ID G2WNM9_YEASK Unreviewed; 603 AA.
AC G2WNM9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A {ECO:0000256|PIRNR:PIRNR037514};
GN Name=K7_MRS6 {ECO:0000313|EMBL:GAA26672.1};
GN ORFNames=SYK7_067751 {ECO:0000313|EMBL:GAA26672.1};
OS Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=721032 {ECO:0000313|EMBL:GAA26672.1, ECO:0000313|Proteomes:UP000001608};
RN [1] {ECO:0000313|EMBL:GAA26672.1, ECO:0000313|Proteomes:UP000001608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyokai no. 7 / NBRC 101557 {ECO:0000313|Proteomes:UP000001608};
RX PubMed=21900213; DOI=10.1093/dnares/dsr029;
RA Akao T., Yashiro I., Hosoyama A., Kitagaki H., Horikawa H., Watanabe D.,
RA Akada R., Ando Y., Harashima S., Inoue T., Inoue Y., Kajiwara S.,
RA Kitamoto K., Kitamoto N., Kobayashi O., Kuhara S., Masubuchi T.,
RA Mizoguchi H., Nakao Y., Nakazato A., Namise M., Oba T., Ogata T., Ohta A.,
RA Sato M., Shibasaki S., Takatsume Y., Tanimoto S., Tsuboi H., Nishimura A.,
RA Yoda K., Ishikawa T., Iwashita K., Fujita N., Shimoi H.;
RT "Whole-genome sequencing of sake yeast Saccharomyces cerevisiae Kyokai no.
RT 7.";
RL DNA Res. 18:423-434(2011).
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|ARBA:ARBA00005593, 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; DG000051; GAA26672.1; -; Genomic_DNA.
DR AlphaFoldDB; G2WNM9; -.
DR HOGENOM; CLU_021695_3_1_1; -.
DR Proteomes; UP000001608; Chromosome XV.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:UniProtKB-UniRule.
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; 1.
DR PRINTS; PR00891; RABGDIREP.
DR PRINTS; PR00894; YEASTMRS6P.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 603 AA; 67397 MW; 71295C4CD5AA45F6 CRC64;
MLSPERRPSM AEHRPSFFSF TQNPSPLVVP HLAGIEDPLP ATTPDKVDVL IAGTGMVESV
LAAALAWQGS NVLHIDKNDY YGDTSATLTV DQIKRWVNEV NEGSVSCYKN AKLYVSTLIG
SGKYSSRDFG IDLSPKILFA KSDLLSILIK SRVHQYLEFQ SLSNFHTYEN DCFEKLTNTK
QEIFTDQNLP LMTKRNLMKF IKFVLNWEAQ TEIWQPYAER TMSDFLVEKF KLEKPQVFEL
IFSIGLCYDL NVKVPEALQR IRRYLTSFDV YGPFPALCSK YGGPGELSQG FCRSAAVGGA
TYKLNEKLVS FNPTTKVATF QDGSKVEVSE KVIISPTQAP KDSKHVPQQQ YQVHRLTCIV
ENPCTEWFNE GESAAMVVFP PGSLKSGNKE VVQAFILGAG SEICPEGTIV WYLSTTEQGP
RAEMDIDAAL EAMEMALLRE SSSGLENDEE IVQLTGNGHT IVNSVKLGQS FKEYVPRERL
QFLFKLYYTQ YTSTPPFGVV NSSFFDVNQD LEKKYIPGAS DNGVIYTTMP SAEISYDEVV
TAAKVLYEKI VGSDDDFFDL DFEDEDEIQA SGVANAEQFE NAIDDDDDVN MEGSGEFVGE
MEI
//
