ID A0A2A9NWX8_9AGAR Unreviewed; 569 AA.
AC A0A2A9NWX8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=B30.2/SPRY domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMATHDRAFT_134637 {ECO:0000313|EMBL:PFH54698.1};
OS Amanita thiersii Skay4041.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pluteineae; Amanitaceae; Amanita.
OX NCBI_TaxID=703135 {ECO:0000313|EMBL:PFH54698.1, ECO:0000313|Proteomes:UP000242287};
RN [1] {ECO:0000313|EMBL:PFH54698.1, ECO:0000313|Proteomes:UP000242287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKay4041 {ECO:0000313|EMBL:PFH54698.1,
RC ECO:0000313|Proteomes:UP000242287};
RG DOE Joint Genome Institute;
RA Hess J., Skrede I., Wolfe B., LaButti K., Ohm R.A., Grigoriev I.V.,
RA Pringle A.;
RT "Transposable element dynamics among asymbiotic and ectomycorrhizal Amanita
RT fungi.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ301969; PFH54698.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9NWX8; -.
DR STRING; 703135.A0A2A9NWX8; -.
DR OrthoDB; 38145at2759; -.
DR Proteomes; UP000242287; 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:SF3; GLUCOSE-INDUCED DEGRADATION PROTEIN 8 HOMOLOG; 1.
DR PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1.
DR Pfam; PF10607; CTLH; 1.
DR Pfam; PF08513; LisH; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 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:UP000242287}.
FT DOMAIN 17..207
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 332..390
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 62603 MW; 33792FCDB5CF2671 CRC64;
MSPPTDSDDD SNASPPREPP PVSPVLLPPV HVLRLPTRWS DQVKHSSLSV TADGRDLSYN
GSACTGERDA AAARTSHPIP PACGIYYYEI EILSKGQKGH ISVGLFAGRD VKLNRLPGCE
MNSWGYHSDS GCSFAAEKNG TPYGPTYVGD IIGCGIDFTS HKAFFTKNGT LLGNAFEGIG
KDIELYPSVG LQHNGELIRV NFGHEPFKFD IDYHVQQQRN STWRKILSTP LDVTLLLDGP
QKHNNEDRDD SKGKHTPQSS ISEAQTRSMM NKLVLSYLIH HGYAKTAQAL QRQEMLLKMK
LPQPSKPVTK SGDQDMDMDA NGSTEETSLS TAIERRTRIV NAVVAGDIDL AISETEKYHP
IVFETEAGLM LFKLRCRKFV ELVLEASELK KRLRTSQSKP SVDDDVMEMS MDVDDDITIA
RHSDNAMGTN GFVSSTTYST WPEKGKESAT TLVEQALSRA IAYGQVLAND YKADTRSEVR
QLFKRTFAIV AWDDPREAGG LVAEVVSLEA RINLANELNQ TILRSQGHPT RPALETLCRH
TATCVTQLGL LGVGAAAFAD MSRELFSET
//
