ID A0A0F4YK45_TALEM Unreviewed; 634 AA.
AC A0A0F4YK45;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Rho GTPase activator (Rgd1) {ECO:0008006|Google:ProtNLM};
GN ORFNames=T310_7537 {ECO:0000313|EMBL:KKA18500.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA18500.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA18500.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA18500.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA18500.1}.
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DR EMBL; LASV01000448; KKA18500.1; -; Genomic_DNA.
DR RefSeq; XP_013325112.1; XM_013469658.1.
DR AlphaFoldDB; A0A0F4YK45; -.
DR STRING; 1408163.A0A0F4YK45; -.
DR GeneID; 25319809; -.
DR OrthoDB; 5482027at2759; -.
DR Proteomes; UP000053958; 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 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; 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:UP000053958}.
FT DOMAIN 30..297
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 441..631
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 634 AA; 69792 MW; A2C053D417618AAB CRC64;
MAEVASSDAQ LPPALPSQDD SASPAGVRPQ SSSGQNTGPE TAAADPDKER IDRVLQSEDF
ATFLKKRAAL EEEHAQGLKK LARLSQETTH RSDHRQGTYS RAQDEVNRIQ ERMADHGLQF
AVSLQQMSED LQELASNIER GRKQWKQTGL NAEKKVQDAE SQVEKAKAKY DSLAEQYDRV
RTGDKQSGKF GLKGHKSAAQ HEEDLHRKVQ NADSDYQAKV QAAQTARQEL VSTHRPQTVH
HLQRLIYECD SGLTLQLQKF AAFNEKLLLG QGLCVSPLNS GSKSMREVIH QIDSEKDFND
YILSFAGNPG AVAAPEVQYT PHPTLAPASA PSAPPSQPNT QNKRQSLALH AAMPSQQSLG
PTSPPQTSPQ AGQGSTLPPS FSPQPSSEGY QAYHPPYPTD PTPPPLQQPV SSGPPMGRSP
VLQPTNGYQP NLPPLNPVFG VSLEELYRRD GSAVPMIVYQ CIQAVELFGL DVEGIYRLSG
SANHINHMKA LFDNDSSQVD FTNPESFYHD VNSVAGLLKQ FFRELPDPLF TRQYYQDFIN
AARIDNDVQR RDTLHAIINN LPDPNYATLC ALVLHLNKVQ EHYPQNRMNA GNLAICFGPT
LMGANSGGNI ADAGWQARVI ETVLLNTFQI FDDD
//