ID   A0A0M3IPX5_ASCLU        Unreviewed;       556 AA.
AC   A0A0M3IPX5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR016550};
OS   Ascaris lumbricoides (Giant roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6252 {ECO:0000313|Proteomes:UP000036681, ECO:0000313|WBParaSite:ALUE_0002080301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:ALUE_0002080301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Substrate-binding subunit (component A) of the Rab
CC       geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC       proteins and presents the substrate peptide to the catalytic component
CC       B. The component A is thought to be regenerated by transferring its
CC       prenylated Rab back to the donor membrane.
CC       {ECO:0000256|PIRNR:PIRNR016550}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR016550}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|PIRNR:PIRNR016550}.
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DR   AlphaFoldDB; A0A0M3IPX5; -.
DR   WBParaSite; ALUE_0002080301-mRNA-1; ALUE_0002080301-mRNA-1; ALUE_0002080301.
DR   Proteomes; UP000036681; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.519.10; Guanine Nucleotide Dissociation Inhibitor, domain 2; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR001738; Rab_escort.
DR   PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR   PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR   Pfam; PF00996; GDI; 3.
DR   PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 2.
DR   PRINTS; PR00891; RABGDIREP.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR016550};
KW   GTPase activation {ECO:0000256|PIRNR:PIRNR016550};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        533..553
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   556 AA;  63383 MW;  737AD8521F65728C CRC64;
     MSGEEALPSD VDVVVLGTGL PESIIAAACA RSGLSVLHLD RNDYYGGVWS SFHLQSIAEW
     VDRMKREMDA DPEGDYTDIT LEDGEELIPI GRNQSIESVH LQWHTVEPDT TESEQNGDME
     SDHPIKRDME RNWRRFSIDL LPKVLLSRGA MVQVICDSEV SKYCEFKCVN RLLCLSAKAN
     YAEGPLQELQ VVPCSRSEIF QSEAISMIEK RRIMKFLTSC MQWHEKPDEI DGWSGLYKLS
     FLRTLINFGF YVTVLLSRGA MVQVICDSEV SKYCEFKCVN RLLCLSAKAN YAEGPLQELQ
     VVPCSRSEIF QSEAISMIEK RRIMKFLTSC MQWHEKPDEI DGWSDFADKP FDDFIESRGI
     SGNLKSFVAD TIGILCPNAT AKEGLKAVYR FMESVGRFGD SPFLWTLYGS GELPQCFCRL
     CAVYGGVYCL KQPIDALILK ENRVVAVLTK GQRIRCKHVV MDSSYLPRRY SNDKERRNVL
     QRAILLSNRS LLNDAQKEHI SLLNLMRLDM DASARLLEVG FEACAAPRGY CMFLFYSLCF
     LVFLFVYLIM WSIHML
//