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Database: UniProt
Entry: A0A2H3IEY8_9EURO
LinkDB: A0A2H3IEY8_9EURO
Original site: A0A2H3IEY8_9EURO 
ID   A0A2H3IEY8_9EURO        Unreviewed;       474 AA.
AC   A0A2H3IEY8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   SubName: Full=SGS {ECO:0000313|EMBL:PCG94318.1};
GN   ORFNames=PENO1_079040 {ECO:0000313|EMBL:PCG94318.1};
OS   Penicillium occitanis (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG94318.1, ECO:0000313|Proteomes:UP000218381};
RN   [1] {ECO:0000313|EMBL:PCG94318.1, ECO:0000313|Proteomes:UP000218381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL100 {ECO:0000313|EMBL:PCG94318.1,
RC   ECO:0000313|Proteomes:UP000218381};
RX   PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA   Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA   Gabaldon T., Roncero M.I.G.;
RT   "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT   occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT   Fusarium oxysporum.";
RL   Front. Microbiol. 8:1627-1627(2017).
CC   -!- SIMILARITY: Belongs to the SGT1 family.
CC       {ECO:0000256|ARBA:ARBA00008509}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PCG94318.1}.
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DR   EMBL; NPFK01000283; PCG94318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3IEY8; -.
DR   STRING; 290292.A0A2H3IEY8; -.
DR   OrthoDB; 5479399at2759; -.
DR   Proteomes; UP000218381; Unassembled WGS sequence.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR   CDD; cd06466; p23_CS_SGT1_like; 1.
DR   Gene3D; 2.60.40.790; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR007052; CS_dom.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR007699; SGS_dom.
DR   InterPro; IPR044563; Sgt1-like.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR45862; PROTEIN SGT1 HOMOLOG; 1.
DR   PANTHER; PTHR45862:SF1; PROTEIN SGT1 HOMOLOG; 1.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF05002; SGS; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51203; CS; 1.
DR   PROSITE; PS51048; SGS; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000218381}.
FT   DOMAIN          235..326
FT                   /note="CS"
FT                   /evidence="ECO:0000259|PROSITE:PS51203"
FT   DOMAIN          364..474
FT                   /note="SGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51048"
FT   REGION          345..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..401
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   474 AA;  51401 MW;  21032C05BD975607 CRC64;
     MNEATQGDKA ASQSNWPLAI THYTNALIEN PRAPSYYIKR STAYSRRKAV DGGPDLTAAL
     GDVELALALA RERGKRELII EAQLRRAIVL FQFERFGDAG YLFDLLEDKL GIKDDSAAGD
     KSAQVQAAMS AQKGSQQKLE NELKIWRLKI KGKIGKLEAG DGKLAVSIKE HPDLKIPEEG
     ELRKRLKEQL SSSGAASVVD RTKESTLDVS GSTSAPFTAG LGAPTTTAPA PAATPAKIRH
     EWYQSQDAVV VTIYAKNVDK SKLETDLQDN SLSLEFPLPS GSTYSFNLDP FYAPIDTTQS
     KINVLSTKIE ITLRKRTPGQ KWGSLEGSAT APVVSDATIT VNSTATVPTT QTPAQINNNV
     GGPAYPTSSR HGVKNWDKLA DDLTAKKKRD EKKKKKKSED DDDAEDDDDD AASVDSDIGG
     DAVDSFFKKL YAGADPDTRR AMMKSFYESQ GTALSTNWDE VGKEKVAVVP PSED
//
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