ID   A0A068RPX5_9FUNG        Unreviewed;       443 AA.
AC   A0A068RPX5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   03-MAY-2023, entry version 25.
DE   RecName: Full=Rab GDP dissociation inhibitor {ECO:0000256|RuleBase:RU363124};
GN   ORFNames=LCOR_03743.1 {ECO:0000313|EMBL:CDH52243.1};
OS   Lichtheimia corymbifera JMRC:FSU:9682.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Lichtheimia.
OX   NCBI_TaxID=1263082 {ECO:0000313|EMBL:CDH52243.1, ECO:0000313|Proteomes:UP000027586};
RN   [1] {ECO:0000313|EMBL:CDH52243.1, ECO:0000313|Proteomes:UP000027586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMRC:FSU:9682 {ECO:0000313|Proteomes:UP000027586};
RA   Schwartze V.U., Winter S., Shelest E., Marcet-Houben M., Horn F.,
RA   Wehner S., Hoffmann K., Riege K., Sammeth M., Nowrousian M., Valiante V.,
RA   Linde J., Jacobsen I.D., Marz M., Brakhage A.A., Gabaldon T., Bocker S.,
RA   Voigt K.;
RT   "Gene expansion shapes genome architecture in the human pathogen
RT   Lichtheimia corymbifera: an evolutionary genomics analysis in the ancient
RT   terrestrial Mucorales (Mucoromycotina).";
RL   Submitted (AUG-2013) 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:CDH52243.1}.
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DR   EMBL; CBTN010000012; CDH52243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068RPX5; -.
DR   STRING; 1263082.A0A068RPX5; -.
DR   VEuPathDB; FungiDB:LCOR_03743.1; -.
DR   OrthoDB; 8704at2759; -.
DR   Proteomes; UP000027586; 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:UP000027586}.
SQ   SEQUENCE   443 AA;  49543 MW;  C9E61A115A891D98 CRC64;
     MDEQYDIIVL GTGLTECILS GIFSVEGKKV LHMDRNDYYG GESASLNLKQ LYAKFRPDAE
     VPTDLGRDRD YNIDLIPKFM MANGEIVRFL THTDVTRYLE FKQIAGSFVY RDGKISKVPA
     SETEAISSPL LGMVEKRRLQ KFLEFIQNWK EDDVSTHEGF DLDKDTMIKV YEKFGLEPGT
     QDFIGHAMAL HLDDGYLEKP ARETIDKIIL YVASIARYGK SPYIYPLHGL GELPQSFARL
     SAIYGGTYML DRAADEIVYE NGVAVGVRSG NEVARAKQII CDPSYAKTLV KATGKVVRAI
     CLLKHPIPNT GDADSVQIVI PQNQLNRKHD VYVACVSSNH NVCPKDMYLA IASTVVETDD
     PENEIKAGLD LMGPIHDKFV SVLDLEEPLA DGTSDQVFIS RSYDATSHFE SVCDDVKNIY
     RRMTGSDLVL KQRPTQDQDQ ADA
//