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Database: UniProt
Entry: A0A369HHQ3_9HYPO
LinkDB: A0A369HHQ3_9HYPO
Original site: A0A369HHQ3_9HYPO 
ID   A0A369HHQ3_9HYPO        Unreviewed;       199 AA.
AC   A0A369HHQ3;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Rho GDP-dissociation inhibitor {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CP533_1190 {ECO:0000313|EMBL:RDA95636.1};
OS   Ophiocordyceps camponoti-saundersi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039874 {ECO:0000313|EMBL:RDA95636.1, ECO:0000313|Proteomes:UP000253071};
RN   [1] {ECO:0000313|EMBL:RDA95636.1, ECO:0000313|Proteomes:UP000253071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 79314 {ECO:0000313|EMBL:RDA95636.1,
RC   ECO:0000313|Proteomes:UP000253071};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) 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:RDA95636.1}.
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DR   EMBL; PDHQ01000004; RDA95636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369HHQ3; -.
DR   STRING; 2039874.A0A369HHQ3; -.
DR   Proteomes; UP000253071; 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:UP000253071}.
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  22415 MW;  48BA6F74E7A2FA0B CRC64;
     MASSHDDDTM PDETQGYKLS QPKQSLAEYQ QMDANDESLR RYKESLGLGG DKDVSDPSDP
     RVCIILSLTM ESPGREAVTI DLSRPGSEVS LKEHPFKIKE GAKFTMSATF KVQHEILSGL
     HYVQVVKRKG IKVSKDSEMI GSYAPNTVKQ TTYTKKFQEE EAPSGMLARG HYNAVSSFVD
     DDKKKHLEFE WSFDIAKDW
//
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