ID G3XWD4_ASPNA Unreviewed; 513 AA.
AC G3XWD4;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 22-FEB-2023, entry version 42.
DE RecName: Full=Rab proteins geranylgeranyltransferase {ECO:0000256|PIRNR:PIRNR037514};
GN ORFNames=ASPNIDRAFT_186787 {ECO:0000313|EMBL:EHA25539.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA25539.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA25539.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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:EHA25539.1}.
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DR EMBL; ACJE01000006; EHA25539.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XWD4; -.
DR STRING; 380704.G3XWD4; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1183226; -.
DR HOGENOM; CLU_021695_3_1_1; -.
DR Proteomes; UP000009038; 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; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
SQ SEQUENCE 513 AA; 54950 MW; 24F410569A72BE9B CRC64;
MESLADTPWD VTISGTGLAQ SLLALALSRS GKNVLHVDRN PYYGGPEAAF SLQEAEEWAA
KVNEDTGELP FEHASVYSES SGDSTGQLAS SRAYTLSLSP QLIYSRSQLL PTLVSSKVYR
QLEFQAVGSW WIYNPETDDS SHLYRVPGSR EDVFADDVIS MKSKRTLMRF LRHLGQAQES
GNVSEGPDPS PEEEGLAVPF SEYLATKFQV PTELHGPLLS LCLSQAAPQQ TSAQYALPRI
KRHLSSIGVF GPGFGALSVK WGGGSEISQV GCRALAVGGG VYVLNTGVKS VGSSIEQDSD
DQSRIQIQLT NDESVKSRYI VGSNWDLPAA TRPSLECDKV ARSISIVSSS LANLFPVTAE
GGPVPVGAVV VFPGSSVGGA DGAPPVYTIV HSSETGECPT GQCVVYSSVS IPGSEGQSMI
EAALQKLFQS AADPNTKVLW SLRYTQLGQG ASHNADLSCP SKNVICLPPV SLDLAFDDTL
IDTVKKAWEL IMGEEAAQHE FMKFEDREGA YEE
//