ID A0A135LZE0_PENPA Unreviewed; 519 AA.
AC A0A135LZE0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 03-MAY-2023, entry version 21.
DE RecName: Full=Rab proteins geranylgeranyltransferase {ECO:0000256|PIRNR:PIRNR037514};
GN ORFNames=PGRI_074800 {ECO:0000313|EMBL:KXG54336.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG54336.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG54336.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG54336.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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:KXG54336.1}.
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; LHQR01000013; KXG54336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LZE0; -.
DR STRING; 5078.A0A135LZE0; -.
DR OMA; VGSWWIY; -.
DR OrthoDB; 8704at2759; -.
DR Proteomes; UP000070168; Unassembled WGS sequence.
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; 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:UP000070168}.
SQ SEQUENCE 519 AA; 56736 MW; 7E9115EE31451640 CRC64;
METLSDTTWD VIINGTGISQ SLLALALSRS GKKVLHIDPN QYYGGSDAAF SLDEAQEWAE
KVNKGELLLS TFKDASIFKP EVSPSSEETG ISPKLASSRA YTLSLSPYFL YARSQLMSAL
VTSKVFRQLE FMAVGSWWIY VPEQPDSKNG ELGAEKIFYR VPGNREDVFA ATHISMKSKR
TLMRLLRHIT KPNEDDASIE DEDMSMPLND YLASKFSVPE ELHNPLLSLS LSQLSQQDTS
ASYALPRVQR HLSSIGHLGP GFGAVIPKYG GGAEILQAAC RASAVGGGVY ALDTRISDCL
WRNSSEHSEY PFLLKLNEGP VQGKYFFNSN LDTSPKENLT PLVEVARSIS VVSATFPSLF
PATVEGAPVP ATAVLMFPGD TLGSPQSPPV YLQVHSSDTG ECPPQQSVIY CSVALAGPEG
QALIESAVDR LIRAEGLPAT VLWSLRYTHR GPLSNGAPQR FIVEDEVSHC YNFPPSSLDL
AFEDDTLDLV KEAWKKVVGD EVDDADFMMF DDRDGTSDQ
//
