UniProt: A0A0J1B3Z1

Database: UniProt
Entry: A0A0J1B3Z1_9TREE

LinkDB:  A0A0J1B3Z1_9TREE 
Original site:  A0A0J1B3Z1_9TREE

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (2)   
   InterPro (1)   
   Pfam (1)   
All databases (8)   

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ID   A0A0J1B3Z1_9TREE        Unreviewed;       669 AA.
AC   A0A0J1B3Z1;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=CC85DRAFT_260436 {ECO:0000313|EMBL:KLT42364.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT42364.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT42364.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT42364.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) 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}.
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DR   EMBL; KQ087206; KLT42364.1; -; Genomic_DNA.
DR   RefSeq; XP_018278855.1; XM_018420833.1.
DR   AlphaFoldDB; A0A0J1B3Z1; -.
DR   STRING; 879819.A0A0J1B3Z1; -.
DR   GeneID; 28981436; -.
DR   OrthoDB; 9432at2759; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000053611; 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   Gene3D; 6.10.260.10; -; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
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:UP000053611};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU363104}.
FT   REGION          543..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          612..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   669 AA;  75787 MW;  746E8EAE522B194F CRC64;
     MEGTLNAMRD HGVKYIYGRW LIEGAPRVLL FDTGSCYNRM DEWKGDLWNV AGIPTPPNDH
     ETNETLVFGY MVAWFLGEFS GRCLDTAIIA HFHEWQAGLA IPLARKRKID VTTIFTTHAT
     LLGRYLCAGS VDFYNNLQYF DVDHEAGKRG IYHRYCIERS AAHCADVFTT VSHITAYESE
     HLLKRKPDGV LPNGLNVVKF AAMHEFQNLH VKAKEKINDF IRGHFYGHYD FDLDNTIYMF
     TAGRYEFRNK GVDMFIESLA RLNHRLKAMN SKMTVVAFII MPAATNSYTI EALKGQAVTG
     QLRDVVKQIT DRIGNRLFEH AARYDGTHGT EVPKPEELMS AEDLVLLKRR VFALKRNSLP
     PVVTHNMQDD SNDPILNQIR RVQLFNRTSD RVKVIFHPEF LNSNNPILGL DYEEFVRGCH
     LGVFPSYYEP FGYTPAECTV MGIPSVTTNL SGFGCFMEDL LESPEDYGCY IVDRRGQGVD
     ESVEQLTQVL TEFTTKSRRQ RINQRNRTER LSELLDWKSL GLEYAKARQL ALRRAYPDSF
     NDDEPEFTGV QRVGAPLSAP GSPRYRSGMM TPGDYATLTE EMEHLNTSDY MGAKHPWNWN
     KEDSDEEEGY TFPIAGLKPR GRSDSLASAI SGTMTPSGKH RLNESDLAQA DKALESHSSA
     ANANGNGNK
//

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