ID A0A2P5A938_PARAD Unreviewed; 253 AA.
AC A0A2P5A938;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Rho protein GDP-dissociation inhibitor {ECO:0000313|EMBL:PON33048.1};
GN ORFNames=PanWU01x14_355920 {ECO:0000313|EMBL:PON33048.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON33048.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-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}.
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:PON33048.1}.
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DR EMBL; JXTB01000760; PON33048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5A938; -.
DR STRING; 3476.A0A2P5A938; -.
DR OrthoDB; 5472794at2759; -.
DR Proteomes; UP000237105; 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:UP000237105}.
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 253 AA; 28575 MW; 1A1D0A675DB537CF CRC64;
MSLAIGVVSS SSSKSMGFDD KDNEAGEETK RREEKGLVER ENVVDEEPAG MNRTMSESSI
YATEDDEDDE AGRKIVLGPQ FTLKEQLEKD KDDESLRRWK EQLLGSVDMD SVGETLEPDV
KILSLAIKSP GRQDIVLTIP ENGNRKGSWF TLKEGSRYSL MFTFQVSNNI VSGLKYTNTV
WKTGVRVDST KEMLGTFSPQ SEPYTHEMPE DTTPSGLFAR GSYSARTKFV DDDNKCYLEI
NYTFEIRKDW QSP
//
