ID A0A368R6H2_SETIT Unreviewed; 1925 AA.
AC A0A368R6H2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00032165};
GN ORFNames=SETIT_5G189100v2 {ECO:0000313|EMBL:RCV25733.1};
OS Setaria italica (Foxtail millet) (Panicum italicum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Cenchrinae; Setaria.
OX NCBI_TaxID=4555 {ECO:0000313|EMBL:RCV25733.1};
RN [1] {ECO:0000313|EMBL:RCV25733.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV25733.1};
RX PubMed=22580951; DOI=10.1038/nbt.2196;
RA Bennetzen J.L., Schmutz J., Wang H., Percifield R., Hawkins J.,
RA Pontaroli A.C., Estep M., Feng L., Vaughn J.N., Grimwood J., Jenkins J.,
RA Barry K., Lindquist E., Hellsten U., Deshpande S., Wang X., Wu X.,
RA Mitros T., Triplett J., Yang X., Ye C.Y., Mauro-Herrera M., Wang L., Li P.,
RA Sharma M., Sharma R., Ronald P.C., Panaud O., Kellogg E.A., Brutnell T.P.,
RA Doust A.N., Tuskan G.A., Rokhsar D., Devos K.M.;
RT "Reference genome sequence of the model plant Setaria.";
RL Nat. Biotechnol. 30:555-561(2012).
RN [2] {ECO:0000313|EMBL:RCV25733.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yugu1 {ECO:0000313|EMBL:RCV25733.1};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR EMBL; CM003532; RCV25733.1; -; Genomic_DNA.
DR RefSeq; XP_004968876.1; XM_004968819.1.
DR STRING; 4555.A0A368R6H2; -.
DR GeneID; 101785398; -.
DR KEGG; sita:101785398; -.
DR OrthoDB; 211713at2759; -.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF16; CALLOSE SYNTHASE 7; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR Pfam; PF04652; Vta1; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 501..519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..552
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 573..595
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 750..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1482..1504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1629..1648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1654..1676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1730..1750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1762..1782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1803..1824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1830..1850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1870..1887
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 337..452
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1925 AA; 223060 MW; 868C25F035B04E66 CRC64;
MASAGAGPSG PVRSQSGRQR TMSRLPTRAL TMRPEGFSGE DGVEIVELVP SSLAPIVPIL
RAANEIEEEN PRVAYLCRFT AFEKVHTMDP NSNGRGVRQF KTYLLHKLEK DEQETKRRLA
STDAREIQKF YEYYCQKYLE EDHEKRKPEE MARYYQIASV LYDVLKTVTP GKHHPEYDKY
AEGVEKEKAS FSQYNILPLN ISVPRQPIME IPEIKAAVGL LRQMDGLPMP KPQSSDGKTG
LDGMDRPVQD LLEWLWQTFG FQKGNVENQK EHLILLLANI DMRQQGHAHQ SERHVHMIRN
STVIDLMDKI FKNYNSWCQY LHLESNIRIP RDASTQQPEL LYIGLYLLIW GEASNVRFMP
ECLCYIFHHM ARDLHDIISD RRDGWFDPPF QREGSDDAFL QLVIEPIYSV MQKEAARSKR
GTVSHSKWRN YDDLNEYFWS KKCFKKLGWP MDPTADFFAV PTRTKNETEQ HDHAIRRRRA
SKTNFVEVRT FLHLFRSFDR MWAFFILSFQ AMAIIAWSPS GSLSSIFEAD VFRNVLTIFI
TAAFLNFLQA MLEIILNWKA WKSLECSQRM RCILKFAAAI AWLIILPITY SGSIQNPTGL
VKFFSNWIGN LQNESIYNFA VALYMLPNIL SALFFIFLPI RGVLERSNSR IIRFLLWWTQ
PKLYVARGMY EDTGSLLKYT TFWILLLICK LAFSFYVEIA PLVEPTRIIM SLDRPPYEWH
EFFPNLQHNL GVVTTVWAPI VMVYFMDTQI WYAIFSTICG GVNGAFSRLG EIRTLGMLRS
RFQAIPRAFG KKLVPNRGSH FKREEEDRNP PYDKFADIWN AFITSLREED LLNNREKNLL
IVPSSGGETS VFQWPPFLLA SKIPIALDMA KNVKKKDDEL MKRINQDPYT EYAVIECYET
LLDILYSIIV EQSDKKVIDK IDESIKNSIE CKQLVKEFRL DELPQLSEKF DKLLDLLKFY
DENDPTKNNT QIANLLQDIM EIITQDIMKN GQGILKDEGQ KQLFANLNLD PLKHVAWREK
CVRLQLLLTT KESAIYVPTN LEARRRITFF ANSLFMKMPR APPVRSMMSF SVLTPYFKEE
VLFSPKDLGR KNEDGISILF YLRKIFPDEF RNFLQRINCK PKDEEELKER MEEICHWASY
RGQTLSRTVR GMMYYRKALE IQCLQDTKDP AKFGRDTSIE SYQELQSDSE MAQAIADIKF
TYVVSCQIYG MQKTSKKKED KNRYLNILNL MITNPSLRVA YIDEVEAPTG NGTTEKTYYS
VLVKGGEKYD EEIYRIKLPG RPTDIGEGKP ENQNHAIIFT RGEALQAIDM NQDNYIEEAF
KMRNVLEEFE SRKYGKRKPT ILGLREHIFT GSVSSLAWFM SNQETSFVTI GQRVLANPLK
VRFHYGHPDI FDRLFHITRG GISKASKTIN LSEDIFSGFN STMRGGNVTH HEYMQVGKGR
DVGMNQISSF EAKVANGNGE QTLSRDIYRL GRRFDFYRML SFYFTTVGFY FSSMVTVLTV
YVFLYGRLYL VMSGLEKSIL MDPRNQQNVK ALENALASQS VFQLGLLLVL PMIMEVGLEK
GFRTALGEFI IMQLQLASMF FTFQLGTKTH YYGRTILHGG AIYRPTGRGF VVYHAKFTEN
YRLYSRSHFV KGLELLILLV VYLVYGSSYR SSNLYIFVTC SIWFLVASWL FAPFIFNPSC
FEWQKTVDDW TEWRKWMGNR GGIGMSVEKS WEAWWISEQD HLRKTSIRAL LLEIIISLRF
LIYQYGIVYH LNIAVARHNK SIMVYALSWV VMLLVLVVLK MVSIGRQKFG TDLQLMFRIL
KGLLFLGFVS VMAVLFVVLN LTIADVFASI LGFLPTGWCI LLIGQACSPL LRRTVLWDSI
MELGRSYENI MGLILFLPIG FLSWFPFVSE FQTRLLFNQA FSRGLQISRI LAGQEVDIGD
ESESE
//
