ID A0A0G4EJF9_VITBC Unreviewed; 770 AA.
AC A0A0G4EJF9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Rab proteins geranylgeranyltransferase component {ECO:0008006|Google:ProtNLM};
GN ORFNames=Vbra_3962 {ECO:0000313|EMBL:CEL97118.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEL97118.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEL97118.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593}.
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DR EMBL; CDMY01000254; CEL97118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4EJF9; -.
DR STRING; 1169540.A0A0G4EJF9; -.
DR VEuPathDB; CryptoDB:Vbra_3962; -.
DR InParanoid; A0A0G4EJF9; -.
DR OMA; PTHIIAR; -.
DR OrthoDB; 231046at2759; -.
DR PhylomeDB; A0A0G4EJF9; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; 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; 2.
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 PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR Pfam; PF00996; GDI; 3.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000041254}.
FT REGION 99..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 83392 MW; 7151E66CF427FAF8 CRC64;
MASEGFIDTL STLESWHFAC EGDQSPRFLA LVRRRNLSRM LLDEGEREFD VCVVGTGLIE
CLIAASLSRC GLKVLHLDGR DYYGGNWSSL NYKQLKLWSQ GREQPEPPTD QQLQADGQTA
PPPGEEWVPL DDVGSDSGVT SSCFVDRFMA TEPFLLDESE PASAASASAS GGGGGGGGGC
ETTEERLVRQ SNQFCVDVCP RLLYCRSDLV DILLRSGVSR YLEFKGMEGL FTWSDGDWFR
LPFSRSDIFQ SSALSLIEKR LLMKFLTSLT AAQSSAAFHT PKALQGRDLP TASTAAAAAA
SDTDNEAEDS GDGGDESGVL DGTWFEYMGS HQLTDRLQSL MTYGVCMGEE RHPQWTARQG
VDRVERIIRS LGIYAAGSPF LYPMYGTAEL PQAFTRVCAL HRGLYMLRCR PTHIIARQGD
NEKNRLVGLR LDNGQTIQAS RLISSPDYIP PPQTTPAPSP IPSVLHLIAL TDRALLADPS
PRERPSEART RPSPVPSDTE TTASETNGGG KVGVGAGAVL EDGMTNPVQL LQVDHTTGCC
PRGLFLTHLC QRAPTTLPDA AAASAAECTR VDGASPAFDE LVRVLQRLLE ARGGAQSCRV
VVGYRQYVRR DSLDCLPDPA TDAQSASEPP AEGPTSDVWG SLDGLVRQRD VIVCPDPPTQ
PSFPMQWEPQ MAAKVVWSCL RDHIREHGPI EMDAPVQPDG EPSPPLPPYT EGMLMSACTS
VVDILQPVIS QLEQQAREEQ HQEQGGSDEA AEHNEQGGAA CDNQTDGPGK
//
