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Database: UniProt
Entry: A0A161TEE8_XYLHT
LinkDB: A0A161TEE8_XYLHT
Original site: A0A161TEE8_XYLHT 
ID   A0A161TEE8_XYLHT        Unreviewed;       688 AA.
AC   A0A161TEE8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=SPRY domain-containing protein {ECO:0000313|EMBL:KZF24307.1};
GN   ORFNames=L228DRAFT_245217 {ECO:0000313|EMBL:KZF24307.1};
OS   Xylona heveae (strain CBS 132557 / TC161).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC   Xylonales; Xylonaceae; Xylona.
OX   NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF24307.1, ECO:0000313|Proteomes:UP000076632};
RN   [1] {ECO:0000313|EMBL:KZF24307.1, ECO:0000313|Proteomes:UP000076632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC161 {ECO:0000313|EMBL:KZF24307.1,
RC   ECO:0000313|Proteomes:UP000076632};
RX   PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA   Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA   Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The genome of Xylona heveae provides a window into fungal endophytism.";
RL   Fungal Biol. 120:26-42(2016).
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DR   EMBL; KV407456; KZF24307.1; -; Genomic_DNA.
DR   RefSeq; XP_018189862.1; XM_018332111.1.
DR   AlphaFoldDB; A0A161TEE8; -.
DR   STRING; 1328760.A0A161TEE8; -.
DR   GeneID; 28897248; -.
DR   InParanoid; A0A161TEE8; -.
DR   OMA; LPTRWNK; -.
DR   OrthoDB; 38145at2759; -.
DR   Proteomes; UP000076632; 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:UP000076632}.
FT   DOMAIN          195..383
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   DOMAIN          469..526
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          160..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   688 AA;  75414 MW;  F67FE0B02C79BBDF CRC64;
     MTNTLPQGPS GPGSTPYSST SNPRSFLMPR RSSYASVLSG SAATNQYTPP MRSGAFSHLL
     HSQSPVPPGG FLGHRASPPQ QSRQVSREMD HVWTLGGSPS APGSWGKGAY SLPGGIHSGF
     GTGAYNFLGP DAESNEFFTP SYLRNSRYVE RLAEAHKAKL AAQKESNTSL SNNGSLSTSS
     SSANLHKMAP SHRGMTYDII EKEPIKEDVL NPLPSKWNDN DKFAGLELQA DRLEVRFTGP
     SKSHDEAAAV RADRPMPPEC GIYYYEVTVI SKGKEGLIGV GFSGPNVSLN RLPGWEPESW
     AYHGDDGFSF SCTASGKAYG PKFSTSDVIG CGVNFRTGCA FFTKNGVYLG VAFRDLKGAK
     LFPSVGMKRP GEHLRVNFGQ TPFVFDIDGM MAEERQMVRR EINATSATKL HPPLDETSLI
     QALVAQFLAH DGYVETAKAF AEEVREESKA LQSGKTAPGP NLEAEEDLDA VNRQRIRAAI
     LDGDIDTALK HTNAYYPNVL KDNEQIYFRL RCRKFVEMIR QCSDLHLGPE DKHQSSNGRS
     DGAYVDVFDQ QMELDDQNGP EDWSKMDTED SDVGLRYQHL LQETLHYGQE LQLEFREDGR
     KEIKKALEET FSLLAYEDPR TSVVAHLLDP SGRIPVAEEL NSAILVSLGK SSSAALEKLC
     QQTEALINEI SDDGGAGAFI NMANDFLR
//
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