(data stored in SCRATCH zone)

SWISSPROT: Q6BMT7_DEBHA

ID   Q6BMT7_DEBHA            Unreviewed;       627 AA.
AC   Q6BMT7;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   11-DEC-2019, entry version 75.
DE   RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR037514};
GN   OrderedLocusNames=DEHA2F02684g {ECO:0000313|EMBL:CAG88791.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 /
OS   IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88791.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88791.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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:PIRNR037514}.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC       {ECO:0000256|PIRNR:PIRNR037514}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382138; CAG88791.2; -; Genomic_DNA.
DR   RefSeq; XP_460483.2; XM_460483.1.
DR   STRING; 4959.XP_460483.2; -.
DR   EnsemblFungi; CAG88791; CAG88791; DEHA2F02684g.
DR   GeneID; 2903066; -.
DR   KEGG; dha:DEHA2F02684g; -.
DR   HOGENOM; HOG000248782; -.
DR   InParanoid; Q6BMT7; -.
DR   KO; K23460; -.
DR   OMA; YPKWGGL; -.
DR   OrthoDB; 1017439at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0016020; C:membrane; IEA:EnsemblFungi.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:EnsemblFungi.
DR   GO; GO:0017137; F:Rab GTPase binding; IEA:EnsemblFungi.
DR   GO; GO:0090630; P:activation of GTPase activity; IEA:EnsemblFungi.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR   GO; GO:0018344; P:protein geranylgeranylation; IEA:EnsemblFungi.
DR   GO; GO:0006612; P:protein targeting to membrane; IEA:EnsemblFungi.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR017230; Mrs6.
DR   PANTHER; PTHR11787; PTHR11787; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PIRSF; PIRSF037514; Rab_ger_ger_transf_A_fun; 1.
DR   PRINTS; PR00891; RABGDIREP.
DR   PRINTS; PR00894; YEASTMRS6P.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BMT7.
DR   SWISS-2DPAGE; Q6BMT7.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
FT   REGION          572..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          427..450
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        583..606
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..627
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   627 AA;  70279 MW;  CB2D06173FE0DE5E CRC64;
     MSSFNRSERR KSVAERRPSV PYIAPVIPHL AGLEKPQEHS LKMDHCDVLI MGTGLVESIL
     AAALSWQGVE ILHIDNKQYY GDSTSTLTID QLKKWCMEVN QGKVQHFHDA QFYMPGGKLK
     DQFHSKDYGI DLTPKIMFAQ SDLLSLLIKS RVYKYLEFQS LSNFHVFEND NFNKKLSNTT
     KEDIFTDQSL SLVTKRYLMK FLKFVLQDNN DQNKKSMLQD NANVPIGEFL TKNFNLETPQ
     INELVYSIGL CAKTTTKTPE ALTRIKRFLV SFDVYGNFPV MVSKYGGPGE ISQGFCRSAA
     VAGTTYKLNT TLVDYDPQSK IARFNDGSNI KINEKVVVSP TQMPKFLQQS YNEITEDLKP
     YNVTRLVTIV KNDCKEWMSE QETSAIVVFP PNSLPTSNQQ SVQVIIQNGG SGVCPEGQAV
     WFSHSSEQDL NKAKQDLECA HEKMESAILR ESSNNLDEVL DDKDFVLSAQ GTPVLVNSIK
     LGESLQSFVP EEKLEIVCKL GYVQKTFVKP DLSNVIAPTP ENNVSSATIS DAEDIIFSNM
     PSSEISYDGI IGECKSIFSR ITGSDEDFFD VDFEDEDDDY NNHQAPSTNS KTTSDSTTTN
     NIGSPILDSV LDDEGHHEPF GADEMEL
//

If you have problems or comments...

PBIL Back to PBIL home page