ID   A0A178B475_9PLEO        Unreviewed;      1326 AA.
AC   A0A178B475;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=WD repeat-containing protein 26 {ECO:0000313|EMBL:OAL04363.1};
GN   ORFNames=IQ06DRAFT_213267 {ECO:0000313|EMBL:OAL04363.1};
OS   Stagonospora sp. SRC1lsM3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX   NCBI_TaxID=765868 {ECO:0000313|EMBL:OAL04363.1, ECO:0000313|Proteomes:UP000077206};
RN   [1] {ECO:0000313|EMBL:OAL04363.1, ECO:0000313|Proteomes:UP000077206}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAL04363.1,
RC   ECO:0000313|Proteomes:UP000077206};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441707; OAL04363.1; -; Genomic_DNA.
DR   STRING; 765868.A0A178B475; -.
DR   InParanoid; A0A178B475; -.
DR   OrthoDB; 5491841at2759; -.
DR   Proteomes; UP000077206; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR22838; WD REPEAT PROTEIN 26-RELATED; 1.
DR   PANTHER; PTHR22838:SF0; WD REPEAT-CONTAINING PROTEIN 26; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW   ProRule:PRU00221}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1326
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008082551"
FT   REPEAT          1018..1059
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REPEAT          1277..1310
FT                   /note="WD"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT   REGION          611..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..669
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        716..744
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..770
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1326 AA;  146531 MW;  1574CE61CDE77937 CRC64;
     MEQLLALFGF FLALSSVAAQ SNATATLSFS LPSGYSTRSF NATAQPTPFN RTDFSPNALA
     ALWDQIGPVA TGPVTTTVSP TPEPSSYAQP DGQYYHALIG SAYPETRDMK LPAGFQWGFS
     SSAYQIEGAA KDEGKGPSIW DLLSHRVPNF VSDNTTGDVV ASHYYLYKQD FARLKSLGVR
     AFSPSFSWPR FFPFGHGPVN EEAVKHYDDV ISEMHANGLH AAVTLFHWDT PLALFNEYGA
     WTDRRIVDHF FEYAKFVITR YDAYVDEWFT INEPQYCNWQ YAGYPAGKYY PAPNGITGGV
     EARFLCGHHS ILAHAKVAKW YHEEFKGRGV ITFKNSGNYY EANSTSEADE IARQRNFDFS
     IGWFGGPWTD GDYPASLKDT LGDLLPTLSQ EEKDMIKGSC DFYAIDPYSS FLAFEVSGGL
     DACTSNRSHP SFPDCAGSAS ISPGGFPIGP AADPQMSWFY SAPSGVRRFL KHITQVLFPS
     IPSIVVSEFG FAEPFESQWD SLNPILWDIR RSDYFQQYLD NILLAIHVDG VNVTGAWGWA
     IYDNFEWAIG TGVKFGLQYV NYTSLERVPK ASLRQFLGIV LYRKPFSGTA PDRPIPASTA
     GTWRHAEVLA NNNDIPTPPP IASADPSIPT SQASPSPPSS AHHTLPGPPT APTTTSQQLP
     TTTTALPSDL SAPGKRRHSL SESDHEPDPT GTSARSTRPR TKRRRRTHET MRLDNNDASK
     PPSSPSQTYT NGSSRSSGLR SPRAKTSNGD GHERTESNGS YTNGGPVANG DTVSPTFYGH
     DREEVTRILI QSLTDLGYHG AAGALSKESG FQLEGPTVAS FRNSVMNGDW TEAEALLFGT
     STYDGGGVGL DASYGKSWAK STSRTSHHTR GLTLAEGANR SEMLFWMKQQ KYLELLERRE
     LGKALAVLRQ ELTPLHQDVG RLHVLSSLMM CQSAEDLRIQ ANWDGAQGES RTMLLSELSK
     SISPSIMIPE HRLSVLLDEV KDNWVSNCQY HNTAASPSLY LDHNCERDDF PTKPVHELKS
     HRDEVWFVQY SNNGKYLASS SKDETICIYE TETYKVKYRF NEHQNSGVTH IAWSPDDTKI
     VTCCSQPENS ARIWDVKSGM CIAQISEFTY PCTTAAWAPS GKYVVIGSQD DKTGCGVWDA
     EGRIIHNFCD DGSKIRANDL AISPDGSRLV IVAETSVVVY DFESYEKICE WRTDEVKLTS
     VNISQDSRHM LISMNPDTIK LMEIDTSEVI KTFYGHSQKQ FIIRSSFGGA NENFIVSGSE
     DSRIHIWRSS GQHIENLEAH VGCVNSVAWH PTDPTVFASA GDDHRVRIWK PARLAAASGA
     SNGYGQ
//