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Database: UniProt/TrEMBL
Entry: A0A1D9QFH6_SCLS1 A7ER65_SCLS1
LinkDB: A0A1D9QFH6_SCLS1 A7ER65_SCLS1
Original site: A0A1D9QFH6_SCLS1 A7ER65_SCLS1 
ID   A0A1D9QFH6_SCLS1        Unreviewed;       711 AA.
AC   A0A1D9QFH6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   30-AUG-2017, entry version 4.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=sscle_11g083120 {ECO:0000313|EMBL:APA13542.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White
OS   mold) (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:APA13542.1, ECO:0000313|Proteomes:UP000177798};
RN   [1] {ECO:0000313|Proteomes:UP000177798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000177798};
RX   PubMed=28204478; DOI=10.1093/gbe/evx030;
RA   Derbyshire M., Denton-Giles M., Hegedus D., Seifbarghy S., Rollins J.,
RA   van Kan J., Seidl M.F., Faino L., Mbengue M., Navaud O., Raffaele S.,
RA   Hammond-Kosack K., Heard S., Oliver R.;
RT   "The complete genome sequence of the phytopathogenic fungus
RT   Sclerotinia sclerotiorum reveals insights into the genome architecture
RT   of broad host range pathogens.";
RL   Genome Biol. Evol. 0:0-0(2017).
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: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC       {ECO:0000256|RuleBase:RU363104}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|RuleBase:RU363104}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|RuleBase:RU363104}.
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DR   EMBL; CP017824; APA13542.1; -; Genomic_DNA.
DR   RefSeq; XP_001591193.1; XM_001591143.1.
DR   GeneID; 5487315; -.
DR   KEGG; ssl:SS1G_07818; -.
DR   KO; K00693; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000177798; Chromosome 11.
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; GT1_Glycogen_synthase_GSY2_lik; 1.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176; PTHR10176; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000177798};
KW   Glycogen biosynthesis {ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW   Transferase {ECO:0000256|RuleBase:RU363104}.
SQ   SEQUENCE   711 AA;  80793 MW;  569D9456B3FB2E8B CRC64;
     MSGKTNRDVK NHFLFEIATE VANRVGGIYS VIKSKAPVTT AEYGDRYTLI GPLNRQSAAV
     EVEALTPTNP HLAATIEAME ERGIQMLYGR WLIEGAPRVL LIDTKSAYRF LDEWKADLWN
     TAGIPSPPGD DETNEAVVFG YLVAWFLGEF VAHEKEKAVI AHFHEWLSGV ALPLCKKRRI
     DVTTIFTTHA TLLGRYLCAG SVDFYNNLQW FDVDAEAGKR GIYHRYCIER AATHSCDVFT
     TVSHITAYES EHLLKRKPDG VLPNGLNVTK FSAMHEFQNL HQQAKEKIHD FVRGHFYGHN
     DFDPENTLYF FTAGRYEYRN KGVDMFIESL ARLNHRLKSA GSKMTVVAFI IMPAQTQSLT
     VEALKGQAVI KSLRDTVDVI ERGVGKRIFE RALKWHEGEV MPDDKDLITS QDRILLRRRL
     FAMKRHGLPP IVTHNMANDS EDPILNQIRR VQLFNHPSDR VKVVFHPEFL NSANPVLPMD
     YDEFVRGTHL GVFSSYYEPW GYTPAECTVM GVPSITTNLS GFGCYMEELI ENSTDYGIYI
     VDRRMKGVDD SVNQLTSYMF DFAGKSRRQR INQRNRTERL SDLLDWKRMG MEYVKARQLA
     LRRAYPASFD GEEEDDFIPG VEQKISRPFS VPGSPRDRSG MMTPGDFASL QEGREGLSTE
     DYVAWKLPEE EDPDEYPFPL TLRTKKNGAQ SPYGGAQSPS EYAITNGNGL R
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (2)   
   InterPro (1)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (11)   

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ID   A7ER65_SCLS1            Unreviewed;       711 AA.
