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Database: UniProt
Entry: G4U6J9_NEUT9
LinkDB: G4U6J9_NEUT9
Original site: G4U6J9_NEUT9 
ID   G4U6J9_NEUT9            Unreviewed;       742 AA.
AC   G4U6J9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=RhoGAP-domain-containing protein {ECO:0000313|EMBL:EGZ76558.1};
GN   ORFNames=NEUTE2DRAFT_77108 {ECO:0000313|EMBL:EGZ76558.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ76558.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ76558.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
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DR   EMBL; GL890999; EGZ76558.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4U6J9; -.
DR   STRING; 510952.G4U6J9; -.
DR   eggNOG; KOG1450; Eukaryota.
DR   HOGENOM; CLU_010730_3_0_1; -.
DR   Proteomes; UP000008513; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd07652; F-BAR_Rgd1; 1.
DR   CDD; cd04398; RhoGAP_fRGD1; 1.
DR   Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR001060; FCH_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   PANTHER; PTHR23176:SF138; RHO GTPASE ACTIVATOR; 1.
DR   PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 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   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:UP000008513};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          36..312
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000259|PROSITE:PS51741"
FT   DOMAIN          545..738
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..393
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..516
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..537
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   742 AA;  80742 MW;  D92918C0DD7F324C CRC64;
     MSLGDASAPA TSPTPDSGSP VIAAAPAPPT APTSNDETKS HVQDVLSSEI GIATMLNRLK
     QSIASAKEFA TFLKKRSVLE DEHANGLRKL CKASHESSSR SEHRGGTFAK AYEDMMTIHE
     RMAENGTQFA MSLHQMHEDL LELAGIAEKS RKGWKQSGLT AEQRVADLEA AMRKSKAKYD
     ALAEEYDRAR TGDTTGQQKG KMFGFKGPKS AAQHEEDLLR KAQAADQDYQ AKVNTVQTER
     GELINKIRPD TIKALQEIVR ECDAGVVLQM QKFASFNEKL LLSNGLSVSP LKHGPEARSL
     RECVQAINND KDLDEYLLSQ YPRLPPRTGE PKYEKNALLD PANRTTTTPY VPPGGSQQAP
     THSREQGSMN SRTGPLNDTP TAPLGHHYGQ SSSSIPIISA SQQSESQPSH ERSFSHGNIL
     NQISTPFNPQ YGDSRSAATQ QAQAASSRYN GAIGSISSSG PPQLGALPFQ YSQPQSPPST
     TRQPPQQPSQ PPPPQPSQQP PSSQPPQQPP APLASPTQQA YPSGPVQGRQ STPPMAQPTR
     PVFGVSLLKL YERDGLAVPM VVYQCIQAVD LFGLGLEGIY RLSGSVPHVN KLKTLFDTDS
     GSSNLDFRNP ENFFHDVNSV AGLLKQFFRD LPDPLLTKEH YASFIEAAKN EDEVIRRDSL
     HAIINSLPDP NYATLRALTL HLHRVINNSS VNRMSSQNLA IVFGPTLMGT AGPGANIADA
     GWQVRVVDTI LQNTYQIFDD DD
//
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