ID C6HRY4_AJECH Unreviewed; 537 AA.
AC C6HRY4;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 03-MAY-2023, entry version 47.
DE RecName: Full=Rab proteins geranylgeranyltransferase {ECO:0000256|PIRNR:PIRNR037514};
GN ORFNames=HCDG_08965 {ECO:0000313|EMBL:EER36802.1};
OS Ajellomyces capsulatus (strain H143) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544712 {ECO:0000313|EMBL:EER36802.1, ECO:0000313|Proteomes:UP000002624};
RN [1] {ECO:0000313|Proteomes:UP000002624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H143 {ECO:0000313|Proteomes:UP000002624};
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.M.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S.,
RA Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J.,
RA Yandava C., Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S.,
RA Nino-Vega G., San-Blas G., Taylor J.W., Mendoza L., Galagan J.E.,
RA Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain H143.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593, ECO:0000256|PIRNR:PIRNR037514}.
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DR EMBL; GG692437; EER36802.1; -; Genomic_DNA.
DR AlphaFoldDB; C6HRY4; -.
DR STRING; 544712.C6HRY4; -.
DR VEuPathDB; FungiDB:HCDG_08965; -.
DR eggNOG; KOG1439; Eukaryota.
DR HOGENOM; CLU_021695_3_1_1; -.
DR OMA; VGSWWIY; -.
DR Proteomes; UP000002624; 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; 1.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002624};
KW Transferase {ECO:0000313|EMBL:EER36802.1}.
FT REGION 58..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 57350 MW; F372C08F06E20121 CRC64;
MEPLTDVDWD VLISGTGLPQ SILRCKKVLH VDKHGYYGGS DAALSLHETE DWVTRINEAP
GSTPFESASI STSPASSEDG GSGKLSPSRA YTLSLSPQLI YSRSGLIPTL VSSRIFRQLE
FQAVGSWWVM EHGSSASLNR VPGSREDVFA NDNMSNKSKR ALIKLLRHLT QQSLDDGDAD
GGEDSDLDVV PFTQYLESKF HIPSDLHCPL TSLSLSPRSW DETSARYGVE RIKRHLGSIG
VFGVGFGALL AKWGGGAEIS QVGCRACAVG GGVYVLNRGV RHIEVPAAGS QNDDARRLRV
QLSDGGTVRS KFVVGSPWDL PTEIQSPTSP KYTKVARSIM IVSSPLESLF PLTSEGGVIP
AGAVVFVPGP PGTTRAPVYL IVHSSDTGEC PTGQSIIYGS TLAGDDDDDD DNRQSESQSL
IRSAATNLLR AADADAKILW SAQYTQLGLL SRAPSPSASA SPRAEAATVS SSSLTGRVFL
FAPLNLDLAF DEGMLAQVRA VWEAVTGGDA EEERGQFCQF EDRESMDEGE GDEAGLN
//