ID U7PV33_SPOS1 Unreviewed; 551 AA.
AC U7PV33;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Rab proteins geranylgeranyltransferase {ECO:0000256|PIRNR:PIRNR037514};
GN ORFNames=HMPREF1624_04688 {ECO:0000313|EMBL:ERS99488.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS99488.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|PIRNR:PIRNR037514}.
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DR EMBL; KI440845; ERS99488.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PV33; -.
DR STRING; 1391915.U7PV33; -.
DR eggNOG; KOG1439; Eukaryota.
DR HOGENOM; CLU_021695_3_1_1; -.
DR OrthoDB; 8704at2759; -.
DR Proteomes; UP000018087; 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; 2.
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 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:UP000018087}.
FT REGION 473..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 58095 MW; 3F4E74D0E962A66C CRC64;
MESLSDTIWD VVICGTGLQQ SLLALALSRS NKNILHIDPN QYYGGSEAAL SVAEADAWAA
ARPEASAARP TAAIDGAVQL GPLSAYSVAL APQFLHARST LVELLVSSRA FRQLEFLAVS
SFFVLESSSS SSSSSGPANP SLARIPATRE DVFASTAMPA RAKRQLMKFL KFVLAFDGTD
TGDDKGDGDS AWQSHASEPL GAFLQTSFGL DDRLRDNVLA LTLSLDGAAV TVAHGLARLH
RHITSMGLFG PGFAAVYPKW GGCGEIVQVA CRAAAVGGGI YMLGSGIKSV SVTAPVEGDT
QQDQLLELEL TRDMTVKTKL LVRGSEAIGG PSSEDVPAST SKQSGQHLSR LIAVIGAPLP
FLFAPTVEGA PVAGGAVIAL PAGRPVLADG AASEHPVFVM AHSSDTGECP VGQSVLLFTT
IRTEGSKAVL ESALTTLLVA FAKETSSDAE GRANDESPSI PVLYSLYYEQ PRGEEARAPD
AEPEPEPQPE PETPLGVFRF PPLPVDLMVQ DAPLEVVREA WRRVMGPEED DAAYMAFVDR
EGNDADDMEY D
//