ID Q0UZR7_PHANO Unreviewed; 832 AA.
AC Q0UZR7;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 24-JAN-2024, entry version 86.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EAT89478.2};
GN ORFNames=SNOG_02747 {ECO:0000313|EMBL:EAT89478.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT89478.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000256|ARBA:ARBA00006330}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
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DR EMBL; CH445328; EAT89478.2; -; Genomic_DNA.
DR RefSeq; XP_001793344.1; XM_001793292.1.
DR AlphaFoldDB; Q0UZR7; -.
DR STRING; 321614.Q0UZR7; -.
DR EnsemblFungi; SNOT_02747; SNOT_02747; SNOG_02747.
DR GeneID; 5970201; -.
DR KEGG; pno:SNOG_02747; -.
DR VEuPathDB; FungiDB:JI435_027470; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_0_1; -.
DR InParanoid; Q0UZR7; -.
DR OrthoDB; 1023at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IBA:GO_Central.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:EnsemblFungi.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR NCBIfam; TIGR00685; T6PP; 1.
DR PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR PANTHER; PTHR10788:SF123; TREHALOSE-PHOSPHATASE; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001055}.
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 832 AA; 93438 MW; F5344C48A2683C8E CRC64;
MTPPTEPDPA SPEAFEPRES DHPALHPSIT NVPVTPGVHL TGQSAYIDPE DTDSTSKLPF
DPEKATPGPS WSANSYFADK QQVQDKAGST FEAGTAQTEK DTQQKMEPRP DESTENDLSS
VDPRAAHPGL NLSGRIISAT FAVPYNIGFS KGNDWELEPR RGTSALFDSF SYLASSSSPW
NHTLVGWTGE ISTAKSAGDL AVQPPVNKAA APIPVDPKKP NPVPQQPTGL RIGRDDRVRL
EKQLERDHGG KIVPVWLVDE VDDHKDEYVV KDQSRWRTFA EHELYTLFHY KQNEPEDGRA
ARKSWADYYR MNKLFADRIL EIYNPGDIIM VHDFYLLLLP SLLRQRLPNI YIGFFLHVPF
PSSEFYRCLS RRKEILEGVL GANMIGFQSY SYSRHFSSCC TRILGFDSSS AGVDAYGAHV
AVDVFPIGIN AASTQRQAFG DPEIDDRIKG IREMYAGKKI IVGRDRLDAV RGVVQKLQAF
EMFLEKYPEW QGKVVLIQVT SPSSVHTDRG ESARERIVNN ISDLAAKING VHGSLDFTPV
RHFPQYLSRE EYFALLRLAD IGLITSVRDG MNTTSMEYVI CQKDNHGPLI LSEFSGTAGS
LSGAIHINPW DLGGVADAIN EALKLDDQQR EQQHTKLYNH VVSNNVQSWT NNYLKRLMTN
LSAFDQSFAT PALDRAKLLS QYRQAKKRLF MFDYDGTLTP IVKDPQAAIP SDRVIRTLKT
LASDPNNAVW IISGRDQAFL DEWMGHISEL GLSAEHGSFM RHPKSQDWEN LTETTDMSWR
KEVIDVFQYY TDKTTGEFLR RDKEDCFDMA LSEELNPEYG ATSRLAKCPE AS
//