ID G4UA00_NEUT9 Unreviewed; 625 AA.
AC G4UA00;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 03-MAY-2023, entry version 35.
DE RecName: Full=Rho-GAP domain-containing protein {ECO:0000259|PROSITE:PS50238};
GN ORFNames=NEUTE2DRAFT_102727 {ECO:0000313|EMBL:EGZ78607.1};
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:EGZ78607.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ78607.1, 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; EGZ78607.1; -; Genomic_DNA.
DR AlphaFoldDB; G4UA00; -.
DR STRING; 510952.G4UA00; -.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_017095_1_0_1; -.
DR OMA; PPEDHSR; -.
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; cd00159; RhoGAP; 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; PTHR23176:SF125; GTPASE ACTIVATOR (BEM2), PUTATIVE (AFU_ORTHOLOGUE AFUA_7G04450)-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 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:UP000008513}.
FT DOMAIN 291..482
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 625 AA; 70632 MW; CF1A855391EFE8D6 CRC64;
MARKGVPQPL TLAESGTLGK ETSPRLGDTT QQQHHHHHQQ QAPSSSAVSA TGSGGGSLAS
GRSTPQASRS PRSPRSPFKI GPQKVEYPGE PPRTSSPPTE QPVEAVAISQ DQRYQRQKSP
DVPPEDHSRV TTSTSAPSQS SDHRGHKHSR NDEDKSSKSS FFFSFGKSSR LSERAISPQL
LEPQTEGIRT RSHKEKEKEN HQYSREPVYA PARAGEPDKV NQSLSLKEAG GSLFNGLKES
RAAGFLSKKL FGGSKEDKFA PKEPVIDDEH YVLKVINLPL VEQTRLTRIS KRLEDSRDKT
EFWMPAFPWR AIDYLNYKGS DVEGLYRVPG SGPQIKKWQR KFDEELDVDL FEQPDLYDIN
IIGSMLKAWL RELPDELFPK AAQERVAKEC AGAEKVPELL REELSNLSPF KYYLLFAITC
HLSLLLAHSD KNKMDFRNLC ICFQPCMKID AFCFKFLVCD WRDCWKGCKN EAKYIEEEYA
LFDQPPPRSY RSKRETELRE REEKEDRERA IHRDREREQR TQSQVQASYQ QQGGQVIPPA
HRNGNVQQSP APPQQVQRLR KKNTAQETTQ TAVVDTGSTV STTITLVSDR DTSHGRGTNH
PNQRQLQPGE LPALSPIKPL SPMGF
//