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Database: UniProt
Entry: A0A168HDA3_CORDF
LinkDB: A0A168HDA3_CORDF
Original site: A0A168HDA3_CORDF 
ID   A0A168HDA3_CORDF        Unreviewed;       501 AA.
AC   A0A168HDA3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Rab proteins geranylgeranyltransferase {ECO:0000256|PIRNR:PIRNR037514};
GN   ORFNames=LEL_04449 {ECO:0000313|EMBL:OAA77626.1};
OS   Akanthomyces lecanii RCEF 1005.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC   Cordyceps confragosa.
OX   NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA77626.1, ECO:0000313|Proteomes:UP000076881};
RN   [1] {ECO:0000313|EMBL:OAA77626.1, ECO:0000313|Proteomes:UP000076881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA77626.1,
RC   ECO:0000313|Proteomes:UP000076881};
RX   PubMed=27071652; DOI=10.1093/gbe/evw082;
RA   Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT   "Divergent and convergent evolution of fungal pathogenicity.";
RL   Genome Biol. Evol. 8:1374-1387(2016).
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|PIRNR:PIRNR037514}.
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:OAA77626.1}.
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DR   EMBL; AZHF01000003; OAA77626.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168HDA3; -.
DR   STRING; 1081108.A0A168HDA3; -.
DR   OrthoDB; 8704at2759; -.
DR   Proteomes; UP000076881; Unassembled WGS sequence.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
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; IPR017230; Mrs6.
DR   PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR   PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PIRSF; PIRSF037514; Rab_ger_ger_transf_A_fun; 2.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076881};
KW   Transferase {ECO:0000313|EMBL:OAA77626.1}.
SQ   SEQUENCE   501 AA;  53789 MW;  7843EF39478CB487 CRC64;
     MESLSDTDWD VVISGTGLQQ SLFALALSRS GKNILHVDPE GYYGEHEAAF SLQEADAWAQ
     KHASPDAPGI FRAAKVTKVT KADGPPSPRG YSLALAPQLI HARSELLNKL VSSKAFRQIE
     FQAVGSFFIF QAETEDATTP TLARIPSTRE DVFLSTAIPV RAKRSLMKFL KFVFDFESES
     QAEVWKPHAD KPLAEFLSSE FKLDTMLQSY IITLTLSLDG NISVENGLAV ISRHLGSMGV
     FGAGFAAVYP KWGGLSEVCQ VGCRAAAVGG AVYMLGTGIT QVAKRSDEAV KLDISLSNDM
     VVRAKTLFRG SETSPADGVS LARTTAVIGT ALPNLFETVV EGSPTPSAIV VAFPAGLVAG
     GNGHMSQYPI YAMVHSSDTG ECPVGQCVVY LSTISTPSSR ALLDTALSSL LQAASGNLEP
     PEVVFRLQYE QRGARLPSLN ADDSIVTFGA PVLDLAFRDD MLQPVRQAWE NFAGQTGEQA
     DAEYLVFEDR EVVDDDDVFD A
//
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