ID A0A165XB03_9AGAM Unreviewed; 702 AA.
AC A0A165XB03;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=RhoGAP-domain-containing protein {ECO:0000313|EMBL:KZV59915.1};
GN ORFNames=PENSPDRAFT_659856 {ECO:0000313|EMBL:KZV59915.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV59915.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV59915.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV59915.1,
RC ECO:0000313|Proteomes:UP000077086};
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; KV424929; KZV59915.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165XB03; -.
DR STRING; 1314672.A0A165XB03; -.
DR InParanoid; A0A165XB03; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProt.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.20.1270.60; 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:SF134; ACTIVATING PROTEIN, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR23176; RHO/RAC/CDC GTPASE-ACTIVATING PROTEIN; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 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:UP000077086}.
FT DOMAIN 110..399
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 494..688
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..489
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 75728 MW; 0C319722159FD65E CRC64;
MSVDGQHPSR APMSLDGHTH PHDDHPSVSS GLPSDAYSRP SLSLSSSTSI SPPPDRDDKR
SSYTGSLTAK PFTPSVAGGG GGGPSQAALA AGADYISLSE QPEAPPLVDA SFDEDVLRAL
CTLDCSVPLM TDRLKQDLAA TKEVAGFLKR RAAVEDEYGR KLLKTARSTA ESYALSDGKA
GSFVNAWSQC LRIHERMGEN RVRYASRLRE MADDLGKLSA ETERARQTHK DAAESAEADL
RASEQSTEKA KLRLDGSADE LERLLLAKEG ESAKDGVQIR PPGAGGTGKR ALGKATALLK
GRGPAAIQRQ EEDVRTRLNA NGVSYNKSME DTQKRRQEYF GFHLPRTLRA LKEASDEIDL
GTQYHLQRYA FLTESIVMAD GQILAPTTNT IGKDGKEEDN TGLQAALAAL DYRADFRVYM
QNYAYAHGGT AKGPRRTGPE HEGFLPPLPQ HVPSPRTALP TNGFPPPPTS ASSTTTPLPP
PPPLQIPPRA TFGIPLSSQL LRDNAEIPPI LIKLTSFIEK YGLLSQGIYR LSGTMSKINK
LKGLLDEGLD KVDLDREEWK GDVNNVASAA KAWFRELPEG VMTDALRLGF LDAAAIENDR
LRHIRLHERI NDLPDANYAT LKFFLGHLSR IAQHADANQM SVGNLAIVFG PTLFGSPAGA
GQGSGGGGEL VLQNKAIETI LEHYADIFID EGEAEQPGPA VP
//