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Database: UniProt
Entry: A0A094CQI9_9PEZI
LinkDB: A0A094CQI9_9PEZI
Original site: A0A094CQI9_9PEZI 
ID   A0A094CQI9_9PEZI        Unreviewed;       720 AA.
AC   A0A094CQI9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=V496_06708 {ECO:0000313|EMBL:KFY56406.1};
OS   Pseudogymnoascus sp. VKM F-4515 (FW-2607).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420909 {ECO:0000313|EMBL:KFY56406.1, ECO:0000313|Proteomes:UP000029302};
RN   [1] {ECO:0000313|EMBL:KFY56406.1, ECO:0000313|Proteomes:UP000029302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4515 (FW-2607) {ECO:0000313|Proteomes:UP000029302};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFY56406.1}.
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DR   EMBL; JPJY01001259; KFY56406.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094CQI9; -.
DR   STRING; 1420909.A0A094CQI9; -.
DR   HOGENOM; CLU_015910_1_0_1; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000029302; 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:UP000029302};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          627..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   720 AA;  80897 MW;  42320A3D60A8BB75 CRC64;
     MATTNRDVRN HYLFEIATEV ANRVGGIYSV IKSKAPVTTA EYGDRYTLIG PLNRQSAAVE
     VEALTPTNPA LAATIAAMEE RGISIVYGRW LIEGAPRVLL IDTKTAYKFL DEWKADLWNT
     ASIPSPPGDD ETNEAVVFGY LVAWFLGEFV AHEKEKAVIA HFHEWLSGVA LPLCKKRRID
     VTTIFTTHAT LLGRYLCAGS VDFYNNLQYF DVDAEAGKRG IYHRYCIERA ATHSCDVFTT
     VSHITAYESE HLLKRKPDGV LPNGLNVTKF SAMHEFQNLH QQSKEKIHDF VRGHFYGHND
     FDPDNTLYFF TAGRYEYRNK GCDMFIESLA RLNHRLKASG SKMTVVAFII MPAQTQSLTV
     EALKGQAVIK SLRDTVDVIE RGVGKRIFER ALKWHDGDPM PDSKDLITSQ DRILLRRRLF
     AMKRHGLPPI VTHNMANDAE DPILNQIRRV QLFNHPSDRV KIVFHPEFLN SANPVLPLDY
     DDFVRGTHLG VFPSYYEPWG YTPAECTVMG VPSITTNLSG FGCYMEELIE NSTDYGIYIV
     DRRTKGVDDS VNQLTHFMAE FAGKSRRQRI NQRNRTERLS DLLDWKRMGM EYVKARQLAL
     RRAYPASFEG EEGDVFAGSD VKISRPFSVP GSPRDRSGLM TPGDFGSLQE GREGLSTEDY
     IAWKLPEEED PDEYPFPLTL RTRRPSGTSL DPMSGGPTSP AEPGKAAAAA AANGDGKAKV
//
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