ID M1W1D7_CLAP2 Unreviewed; 496 AA.
AC M1W1D7;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Rab proteins geranylgeranyltransferase {ECO:0000256|PIRNR:PIRNR037514};
GN ORFNames=CPUR_04701 {ECO:0000313|EMBL:CCE30851.1};
OS Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE30851.1, ECO:0000313|Proteomes:UP000016801};
RN [1] {ECO:0000313|EMBL:CCE30851.1, ECO:0000313|Proteomes:UP000016801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20.1 {ECO:0000313|EMBL:CCE30851.1,
RC ECO:0000313|Proteomes:UP000016801};
RX PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA Yoshida R., Zeng Z.;
RT "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT Clavicipitaceae reveals dynamics of alkaloid loci.";
RL PLoS Genet. 9:E1003323-E1003323(2013).
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:CCE30851.1}.
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DR EMBL; CAGA01000025; CCE30851.1; -; Genomic_DNA.
DR AlphaFoldDB; M1W1D7; -.
DR STRING; 1111077.M1W1D7; -.
DR VEuPathDB; FungiDB:CPUR_04701; -.
DR eggNOG; KOG1439; Eukaryota.
DR HOGENOM; CLU_021695_3_1_1; -.
DR OrthoDB; 8704at2759; -.
DR PhylomeDB; M1W1D7; -.
DR Proteomes; UP000016801; 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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW Transferase {ECO:0000313|EMBL:CCE30851.1}.
SQ SEQUENCE 496 AA; 53371 MW; 629FA4821A8393CD CRC64;
MESLSETKWD VVISGTGLQQ SLLALALSRS GKNVLHVDSN EYYGAAEAAL SLQEADEWTE
KYASVEGNEP FAAAQVFKDG DGLAASRSYS IALAPQPVHA RSELLNQLVA SKAFRQIEFL
AVGSFFIFQP GSESSGPSLT RIPSTREDVF SNKDIPTRAK RSLMKFLKFV LEYDVEPQTE
LWKSQESEPL AEFLEREFKL DSQTQSYVAT LTLSFQKDTS VGDGLASIHR HLKSMGVFGA
GFAAVYPKWG GLSEVAQVGC RAGAVGGTIY MLGVGVSDTK HISKDGQDLV AISLTNDVTV
ETKTFIRDDV ETSDEGLCVS RLSAIIDAPL SAMFEAVVPG APTPCAAVVA FPAGSVLDED
GTPSQYPIYA LVHSSDTGEC PVGQCVLYLS TPSCLNSQAL LDTALAKLIT AAPSSPSAKC
LWRLRYEQTC GSGSFSMKDN IGTFGRFAPD VAFNDSVLAP VQEAWQIVAG PDADTSSYMR
FEDREGVQDD EDVFDE
//
