ID A0A2B7XS17_9EURO Unreviewed; 692 AA.
AC A0A2B7XS17;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Protein FYV10 {ECO:0000256|ARBA:ARBA00018741};
DE AltName: Full=Protein fyv10 {ECO:0000256|ARBA:ARBA00017917};
GN ORFNames=AJ80_05884 {ECO:0000313|EMBL:PGH14564.1};
OS Polytolypa hystricis UAMH7299.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Polytolypa.
OX NCBI_TaxID=1447883 {ECO:0000313|EMBL:PGH14564.1, ECO:0000313|Proteomes:UP000224634};
RN [1] {ECO:0000313|EMBL:PGH14564.1, ECO:0000313|Proteomes:UP000224634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH7299 {ECO:0000313|EMBL:PGH14564.1,
RC ECO:0000313|Proteomes:UP000224634};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-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:PGH14564.1}.
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DR EMBL; PDNA01000092; PGH14564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XS17; -.
DR STRING; 1447883.A0A2B7XS17; -.
DR OrthoDB; 38145at2759; -.
DR Proteomes; UP000224634; 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:UP000224634}.
FT DOMAIN 193..385
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 471..528
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 76181 MW; 5CB3FDD25B05B887 CRC64;
MTNAPPPPGS GGAPSTSHPS GLTFSSMPRR SSYASVVSGT AAAQNLYSPT WSGPLSNLVT
STPSSSYPPQ YQPDSRLHRY SSAIESDMQT NGGGTSGGGW RRAAPIPSHS RQFANSIDYV
EYPHGQQSSN SFFTPSYLKT SKYVAQLAAA HRSKSSSAQK DPSSNHSSAA PSLSASSSNV
NLHRMAPSHR GMTYDIIEHQ PPSEDDNLVP LPSKWNEADK YGGLDILGEG LEIRYMGAIC
KHEHEAAAVR ADHPMPRQCG IYYFEITVLA KSKDGIISIG FSSPKASLER LPGWEQESWA
YHGDDGKIFF GDNQGQGKDY AKPFAVNDTV GCGVNFSTGT AFFTKNGVYL GNAFRELKNV
KLYPSIGMRK FPGSHIKANF GQFPFIFDID GMMGKERHCV QADINTTSVA SLHPTLDESS
LIQELVAQFL AHDGYVETAQ AFAEEVREEA QALHSGQDVP LKDYEVVEDV DAINRQKIRA
AILEGDIDKA LKFTNAYYPN VLEDNPQIYF RLRCRKFIEM MRRCTEPQGF ASKRSKSSNG
AAHDTSDDVF THDMELDEQM KDAEDSSDIM EMEDSDYGMK YQDLLHETIM YGQELQADYP
GDEKREYKKT LDDIFSLVAY PDPKSSVHGH LLEPSGRVPV SEELNSAILV SLGRSSSAAL
EKLYQQTEVL FNEISEEGGA GAFINVRNDF LI
//
