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Database: UniProt
Entry: A0A453D0K5_AEGTS
LinkDB: A0A453D0K5_AEGTS
Original site: A0A453D0K5_AEGTS 
ID   A0A453D0K5_AEGTS        Unreviewed;      1231 AA.
AC   A0A453D0K5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=starch synthase {ECO:0000256|ARBA:ARBA00012588};
DE            EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET2Gv21035000.12, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET2Gv21035000.12}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004727}.
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC       {ECO:0000256|ARBA:ARBA00004602}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC       Bacterial/plant glycogen synthase subfamily.
CC       {ECO:0000256|ARBA:ARBA00010281}.
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DR   AlphaFoldDB; A0A453D0K5; -.
DR   EnsemblPlants; AET2Gv21035000.12; AET2Gv21035000.12; AET2Gv21035000.
DR   Gramene; AET2Gv21035000.12; AET2Gv21035000.12; AET2Gv21035000.
DR   UniPathway; UPA00152; -.
DR   Proteomes; UP000015105; Chromosome 2D.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro.
DR   GO; GO:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 3.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   HAMAP; MF_00484; Glycogen_synth; 1.
DR   InterPro; IPR005085; CBM25.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR011835; GS/SS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013534; Starch_synth_cat_dom.
DR   PANTHER; PTHR46083; -; 1.
DR   PANTHER; PTHR46083:SF7; OS04G0624600 PROTEIN; 1.
DR   Pfam; PF16760; CBM53; 3.
DR   Pfam; PF08323; Glyco_transf_5; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
DR   SMART; SM01066; CBM_25; 3.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Amyloplast {ECO:0000256|ARBA:ARBA00023234};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Plastid {ECO:0000256|ARBA:ARBA00023234};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW   Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          348..433
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   DOMAIN          523..614
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   DOMAIN          685..774
FT                   /note="Carbohydrate binding module family 25"
FT                   /evidence="ECO:0000259|SMART:SM01066"
FT   REGION          1..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          624..654
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        52..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1231 AA;  139038 MW;  DBD3BD620716E897 CRC64;
     TLHYSDYPKR NPRRSSAPKP KGTASRGYAP RPSAESWTST KKTEHSSADE DGDLGTSNGT
     LSSEATEQTS SAEEEYEVEF SGNVSSSMEL KGVNEVETEE EADQKQPPAL ASTSMDVDSV
     NEATEQTSTA DESSEVDFSG NVSSSLELEV VDESETEEEA DQKQSSALAS TSMDSESIDR
     ELEEYRVRIS ALVGASTQGQ DQSIISVHEQ DKSVITSDGQ DISAVDVPEQ SQSVVGVTRK
     DPMEQTTSEQ DIAEAAVEEI ASKNLVARKH SSSEDGVGAS KDANEEPLVA GDELRVTEDE
     EQHEPEMQEQ VQMDVDPQAL KRRLEELADK NYSIGNKCFV FPELVEADSV IDLYLNRSMS
     ALASEPDILI KGAFNGWRWN HFTEKLHRSE LTGDWWCCKL YIPKQAYRLD FVFFNGDTVY
     ENNSYNDFVL HIESDIDEYS FEDFLLEEKQ RELERLAAEE AERERQAEEE RRKEEERAAM
     EADRAQSKAE VEMMRNKLQH VLGLASRYAD NLWYIEPSTY KGGDRVRLYY NRSSRPLNHK
     NEIWLHGGYN NWTDGPSIVE RLVKSEEKDG DWWYANVTLP ESALVLDWVF ADGSPGNANK
     YDNNGKRDFH AAVSKSISDD LFWVEEERRI FERLQRERKE KEDAGRRKAE ITARMKAEMK
     EKTMREFLLS QKHIVYTEPL EVRAGTTVDV LYNPSNTVLN GSPEVWFRCS FNRWTHPSGP
     LPPQKMVNEV NGSHLQATVR VPLDAYMMDF VFSESEEGGI YDNRDGMDYH IPVSDSTAKE
     PPMHIVHIAV EMAPIAKVGG LGDVVTSLSR AIQDLGHKVE VIFPKYDCLN LSNVKDLHCR
     QSFTWGGTEI KVWFGKVEGI SVYFLEPQNG MFWVGCVYGK NDESRFGFFC HSALEFLLQS
     GSSPDIIHCH DWSSAPVAWL YKQQYVHNGL PNGRVVFTIH NLEFGVHHIG KAMAHCDKAT
     TVSYTYSKEV SGHGSIAPHY FKFHGIRNGI DSDIWDPYND NFIPVHYTSE NVVEGKSSAK
     RALQEKLGLH QTDSPLVGII SRLTAQKGIH LIKHAIYRTL ERNGQVVLLG SAPDHRIQGD
     FSNLAAKLHG EFDGRVKLCL TYDEPLSHLI YAGADFILVP SIFEPCGLTQ LTAMRYGSIP
     IVRKTGGLYD TVFDVDDDKD RAHEQGLEPN GFSFEGADSN GVDYALDRAI TTWYDARDWF
     DSLCKRVMEQ DWSWNRPALD YMELYHSARK N
//
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