ID M5BQJ8_THACB Unreviewed; 442 AA.
AC M5BQJ8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Rhizoctonia solani AG1-IB WGS project CAOJ00000000 data, isolate 7/3/14, contig 08698 {ECO:0000313|EMBL:CCO30078.1};
GN ORFNames=BN14_04102 {ECO:0000313|EMBL:CCO30078.1};
OS Thanatephorus cucumeris (strain AG1-IB / isolate 7/3/14) (Lettuce bottom
OS rot fungus) (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=1108050 {ECO:0000313|EMBL:CCO30078.1, ECO:0000313|Proteomes:UP000012065};
RN [1] {ECO:0000313|EMBL:CCO30078.1, ECO:0000313|Proteomes:UP000012065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG1-IB / isolate 7/3/14 {ECO:0000313|Proteomes:UP000012065};
RX PubMed=23280342; DOI=10.1016/j.jbiotec.2012.12.010;
RA Wibberg D.W., Jelonek L.J., Rupp O.R., Hennig M.H., Eikmeyer F.E.,
RA Goesmann A.G., Hartmann A.H., Borriss R.B., Grosch R.G., Puehler A.P.,
RA Schlueter A.S.;
RT "Establishment and interpretation of the genome sequence of the
RT phytopathogenic fungus Rhizoctonia solani AG1-IB isolate 7/3/14.";
RL J. Biotechnol. 0:0-0(2013).
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC {ECO:0000256|ARBA:ARBA00005593}.
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:CCO30078.1}.
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DR EMBL; CAOJ01005899; CCO30078.1; -; Genomic_DNA.
DR AlphaFoldDB; M5BQJ8; -.
DR HOGENOM; CLU_021695_3_0_1; -.
DR Proteomes; UP000012065; Unassembled WGS sequence.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR PANTHER; PTHR11787; RAB GDP-DISSOCIATION INHIBITOR; 1.
DR PANTHER; PTHR11787:SF4; RAB PROTEINS GERANYLGERANYLTRANSFERASE COMPONENT A; 1.
DR Pfam; PF00996; GDI; 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;
FT REGION 115..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 48145 MW; B9DB16A1495F7A7C CRC64;
MFATGEFEQS TELQGKETTP LLEFVRDVFG IDKELAEALA YAVAFCVDVK DQTLPALFRT
RAYLRSVGRY GPSPFLIGHY GGAGELAQGF CRTCAVQGGT YVLGRKVVEV TRHDCPTSYP
EKGKQVEKDD KQEDGKETTH RSWTGSSGKS FTSYHPPSTF EGYGVEGAEV PSTDTETEAG
SQTQSQSQTQ AGQPKPEESG TKVEVDAPTP TGPYFRVQLE GFAAPFTANM VIGSEGWLTN
TLGEPKPETS NEPKLGNTIR AILIIDAPAT FASPSEQPAS SEGSSGETRL EESIIILPSE
EGAVSVLVNG ASTMSCPDGK CILYFTAQSS QDPKEYFTKH ISAVLDACSP RPEIRGEVYW
REQELDKVVV RHADPSRQSP PRQEEQFSYS TTHLTEGSDA AAREAERVFW AALGDQPGQD
GKGKDGVEFF ARIEREEDLF DD
//
