ID   E3RZL0_PYRTT            Unreviewed;       705 AA.
AC   E3RZL0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=PTT_15101 {ECO:0000313|EMBL:EFQ88821.1};
OS   Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS   (Drechslera teres f. teres).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN   [1] {ECO:0000313|EMBL:EFQ88821.1, ECO:0000313|Proteomes:UP000001067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0-1 {ECO:0000313|EMBL:EFQ88821.1,
RC   ECO:0000313|Proteomes:UP000001067};
RX   PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA   Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA   Oliver R.P., Friesen T.L.;
RT   "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT   teres.";
RL   Genome Biol. 11:R109.1-R109.14(2010).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan. {ECO:0000256|RuleBase:RU363104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-
CC         alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:18549, Rhea:RHEA-
CC         COMP:9584, Rhea:RHEA-COMP:9587, ChEBI:CHEBI:15378, ChEBI:CHEBI:15444,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00043769};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18550;
CC         Evidence={ECO:0000256|ARBA:ARBA00043769};
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004964, ECO:0000256|RuleBase:RU363104}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010686, ECO:0000256|RuleBase:RU363104}.
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DR   EMBL; GL536097; EFQ88821.1; -; Genomic_DNA.
DR   RefSeq; XP_003303065.1; XM_003303017.1.
DR   AlphaFoldDB; E3RZL0; -.
DR   STRING; 861557.E3RZL0; -.
DR   EnsemblFungi; EFQ88821; EFQ88821; PTT_15101.
DR   KEGG; pte:PTT_15101; -.
DR   eggNOG; KOG3742; Eukaryota.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001067; Unassembled WGS sequence.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03793; GT3_GSY2-like; 1.
DR   Gene3D; 6.10.260.10; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176:SF3; GLYCOGEN [STARCH] SYNTHASE; 1.
DR   PANTHER; PTHR10176; GLYCOGEN SYNTHASE; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 2.
PE   3: Inferred from homology;
KW   Glycogen biosynthesis {ECO:0000256|ARBA:ARBA00023056,
KW   ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          612..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   705 AA;  79839 MW;  6A4CBB738A3E4383 CRC64;
     MAETGARDVQ NHCLFEVATE VANRVGGIYS VLKSKAQVTT AEYGAAYTLL GPWNRASAAV
     EVEPIEPKDP ALVATIKSMD DRGIKTLYGR WLIDGAPRVL LFDTGTGYRW LDEWKGDLWS
     STGIPSPPGD SETNEAIVFG YLIAWFLGEY VYHEKKRAVI VQFHEWLAGV AVPLCKKRRI
     DVTTIFTTHA TLLGRYLCAG SVDFYNNLQY FDVDAEAGKR GIYHRYCIER AATHAADVFT
     TVSHITAYES EHLLKRKPDG VLPNGLNVKK FSATHEFQNL HQQAKVKIND FVRGHFYGHN
     DFDPENTLYF FTAGRYEYRN KGVDMFIESL ARLNHKMKNE NSNMTVVAFI ILPAQTTSLS
     VDSLKGQAVI KALHDSVNNI AENVAKKLFE RSLTWTEGSE LPEDKDLITP ADKILLRRRL
     FAMKRHNLPP IVTHNMVNDA EDPVLNQLRR CQLFNHPSDR VKVVFHPEFL NSANPVLPMD
     YDDFVRGTHL GVFSSYYEPW GYTPAECTVM GVPSITTNLS GFGCYMEELI ENAQDYGIYI
     VDRRMKGVDD SVNQLVDYMY DFTKKSKRQR INQRNRTERL SDLLDWKRMG LEYVKARQLA
     LRRAYPAAYE DDDEPDFFSS QDVKISRPLS EPGSPRDRSG MMTPGDFASL QEGREGLSTE
     DYIAWKLPEE EEADDFTFPL TLKTKSKPNS GANTPTLPAA VNGTD
//