ID A0A165MFR6_9APHY Unreviewed; 1146 AA.
AC A0A165MFR6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DAEQUDRAFT_768686 {ECO:0000313|EMBL:KZT65625.1};
OS Daedalea quercina L-15889.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Daedalea.
OX NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT65625.1, ECO:0000313|Proteomes:UP000076727};
RN [1] {ECO:0000313|EMBL:KZT65625.1, ECO:0000313|Proteomes:UP000076727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-15889 {ECO:0000313|EMBL:KZT65625.1,
RC ECO:0000313|Proteomes:UP000076727};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV429102; KZT65625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165MFR6; -.
DR STRING; 1314783.A0A165MFR6; -.
DR OrthoDB; 1328399at2759; -.
DR Proteomes; UP000076727; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
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 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 PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR23065:SF17; RHO-GTPASE-ACTIVATING PROTEIN RGD2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 2.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 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:UP000076727}.
FT DOMAIN 8..544
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 322..402
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
FT DOMAIN 578..801
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 187..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..1146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 475..502
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 804..828
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..875
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..966
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1015
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1146 AA; 126186 MW; 7C9F0DA6A3466F86 CRC64;
MAVLSLPLSF QNSFWSQDYR TGLEVLYTQL EKGVLENEEI VAFIWARASA ESALASTLTA
AGPAGIEQFV YAPSRIADGV TKGKAFARED GASLHVAFRG LKEESIAQGK AHEAIAAELR
DVVAAPFEKW AHGYRERLWN SKHNMLDGFM HAYEAAQVEV TKLKHDYLNK MRRADEAEDD
ARFAPIPQSV GDKFTTSPSM VPRDKPRVPT RTPTMTERIS QRFKELRLQA GHATSPEKVE
VQFDAGTDVE SEKGTPRVDK GKGRAIEDVA SPERMASPPP MSPPLPPARL NTNPMPPPPA
PPLTIAGLEM APTDVSDLLK RARDTMPLRP VRFPLIGEYQ DCFSGEDFAS WLKENVKDFS
GSLDHAAFAA RELTEKHNLL RRVGEFGNDF ENVDDAFYQF RGKAFELGTA TAPAENAASP
IQKTLSPMAE AVATRTTTIA SLVSKALNAN GSAEPVHIRA RRDADAADRE YRIAVRKLDR
QRLGLEERIE ETLKTLQKWE LDRLRAVKTV LRQYQTAVAK LAKAYEPSLE RSNVLIDSYA
PEADLKVFIE HYRTGPFRPE PRVYESVTHD ESDVVFGIDL RRWADSAMWP GSEEKKDKPD
VPPVITLMLN AINAAYSKLP NDTERRKTWI YDVPLPAVHH IRESLNAIPP EQPFPDDILE
KYDAPVLAGA IKLWALELNP PLGMYEGWDE LRKLYPTVGS NAKAEDSHTE EQHILELQAA
LQRLPRVHLL TLDTIVKHLK ELIATTPAAE TDESNEVYVT KLALTMGRTI LRPKQESEIS
IQDRHPTLLF MDLINKYDSI VPPAIERKKR ESQRKMPVRR RTRPIDMRMS RSRISAGADL
KELQAEQLAQ RTGARVLRSS PPLPPPAPSL PTVPASPAAL SPESQEISSS AIMKSAEPGE
TFASLPPPVV QSTEKVSPLA QQGPTENTTP PYANIPPPPP LAKTTTPEVP PPPPLEKPTQ
PPHPVFKDPP PEDDDLPPRP TFKEPPAESD EEQPMPTFQP PAPAEPVPEP APKLAPAAIP
AALRTASRPN SRPGSPRVSS QEPSRSPSPT KPSSPTGAAL SRSTRPSRGP RTSGGGSVSS
MVNNFNRQSQ VMDRSSSPSG LNGASGLRRN GSKPGAGHAK RGSVSRVSEL SRRTMASDAE
DEVVDR
//
