE8361432.1};
OS Aspergillus caelatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=61420 {ECO:0000313|EMBL:KAE8361432.1, ECO:0000313|Proteomes:UP000326268};
RN [1] {ECO:0000313|EMBL:KAE8361432.1, ECO:0000313|Proteomes:UP000326268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 763.97 {ECO:0000313|EMBL:KAE8361432.1,
RC ECO:0000313|Proteomes:UP000326268};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics studyof 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; ML737736; KAE8361432.1; -; Genomic_DNA.
DR RefSeq; XP_031924513.1; XM_032068008.1.
DR AlphaFoldDB; A0A5N6ZV88; -.
DR GeneID; 43652454; -.
DR OrthoDB; 2155291at2759; -.
DR Proteomes; UP000326268; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0000935; C:division septum; IEA:TreeGrafter.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005096; F:GTPase activator activity; IEA:TreeGrafter.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:TreeGrafter.
DR GO; GO:0007264; P:small GTPase-mediated signal transduction; IEA:TreeGrafter.
DR CDD; cd04399; RhoGAP_fRGD2; 1.
DR FunFam; 1.10.555.10:FF:000044; Rho-gtpase-activating protein 8; 1.
DR FunFam; 1.20.1270.60:FF:000050; RhoGAP and Fes/CIP4 domain protein; 1.
DR FunFam; 1.20.1270.60:FF:000073; RhoGAP and Fes/CIP4 domain protein; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000326268}.
FT DOMAIN 2..430
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 227..296
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 464..662
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 683..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 116..143
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 343..370
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 688..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..817
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 98239 MW; 496B48DBAD5D06DE CRC64;
MSGFAASFWT PDYATGLGVL YGKLQQGVVE NKQIITIASM RADAEDQYGA RLGDIAPTVD
RLTGAGFAKD DGASVRKAYE GVRTEMVEAA KNHQKIASNI RELVVSPFRR WCDQHEARIQ
NSHDDLQARI KEHTKQADLV KKLRSHYFNK CRVVEDLEEE NKLAFQAPEA SPPVKAPPKI
VLPEEAEEEE PMEIGDHVYT PEGLKQLLVH MLDNIKMGDV KVPIIGTYQN TSTGADIVEY
TQKHMNATSV SYAERIGQDL VDNGLLRLVG NMGSTFANSS KMRYQWRPKV FQITGIPEKK
TPLLRVTSMA NSEDGSESPI STVSEMLAGW NPLNNAHPNE TPAEKLRREA READERYKAA
VRKLDQIRCK LEEEIVENLR FMEQCELDRL KAIKAVVLDF SGAISNVIPN LQSTVDHMML
YQETIQPLGD LRYLLENYRT GGFVPRVQAY ENYYGSVEDQ NFGVDLEARA RADRKRVPVL
VTTLLTYLDN RYPDLEGDEA RRAIWLYDVP LAATHHLRNV LNNSKADYQE VLEKYEVPIV
ASVLKLYLLE LPDSLVSSQV YEIVKTIYST TAHETTEEGR IKVLQSTLGQ LRLNNIATLD
AVMTHFTRLI DLTSADEAYI SALAQALSPC ILRPRVESSL TMNERHSYRL IRDLFAHKDS
IFGELKRQSS ALGVTGSISR PRAISTDESN RRAAMEARAR AIVDRTRANS PAPPRKHRRD
RSSGPSEAGR FPVNVSSPTE RRTVTRNSLD VPSSNSSPTA QEQLSNVNIN AATEAAATEA
TPNGTSSDSS ASATANETPS SGTSTPPPME ATTAPEDSPT PTPTPAADVE KRASITRASF
TRKPGLGNRS SFPVIPSGES GTDSKRNSLA DSEPKGVTLE DKPMDDD
//
