ID A0A165AVX4_EXIGL Unreviewed; 443 AA.
AC A0A165AVX4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZV79454.1};
GN ORFNames=EXIGLDRAFT_846533 {ECO:0000313|EMBL:KZV79454.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV79454.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV79454.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV79454.1,
RC ECO:0000313|Proteomes:UP000077266};
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).
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593}.
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DR EMBL; KV426616; KZV79454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165AVX4; -.
DR STRING; 1314781.A0A165AVX4; -.
DR InParanoid; A0A165AVX4; -.
DR OrthoDB; 8704at2759; -.
DR Proteomes; UP000077266; Unassembled WGS sequence.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR Pfam; PF00996; GDI; 1.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000077266}.
SQ SEQUENCE 443 AA; 47324 MW; 798AF1E4B04B5654 CRC64;
MDSPTHFDVL VLGTSLPNSI AAAALSKAGL TVLHVDEKDN YGGEHAALAP NDFSQDNLPP
YARQYAIQLA PALVPAVGPL ISAVVASGVS KYGAYKLLDA LALFSDGEMK RVPGSKEDVF
RATHIGLADK HRLMKFLLFA ASDAEVTTDA PFAQYVREEF GLPDALADAV VYALAQCADA
TEPTGPALAR VRAFIRSTGR YGNSPFLVAH YGGLGEIAQG FCRTAAVHGA VYILGRKLVS
LTHDEKWRIE LDGVPDVLTA DVLLTNDTDA KEKTACLVAL TDIVPHMDDS ESSADDALLI
FPPASIPTVV RGLVCGARSM SAPQGHWVVQ LFYTSADPDP ELLRPYLTTL LPSSQPFWEH
TFINPSPSTS SSIALPSAEN VVRIPREKGL GPATLGDWAA EAAERAFWEV VKLVKGEAGA
DDVVWFAQDE TDEVAAADDD EGW
//
