ID A0A1Y3NCB2_PIRSE Unreviewed; 204 AA.
AC A0A1Y3NCB2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Rho GDP-dissociation inhibitor {ECO:0008006|Google:ProtNLM};
GN ORFNames=PIROE2DRAFT_67213 {ECO:0000313|EMBL:OUM65399.1};
OS Piromyces sp. (strain E2).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=73868 {ECO:0000313|EMBL:OUM65399.1, ECO:0000313|Proteomes:UP000195826};
RN [1] {ECO:0000313|EMBL:OUM65399.1, ECO:0000313|Proteomes:UP000195826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2 {ECO:0000313|EMBL:OUM65399.1,
RC ECO:0000313|Proteomes:UP000195826};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "A Parts List for Fungal Cellulosomes Revealed by Comparative Genomics.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Rho GDI family.
CC {ECO:0000256|ARBA:ARBA00009758}.
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DR EMBL; KZ150835; OUM65399.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3NCB2; -.
DR STRING; 73868.A0A1Y3NCB2; -.
DR OMA; YKPTAAK; -.
DR Proteomes; UP000195826; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR Gene3D; 2.70.50.30; Coagulation Factor XIII, subunit A, domain 1; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000406; Rho_GDI.
DR InterPro; IPR024792; RhoGDI_dom_sf.
DR PANTHER; PTHR10980:SF3; LD16419P; 1.
DR PANTHER; PTHR10980; RHO GDP-DISSOCIATION INHIBITOR; 1.
DR Pfam; PF02115; Rho_GDI; 1.
DR PRINTS; PR00492; RHOGDI.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000195826}.
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 204 AA; 23083 MW; A1605CEB6F7CB6F7 CRC64;
MSNQNIDQPV SNGDSLEDLN PTQTEGYKVG EKKTIDELKN LDAEDESLNK WKESLGLKAA
VGPADDPRKV VVLSLAMEID GRDDVVLDVS SPEKLANLKD NPMTIKEGVE YKLKIKFKIQ
HEVVSGLKYI HVVKRKGIKV DRDEEMIGSF GPKLEPYEKK FAAEVAPSGF ISRGHYTVKS
RFIDDDNVCH LEFEWSFDIK KDWD
//