AC   A7ER65;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   22-NOV-2017, entry version 39.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=SS1G_07818 {ECO:0000313|EMBL:EDN91957.1};
OS   Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White
OS   mold) (Whetzelinia sclerotiorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN91957.1, ECO:0000313|Proteomes:UP000001312};
RN   [1] {ECO:0000313|Proteomes:UP000001312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P.,
RA   Couloux A., Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S.,
RA   Fournier E., Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M.,
RA   Pradier J.-M., Quevillon E., Sharon A., Simon A., ten Have A.,
RA   Tudzynski B., Tudzynski P., Wincker P., Andrew M., Anthouard V.,
RA   Beever R.E., Beffa R., Benoit I., Bouzid O., Brault B., Chen Z.,
RA   Choquer M., Collemare J., Cotton P., Danchin E.G., Da Silva C.,
RA   Gautier A., Giraud C., Giraud T., Gonzalez C., Grossetete S.,
RA   Gueldener U., Henrissat B., Howlett B.J., Kodira C., Kretschmer M.,
RA   Lappartient A., Leroch M., Levis C., Mauceli E., Neuveglise C.,
RA   Oeser B., Pearson M., Poulain J., Poussereau N., Quesneville H.,
RA   Rascle C., Schumacher J., Segurens B., Sexton A., Silva E., Sirven C.,
RA   Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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: UDP-alpha-D-glucose + ((1->4)-alpha-D-
CC       glucosyl)(n) = UDP + ((1->4)-alpha-D-glucosyl)(n+1).
CC       {ECO:0000256|RuleBase:RU363104}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC       {ECO:0000256|RuleBase:RU363104}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
CC       {ECO:0000256|RuleBase:RU363104}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CH476630; EDN91957.1; -; Genomic_DNA.
DR   RefSeq; XP_001591193.1; XM_001591143.1.
DR   EnsemblFungi; APA13542; APA13542; sscle_11g083120.
DR   GeneID; 5487315; -.
DR   KEGG; ssl:SS1G_07818; -.
DR   EuPathDB; FungiDB:SS1G_07818; -.
DR   InParanoid; A7ER65; -.
DR   KO; K00693; -.
DR   OMA; KVYFGRW; -.
DR   OrthoDB; EOG092C0XGC; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000001312; 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; GT1_Glycogen_synthase_GSY2_lik; 1.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176; PTHR10176; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001312};
KW   Glycogen biosynthesis {ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW   Transferase {ECO:0000256|RuleBase:RU363104}.
SQ   SEQUENCE   711 AA;  80793 MW;  569D9456B3FB2E8B CRC64;
     MSGKTNRDVK NHFLFEIATE VANRVGGIYS VIKSKAPVTT AEYGDRYTLI GPLNRQSAAV
     EVEALTPTNP HLAATIEAME ERGIQMLYGR WLIEGAPRVL LIDTKSAYRF LDEWKADLWN
     TAGIPSPPGD DETNEAVVFG YLVAWFLGEF VAHEKEKAVI AHFHEWLSGV ALPLCKKRRI
     DVTTIFTTHA TLLGRYLCAG SVDFYNNLQW FDVDAEAGKR GIYHRYCIER AATHSCDVFT
     TVSHITAYES EHLLKRKPDG VLPNGLNVTK FSAMHEFQNL HQQAKEKIHD FVRGHFYGHN
     DFDPENTLYF FTAGRYEYRN KGVDMFIESL ARLNHRLKSA GSKMTVVAFI IMPAQTQSLT
     VEALKGQAVI KSLRDTVDVI ERGVGKRIFE RALKWHEGEV MPDDKDLITS QDRILLRRRL
     FAMKRHGLPP IVTHNMANDS EDPILNQIRR VQLFNHPSDR VKVVFHPEFL NSANPVLPMD
     YDEFVRGTHL GVFSSYYEPW GYTPAECTVM GVPSITTNLS GFGCYMEELI ENSTDYGIYI
     VDRRMKGVDD SVNQLTSYMF DFAGKSRRQR INQRNRTERL SDLLDWKRMG MEYVKARQLA
     LRRAYPASFD GEEEDDFIPG VEQKISRPFS VPGSPRDRSG MMTPGDFASL QEGREGLSTE
     DYVAWKLPEE EDPDEYPFPL TLRTKKNGAQ SPYGGAQSPS EYAITNGNGL R
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (2)   
   InterPro (1)   
   Pfam (1)   
Literature (1)   
   PubMed (1)   
All databases (11)   

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