ID   A0A176VYM0_MARPO        Unreviewed;       444 AA.
AC   A0A176VYM0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=Guanosine nucleotide diphosphate dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN   ORFNames=AXG93_4620s1770 {ECO:0000313|EMBL:OAE25362.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE25362.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE25362.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE25362.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|RuleBase:RU363124}.
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:OAE25362.1}.
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DR   EMBL; LVLJ01002341; OAE25362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VYM0; -.
DR   OrthoDB; 8704at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
SQ   SEQUENCE   444 AA;  49698 MW;  9BF46EC68837FE5F CRC64;
     MDEEYDVIVL GTGLKECILS GLLSVDRLKV LHMDRNDYYG GASASLTLNQ LWAKYRGTEK
     PPASLGSNRE YNVDLVPKFM MANGTLVRVL IHTDVTKYLS FKAVDGSFVY KQGKIYKVPA
     TDVEALKSPL MGLFEKRRAR KFFIYVQDYE EKEPRTHEGM NLRAVKTKEL FAKFGIEENT
     IDFIGHALAL HRDDDYLNQP AYDTVMKVKL YAESLARFAG GSPYIYPLYG LGELPQAFAR
     LSAVYGGTYM LAKPDCKVEF DESGKAVGVT SEGETARAKK IVCDPSYLPN KVKKVGKVVR
     AICIMSHPIP DTNDAQSVQV ILPQKQLNRK SDVYVFCCSF SHNVAPKGKY IAFVSTEVET
     DNPERELEAG LRLLGPIDEK IIDTYERFKP VNESSLDNCF ISESYDPTTH FETTVADVLQ
     MYKGITGKEL DLSVDLSHAS AAEE
//