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Database: UniProt
Entry: A0A165T1B6_9APHY
LinkDB: A0A165T1B6_9APHY
Original site: A0A165T1B6_9APHY 
ID   A0A165T1B6_9APHY        Unreviewed;       449 AA.
AC   A0A165T1B6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN   ORFNames=DAEQUDRAFT_743432 {ECO:0000313|EMBL:KZT72788.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Daedalea.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT72788.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT72788.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT72788.1,
RC   ECO:0000313|Proteomes:UP000076727};
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, ECO:0000256|RuleBase:RU363124}.
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DR   EMBL; KV429039; KZT72788.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165T1B6; -.
DR   STRING; 1314783.A0A165T1B6; -.
DR   OrthoDB; 8704at2759; -.
DR   Proteomes; UP000076727; Unassembled WGS sequence.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
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   InterPro; IPR000806; RabGDI.
DR   PANTHER; PTHR11787:SF8; RAB GDP DISSOCIATION INHIBITOR; 1.
DR   PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PRINTS; PR00892; RABGDI.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076727}.
SQ   SEQUENCE   449 AA;  50237 MW;  7389B7674D84600B CRC64;
     MDEEYDVIVL GTGLTECILS GLLSVEGKKV LHMDRNDYYG GDSASLNLTQ LYRKFRPDQA
     LPTDLGRDRD YAVDLIPKFI IASGELTRIL VHTDVTRYLE FKQIAGSFVY RDGRISKVPS
     TEMEAVKSPL MGLFEKRRAK KFFEFLQNWK DDDPATHQGI NLDKDSMATV YEKFGLEPGT
     QDFIGHAMAL YLDDDYKTKP ARPTYERIVL YTSSMARYGK SPYIYPLYGL GELPQSFARL
     SAIYGGTYML DKSIDEIVTD DSGKFVGVRS GSETVKAKQV IGDPSYFGAG KSAESGKVRV
     VEEGKVIRAI CFLKHPIPGT DDADSAQIII PQNQVNRRND IYIAMVSSTH NVCAKDVYVA
     IVSTIVETDR PEQEIAPGLQ LLGPIYDKFV SVSSLYTPTS SGEADQIFIT RSYDATSHFE
     TVVDEVHNVW KRVVGKELVL KKREVEVEA
//
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