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Database: UniProt
Entry: A0A3N4J2J9_9PEZI
LinkDB: A0A3N4J2J9_9PEZI
Original site: A0A3N4J2J9_9PEZI 
ID   A0A3N4J2J9_9PEZI        Unreviewed;       867 AA.
AC   A0A3N4J2J9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=Rho-GTPase-activating protein 8 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=L873DRAFT_1716638 {ECO:0000313|EMBL:RPA90781.1};
OS   Choiromyces venosus 120613-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Tuberaceae; Choiromyces.
OX   NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA90781.1, ECO:0000313|Proteomes:UP000276215};
RN   [1] {ECO:0000313|EMBL:RPA90781.1, ECO:0000313|Proteomes:UP000276215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=120613-1 {ECO:0000313|EMBL:RPA90781.1,
RC   ECO:0000313|Proteomes:UP000276215};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
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DR   EMBL; ML120514; RPA90781.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4J2J9; -.
DR   STRING; 1336337.A0A3N4J2J9; -.
DR   Proteomes; UP000276215; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd04399; RhoGAP_fRGD2; 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   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; 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; SM00049; DEP; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276215}.
FT   DOMAIN          2..440
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          240..309
FT                   /note="DEP"
FT                   /evidence="ECO:0000259|PROSITE:PS50186"
FT   DOMAIN          474..672
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          164..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..867
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..753
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        768..793
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..817
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   867 AA;  95505 MW;  EAB91063EF10D318 CRC64;
     MPGFADSFWS GDYAGGLGVL FGKLQQGVIE NQQIVQIAKL RADAEDAYGQ RLGTIPPGAE
     KPGGFGRDDG ASVRKAFDGL KKEMDDAGKN HRKVADNIRQ LVINPFSKWC EAHEERIINS
     HDDLQGQIKN HDKQAEAVKK LRSHYFNKCR LVEDLEEETK FIQVPAPGTP SSATSPPPTA
     PAAVATATPE IKLPEPEDPE DDEPLEIGDL FYQPVEVKKM LSHMLETIPL GEVKVAILGT
     YQNVSTGENI VKFIQENLGA TSISHAERIG QDLVTHGFLR LVGSVGNTFA NSPKLHYQWR
     PKTFQLTGKP EKPVQKAAKA LENGDSVESP TMAYVGDYLG GLLTNQHPGE TPGDRLRREA
     SEADERYKAG VKKLDLMRCA LEESMMEHLK FMERCELDRL KAIKAVILDL SGAISNVIPS
     IQATVDNMLL YQETIQPLGD LRYMLESYRT GSYVPKVVTY ESYYNSVDEQ TFGVDLEARA
     RADRKRVPII ITSILTYLDH HYPDLEGDEA RRGIWLVDVP LAATHHLRNA INTGKAIPKE
     VLATYEIPIV ASVLKLYLLE LPDSLVSSHK YEIIKTVYTT HGTEGEENRR LAVIQNTLGS
     LPLTNIATLD AITTHFTRLI ELTSADEAYV TSLAHGLSSC ILRPRVESSL TQHERHAYRL
     VRDLFAHKEQ IFGELKRAST LNSGRARAIS TDESQRRAHV EARNRAVIGA ARSRPSSPAP
     SSRHRREVST DGGNRFPIQT SPTSGSPRTS RYRPSSLEVP GGASSLDRDQ KLDSEVEAPR
     VSGEPESFTH HESEESSPAT PTAGLEKSNS LTRKSHAGGG STRFPRKGAN LVRSAAGGPK
     RDSLSMGGSF EEERPTGVSL TDRPMDD
//
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