ID A0A2K3QMT1_9HYPO Unreviewed; 607 AA.
AC A0A2K3QMT1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Ran-binding protein 10 {ECO:0000313|EMBL:PNY28842.1};
GN ORFNames=TCAP_01237 {ECO:0000313|EMBL:PNY28842.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY28842.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY28842.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY28842.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PNY28842.1}.
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DR EMBL; NRSZ01000200; PNY28842.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QMT1; -.
DR STRING; 45235.A0A2K3QMT1; -.
DR OrthoDB; 38145at2759; -.
DR Proteomes; UP000236621; Unassembled WGS sequence.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:UniProt.
DR CDD; cd12909; SPRY_RanBP9_10; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035782; SPRY_RanBP9/10.
DR PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000236621}.
FT DOMAIN 106..298
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 384..441
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT REGION 68..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 67202 MW; 4BE82C600F70E66B CRC64;
MGDPANGRTE AIWSTSGTMP PYSRAFDIFS APFDDDDESA GGDGHFFVPS YLKGSTYMQM
LEEAHKAKLQ AQKESKRSTV NGSANNSSAP FNQPPLPPGA HRGMAHNVIE RPPAFEDDDA
LAPLPARWNK DDIWSGIEVE SDNLSVKYTG GKNHHEREHE ASAVRADRHM PPQCGIYYFE
VQILHGKRDD TTVAIGFSTK TASLARPVGW EPESWAYHGD DGRCYTGQTN GRTYGPTFNA
GDVVGCGVDF RDRTAFFTRN GVKLGGAFHD ISRSKLYPSI SLKKPGEVIV ANFGQLPFVY
NIDDLMREQR EKIQKAIEST DTSRLEPGMN ETDLIQTLVL QFLQHDGYVE TARAFAEDMR
TQKEALNLDP NVKVDGINIK DDEDANNRQR IRRAILEGDI DRALKHTNAY YPQVLRDSEE
VYFKLRCRKF IEMVRKAAQM RSGSDSKGSN GRGSRSSSQD MDLDLDGSDN AAWGETLEMD
GSEQPVELMK LEQSMLEYGQ ALEAQYANDP RKEVSKALGE IWALVAYSNP LTEPQVSHLL
DRKGRAAVAE ELNSAILSSL GKSSRASLEQ VYAQTSALLE NLRQDGGPGA FVSLQGLVEG
ITAFPQI
//
