ID G4U748_NEUT9 Unreviewed; 490 AA.
AC G4U748;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Rab proteins geranylgeranyltransferase {ECO:0000256|PIRNR:PIRNR037514};
GN ORFNames=NEUTE2DRAFT_78989 {ECO:0000313|EMBL:EGZ77450.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ77450.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ77450.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|PIRNR:PIRNR037514}.
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DR EMBL; GL890999; EGZ77450.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U748; -.
DR STRING; 510952.G4U748; -.
DR eggNOG; KOG1439; Eukaryota.
DR HOGENOM; CLU_021695_3_1_1; -.
DR Proteomes; UP000008513; 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 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 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:UP000008513}.
SQ SEQUENCE 490 AA; 53405 MW; 6BABC759B8CA899C CRC64;
MAMGSIGDTL WDVVICGTGL QQSLLALSLS RSGKNILHID PNDYYGGAEA AFSLQEAESW
VDRLATEDKG LFRSASITKP DVVGLSFPRA YSLALAPQLI HARSELLSQL VSSRAYRQVE
FLAVGSFYIF KAPIDPEQQP SLVRIPSTRE DVFSTTAISA KAKRGLMKFL RFVLDYDSPE
QRDAWKPFAD KPLVDFLQEH FKMDTELKTY IITLTLSLDG RINTEDGLFV VHRHLTSMGH
FSPGFAALYP KWGGISEIAQ VACRAGAVGG AVYMLGAGIK SMDTATDEIE LELTSGDKVK
TKLLVRGEES VGDEPIISRL VAVVDSPLKI LFDSTVDGAP TPCVAVVALP PGSLTTPGEA
NTDPVYVFAH SSGTGECPNG QSVLYLSTMA TSNSKEILSR SLESLLFAVD RDRVPQCLYQ
LYYEQAAGVK QSRLDGLILD LPGPSLSLLM DDASLNHVRE AWKKVVGDAV DDAEYMVFTA
REPVDDDDYE
//