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Database: UniProt
Entry: G0WGG8_NAUDC
LinkDB: G0WGG8_NAUDC
Original site: G0WGG8_NAUDC 
ID   G0WGG8_NAUDC            Unreviewed;      1032 AA.
AC   G0WGG8;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=CTLH domain-containing protein {ECO:0000259|PROSITE:PS50897};
GN   Name=NDAI0I03110 {ECO:0000313|EMBL:CCD26879.1};
GN   OrderedLocusNames=NDAI_0I03110 {ECO:0000313|EMBL:CCD26879.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26879.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD26879.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR   EMBL; HE580275; CCD26879.1; -; Genomic_DNA.
DR   RefSeq; XP_003672122.1; XM_003672074.1.
DR   AlphaFoldDB; G0WGG8; -.
DR   STRING; 1071378.G0WGG8; -.
DR   GeneID; 11493969; -.
DR   KEGG; ndi:NDAI_0I03110; -.
DR   eggNOG; KOG1477; Eukaryota.
DR   HOGENOM; CLU_308189_0_0_1; -.
DR   OMA; RHNERQI; -.
DR   OrthoDB; 38145at2759; -.
DR   Proteomes; UP000000689; Chromosome 9.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:UniProt.
DR   CDD; cd12885; SPRY_RanBP_like; 1.
DR   Gene3D; 2.60.120.920; -; 1.
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; IPR044736; Vid30/RanBPM/SPLA_SPRY.
DR   PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1.
DR   PANTHER; PTHR12864:SF84; RAN-BINDING PROTEINS 9_10 HOMOLOG; 1.
DR   Pfam; PF10607; CTLH; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN          845..892
FT                   /note="CTLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50897"
FT   REGION          182..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..248
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..274
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..555
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..713
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        714..731
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1032 AA;  117063 MW;  52C11114B9B2AB13 CRC64;
     MSSNYMEEID KTFVKQLFPE YLLHQPVSQE LWYLYIKNKK LFNRINEQNK DPNSVASGTS
     NTKQKYIWNL ADENADDNDD TTRINTSNAL TSSLSSSLSA RTDNVILPFN VKKEIWHRLM
     ELGVLGTISF ESANDNYLIQ VYKYFYPKQM DLIPTIYSRN SMNANANANG FSLKNGNSFN
     MATEKNGNMR KPFPYNSDND NDNDNDLWNE SSRPESSRSV SLSAVNDNVS NDNVESTTIQ
     QSVTNSNNDS HKENDDDNDE MDIDDEDEED GDADEEIIGS ETESVISRKT NTSPIYHDFQ
     KERTPQNILR KQYENKFKFK SNHVTSDIYN IIGYFLPSHW APPAASGVTV SRDGVMRLQS
     VTLSESSASS TAGLSLAATH EVYPAPSSTS AAAIRNRLNS SHPTSSTATI TGKSNKNQSN
     YTMVKANTFI PTNKMSIFYY EIRVLSVTSS QNAQNCNILL GYNFDFSENH NANVFSINDS
     QQQFGRPTSA GHVMDTSFNM TTTNNLFARN RHNIHNESDD NNNNGNEDYE NNDDIEGDDD
     DDDNDDEDDG GEDEEHEGGD PSRGQSWRRT CGSKKASKEG LDFGFFGLSG QNGSIYFGQK
     FEPYSIPFCR DDIIGCGINY IDSTIFFTKN GVHLGTAFRN LPDLNFIPSV ALKPGNSVRT
     NFGLYEEFAF DISGYQDKWK NKSLQHILQP FNQKNTEMED VEEDEDEAKA EEPDEEENNK
     TKDIENGIEN NEHRKKSLST FLLGPDTRYN KDGRLTKPTD TAINHLNDTE NGDLIVDTLN
     VMINDYLIHE GMIDVAKAFL KDLQDDSVVK DSDGGNDNIV DCETLEIQRE IIRHNERQIL
     KEEKVVQIRQ EIRRLVYNGD IKGCVTWINS ELPNLLQSNI ELSFELKIAE YLISFISNAP
     GMNIEETIKN GQLLTQEFVY NENIPGALRE NFKRHLDNIS LLLAYDDPVN EVTGDLSMYL
     SKEYLQDRLF QVINSNVLQF LKKKSSCSLE DIMGYTRTML STMRNYRIDT SGSNGNCRYY
     RAVNIDEDFL NI
//
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