ID A0A0D2BK58_9EURO Unreviewed; 651 AA.
AC A0A0D2BK58;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Protein FYV10 {ECO:0000256|ARBA:ARBA00018741};
DE AltName: Full=Protein fyv10 {ECO:0000256|ARBA:ARBA00017917};
GN ORFNames=PV08_10961 {ECO:0000313|EMBL:KIW11659.1};
OS Exophiala spinifera.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=91928 {ECO:0000313|EMBL:KIW11659.1, ECO:0000313|Proteomes:UP000053328};
RN [1] {ECO:0000313|EMBL:KIW11659.1, ECO:0000313|Proteomes:UP000053328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 89968 {ECO:0000313|EMBL:KIW11659.1,
RC ECO:0000313|Proteomes:UP000053328};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala spinifera CBS89968.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847499; KIW11659.1; -; Genomic_DNA.
DR RefSeq; XP_016231875.1; XM_016385273.1.
DR AlphaFoldDB; A0A0D2BK58; -.
DR STRING; 91928.A0A0D2BK58; -.
DR GeneID; 27338044; -.
DR VEuPathDB; FungiDB:PV08_10961; -.
DR HOGENOM; CLU_009129_2_1_1; -.
DR OrthoDB; 38145at2759; -.
DR Proteomes; UP000053328; 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; 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:UP000053328}.
FT DOMAIN 173..364
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT DOMAIN 449..506
FT /note="CTLH"
FT /evidence="ECO:0000259|PROSITE:PS50897"
FT REGION 27..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 71847 MW; A3678401B2DD18D0 CRC64;
MADGAGSNRG PRSAYFNHIP RRMSYASVAS GANPQSNLPA PQSEPLSHLA ANFTPSSSYP
SHESESQIQG RQPPQEHESN GSQWRTRTPF PRYSRKFSHI HAAEAGMIPV NQFFVPSYLR
ASRYVAKLEA AHKAKLKRER EHPPNPTSGA NSLSTSAGHS NAQRLAPSHR GMTYDIIESN
PPRDDLALMP LPSRWSEQDK YPGLDAMNEG LELKYTGSGS KAEIEAASVR ADYPMPSACG
IYYFEVEIKH KSKDTAIAIG FSTAEASLER LPGWETHSWG YHGDDGKMFC GEHSGRHYGP
TFDAGDVIGC GVNFNAGHAF FTKNGQDLGV CFKELKKDLR LFPTVGMKKH TGALVAVNFG
QRPFVFDIDD KMESERDKVA KDIDNAKPLS LTERRNETTL VQDLVMQFLS HDGYVETARA
FAEEVQRQRE SLSNTVSTPP AAPPVDDTEA LNRQKIRRAI LFGDIDRALE ATQAHFPSVL
AQNPNIVFKM KCRKWIELIR KTTELNARKN SAQFGASAAT DDDFAQDMDL DDQPNGGSQS
NGLGKAVASE TVLLRDQYLM EAMAYGQELS REYGGQEDHA QTLNETFSLL AYDDPTVSVN
GHLLDPSVFL GRPPAAYIER IWRQTDALLD TLVDNEGGAA AFVNVRAAFE T
//
