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Database: UniProt/TrEMBL
Entry: F9XHH4_ZYMTI
LinkDB: F9XHH4_ZYMTI
Original site: F9XHH4_ZYMTI 
ID   F9XHH4_ZYMTI            Unreviewed;       722 AA.
AC   F9XHH4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   30-AUG-2017, entry version 24.
DE   RecName: Full=Glycogen [starch] synthase {ECO:0000256|RuleBase:RU363104};
DE            EC=2.4.1.11 {ECO:0000256|RuleBase:RU363104};
GN   ORFNames=MYCGRDRAFT_74660 {ECO:0000313|EMBL:EGP84982.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf
OS   blotch fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP84982.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP84982.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J.,
RA   Crane C.F., Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J.,
RA   Aerts A., Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J.,
RA   van der Burgt A., Canto-Canche B., Churchill A.C.L., Conde-Ferraez L.,
RA   Cools H.J., Coutinho P.M., Csukai M., Dehal P., De Wit P.,
RA   Donzelli B., van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E.,
RA   Henrissat B., Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y.,
RA   Kuzniar A., Lindquist E., Lombard V., Maliepaard C., Martins N.,
RA   Mehrabi R., Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A.,
RA   Schmutz J., Schouten H.J., Shapiro H., Stergiopoulos I.,
RA   Torriani S.F.F., Tu H., de Vries R.P., Waalwijk C., Ware S.B.,
RA   Wiebenga A., Zwiers L.-H., Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella
RT   graminicola reveals dispensome structure, chromosome plasticity, and
RT   stealth pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(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}.
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DR   EMBL; CM001203; EGP84982.1; -; Genomic_DNA.
DR   RefSeq; XP_003850006.1; XM_003849958.1.
DR   EnsemblFungi; Mycgr3T74660; Mycgr3P74660; Mycgr3G74660.
DR   GeneID; 13402800; -.
DR   KEGG; ztr:MYCGRDRAFT_74660; -.
DR   InParanoid; F9XHH4; -.
DR   KO; K00693; -.
DR   OrthoDB; EOG092C0XGC; -.
DR   UniPathway; UPA00164; -.
DR   Proteomes; UP000008062; Chromosome 8.
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:UP000008062};
KW   Glycogen biosynthesis {ECO:0000256|RuleBase:RU363104};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU363104};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062};
KW   Transferase {ECO:0000256|RuleBase:RU363104}.
SQ   SEQUENCE   722 AA;  81660 MW;  07E0F756447BE7BD CRC64;
     MGEPQHRDVR NHVLFEIATE VANRVGGIYS VLKSKAQVTT AEYGSMYTLL GPLNRASAAV
     EVEEIEPRDP AMINTIKSMN DRGIKTLYGR WLIDGAPRVL LFDTSTGYYK LDEWKGDLWS
     TAGIPSPPDD HETNEAIVFG YLIAWFLGEY VYHEKERAVI AQFHEWLAGV ALPLCKKRKI
     DVTTIFTTHA TLLGRYLCAG SVDFYNNLQY FDVDAEAGKR GIYHRYCIER GAAHSADVFT
     TVSHITAYES EHLLKRKPDG VLPNGLNVKK FSATHEFQNL HQVNKERITE FIRGHFYGHN
     DFDPDKTLYL FTAGRYEYRN KGVDMFIESL ARLNHRMKSA GSDMTVVAFI IMPAQTTSLA
     VEALKGQAVI KSLRDSVDHI EKSVGKKLFE KALAWHEGAE VPDEKDLITA QDKIMLRRRL
     FAMKRNTLPP IVTHNLVNDA EDPILNQIRR CQLFNHPSDR VKVIFHPEFL SSGNPVLPMD
     YDDFVRGTHM GVFSSYYEPW GYTPAECTVM GVPSITTNLS GFGCYMEELI ENAQDYGIYI
     VDRRMKGVDD SVNQLAEFMY QFTQKSKRQR INQRNRTERL SDLLDWKRMG MEYVKARQLA
     LRRAYPDSFD SATDDEPGFF DGTESMKISR PLSAPGSPRE RSGMMTPGDF ASLQEGREGL
     STEDYIAWKL PEEEEPEDYP FPLTLKTKKG DGSGATTPTM TNGNGNVALP DRGVLASAST
     IQ
//
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