ID   A0A1W5CSQ5_9LECA        Unreviewed;       701 AA.
AC   A0A1W5CSQ5;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   SubName: Full=Rho GTPase-activating protein domain {ECO:0000313|EMBL:SLM33924.1};
OS   Lasallia pustulata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC   Lasallia.
OX   NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM33924.1, ECO:0000313|Proteomes:UP000192927};
RN   [1] {ECO:0000313|Proteomes:UP000192927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sharma R., Thines M.;
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FWEW01000166; SLM33924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W5CSQ5; -.
DR   OrthoDB; 1359393at2759; -.
DR   Proteomes; UP000192927; Unassembled WGS sequence.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
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;
FT   DOMAIN          423..614
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          264..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          618..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   701 AA;  77377 MW;  155F4EF5A5EB4183 CRC64;
     MLPTHDQSCT KERTGSTSNI ATSNERYQNM SKTASLALAV ADPTSTADQP PATYSPTSPR
     TSTSLSSSPA SPTDEFFKFH NLSSDTANSM GRLKLRKMGS KTLENRPPSP AFTSLPPHPT
     SPTAIPSRGR GLSRPFFSNS KAAKSSSRIM PTEATVRQVS EDGHPENENP VYTMGKSQAS
     TQELTNFSND EASDDSPNGT TKGEYTVSGR PGGTPTGSDS TVVGTLPGDL TTKRSRTRFG
     FLNRTHSTHL DKGESARKAK AKLEITDAQI GRQNYPREIT QDRSSPFDDT RAPRTAPLQR
     ERDPGYQSMM DSAARNRSAD RRPSPQRYQI RPLPARSGNP SERLTVSSST VFRDDASSIS
     FSKTLKNTSS KAADGLGKAG KFFVKIGRSG SSNSRDPAED AVYVLQVIRL PLVEQTRRTR
     IAKTLEDSKD KTEFWMPALP WRCIDFLNYR GCEEEGLYRI AGSAPRIKEW ERRFDIEIDI
     NLFDEPELYD INIIGSMFKT WLRNLPNEIF PKEIQARIAR ECPGAVEVPQ MFKDELSMLP
     PWNYYLLFAT TCHLSLLHAH VEKNRMNFQN LCICFQPCLK IDSFCFRFLV CHWKDCFQGC
     WTEDEALDEE KRVLDGLATR GGGSSGGSTA VAEESSISSF EGSKPALSGR ARERQKPPPL
     TIISASGESL ASPSRNGDGH SRNGSRPPEL APVEPMSPIG L
//