ID R0F8G0_9BRAS Unreviewed; 1065 AA.
AC R0F8G0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=starch synthase {ECO:0000256|ARBA:ARBA00012588};
DE EC=2.4.1.21 {ECO:0000256|ARBA:ARBA00012588};
GN ORFNames=CARUB_v10006702mg {ECO:0000313|EMBL:EOA18217.1};
OS Capsella rubella.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Capsella.
OX NCBI_TaxID=81985 {ECO:0000313|EMBL:EOA18217.1, ECO:0000313|Proteomes:UP000029121};
RN [1] {ECO:0000313|Proteomes:UP000029121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Monte Gargano {ECO:0000313|Proteomes:UP000029121};
RX PubMed=23749190; DOI=10.1038/ng.2669;
RA Slotte T., Hazzouri K.M., Agren J.A., Koenig D., Maumus F., Guo Y.L.,
RA Steige K., Platts A.E., Escobar J.S., Newman L.K., Wang W., Mandakova T.,
RA Vello E., Smith L.M., Henz S.R., Steffen J., Takuno S., Brandvain Y.,
RA Coop G., Andolfatto P., Hu T.T., Blanchette M., Clark R.M., Quesneville H.,
RA Nordborg M., Gaut B.S., Lysak M.A., Jenkins J., Grimwood J., Chapman J.,
RA Prochnik S., Shu S., Rokhsar D., Schmutz J., Weigel D., Wright S.I.;
RT "The Capsella rubella genome and the genomic consequences of rapid mating
RT system evolution.";
RL Nat. Genet. 45:831-835(2013).
CC -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004727}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family.
CC Bacterial/plant glycogen synthase subfamily.
CC {ECO:0000256|ARBA:ARBA00010281}.
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DR EMBL; KB870811; EOA18217.1; -; Genomic_DNA.
DR RefSeq; XP_006285319.1; XM_006285257.1.
DR AlphaFoldDB; R0F8G0; -.
DR STRING; 81985.R0F8G0; -.
DR eggNOG; ENOG502R4VJ; Eukaryota.
DR UniPathway; UPA00152; -.
DR Proteomes; UP000029121; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004373; F:glycogen (starch) synthase activity; 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; 2.
DR HAMAP; MF_00484; Glycogen_synth; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR011835; GS/SS.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR NCBIfam; TIGR02095; glgA; 1.
DR PANTHER; PTHR46083; -; 1.
DR PANTHER; PTHR46083:SF2; STARCH SYNTHASE 4, CHLOROPLASTIC_AMYLOPLASTIC-RELATED; 1.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000029121};
KW Signal {ECO:0000256|SAM:SignalP};
KW Starch biosynthesis {ECO:0000256|ARBA:ARBA00022922};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1065
FT /note="starch synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004340337"
FT DOMAIN 569..808
FT /note="Starch synthase catalytic"
FT /evidence="ECO:0000259|Pfam:PF08323"
FT DOMAIN 864..1020
FT /note="Glycosyl transferase family 1"
FT /evidence="ECO:0000259|Pfam:PF00534"
FT REGION 45..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 185..326
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 351..458
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 103..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1065 AA; 120787 MW; E2500E8C6E6EA899 CRC64;
MTTKLSSFCF LTHGLAAGIS CEREHGTSRR FFYLPSSRRL VSTSCKMRQQ RGFDPSKRQE
IKKGSPEPIL SINSSLQRNS DEESEPENGS ADSVPSLKSD VEKGTVDINH VDENTEKRED
IQTIEVTRRK SRPAKKKEEN VNATTDDGQN LNSLTVPEVA KALSINKSGG EQISDGQFGE
LMTMIRNAEK NILRLDQARA SALDDLNKIL SEKEALQGEI NVLEMKLVET DERIKTAAQE
KVHVELLEEQ LEKLRHEMIS PPETDGYVLA LSKELETLKM ENLTLRNDIE MLKSELDSVK
NTGERVVVLE KECSGLESSV KDLESKLSVS QEDVSKLSTL KTECTDLWAK VENLQLLLDR
ATKQAEQAVI VLQQNRDLRN KVDKIEESLK EANVYKESSE KIQQYNELMQ HKVTLLEERL
EKSDAEIFSY VQLYQESIKE FQETLESLKE ESKKNSRDEP VDDMPWDYWS RLLLTVDGWL
LEKKIASNDA DSLREMVWKK DRRIHDTYID VKDKNERDAI SAFLNLVSSP TRLSSSSGKF
LCLFVGFQSF LKRNLFSSSY VDSSSGLYVV HIAAEMAPVA KVGGLGDVVA GLGKALQRRG
HLVEIILPKY DCMQYDRVRD LRALDTVVES YFDGKLYKNK IWIGTVEGLP VHFIEPQHPS
KFFWRGQFYG EQDDFRRFSY FSRAALELLL QSGKKPDIIH CHDWQTAFVA PLYWDLYAPK
GLDSARICFT CHNFEYQGTA SASELGSCGL DVNQLNRPDR MQDHSSGDRV NPVKGAIIFS
NIVTTVSPTY AQEVRTAEGG KGLHSTLNFH SKKFMGILNG IDTDSWNPAT DPFLKAQFNA
KDLQGKEENK YALRKQLGLS SAESRRPLVG CITRLVPQKG VHLIRHAIYR TLELGGQFVL
LGSSPVPHIQ REFEGIEQQF KSHDHVRLLL KYDEALSHTI YAASDLFIIP SIFEPCGLTQ
MIAMRYGSIP IARKTGGLND SVFDIDDDTI PTQFQNGFTF QTADEQAFNY ALERAFNHYK
KDGDKWMKLI EKVMSIDFSW GSSATQYEEL YSRSVARARS AANRM
//
