ID A0A2G5DYP7_AQUCA Unreviewed; 1917 AA.
AC A0A2G5DYP7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=AQUCO_01400908v1 {ECO:0000313|EMBL:PIA48642.1};
OS Aquilegia coerulea (Rocky mountain columbine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC Aquilegia.
OX NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA48642.1, ECO:0000313|Proteomes:UP000230069};
RN [1] {ECO:0000313|EMBL:PIA48642.1, ECO:0000313|Proteomes:UP000230069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT "WGS assembly of Aquilegia coerulea Goldsmith.";
RL Submitted (SEP-2017) 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; KZ305031; PIA48642.1; -; Genomic_DNA.
DR STRING; 218851.A0A2G5DYP7; -.
DR InParanoid; A0A2G5DYP7; -.
DR OrthoDB; 211713at2759; -.
DR Proteomes; UP000230069; Unassembled WGS sequence.
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; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF48; CALLOSE SYNTHASE 3; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000230069};
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 436..453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 507..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1483..1506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1526..1545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1624..1641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1647..1671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1725..1743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1755..1776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1788..1811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1817..1839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1860..1880
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 269..385
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1917 AA; 221243 MW; 8F4A20361FA5A2E8 CRC64;
MKLNLVTLEL LIYVDSTPSR KHTGWTLHLV GRGGSPNSRL HFCNGLEREN DPTLMGRVKK
SDAREMQSFY QHYYKKYIQA LQNAADKADR AQLTKAYQTA AVLFEVLKAV NLTQSLEVDR
EVLETHNKVA EKTEVYVPYN ILPLDPDSAN QAIMRYPEIQ AVVVALRNTR GLPWPTGYKK
KPDEDILDWL QAMFGFQKDS VANQREHLIL LLANVHIRQF PKPDQQPKLD ERALTEVMKK
LFKNYKKWCK YLDRKSSLWL PTIQQEVQQR KLLYMGLYLL IWGEAANLRF MPECLCYIYH
HMAFELYGML AGNVSPMTGE NVKPAYGGEE EAFLRKVITP IYETIAKEAE RSKRGKSKHS
QWRNYDDLNE YFWSVDCFRL GWPMRADSDF FCEPSSQLRL DKNGESKPAA RDRWVGKINF
VEIRSFWHIF RSFDRMWSFF ILCLQAMIII GWNGSGQPSA IFEADVIKKV LSIFITAAIL
KLGQAVLDVI LSWKARRSMS FQVKLRYILK VVSAAAWVII LPVTYAYTWE NPPGFALKIR
KLFGNSPSSP TLYILAVVIY LAPNMLAGVL FLFPFIRRFL EKTDYRIVMF MMWWSQPRLY
VGRGMHESAF SLFKYTMFWV LLIITKLAFS YYIEIKPLVG PTKTIMKAHI TNYQWHEFFP
RAKNNLGVVI ALWAPIILVC IQNAGQFLFL VYFMDIQIWY AIFSTLFGGI YGAFRRLGEI
RTLGMLRSRF QSLPGAFNAR LIPVDKTAAK KKKGLKATFS RKFEEIPSNK EKEAAKFAQL
WNRIISSFRE EDLISDREMD LLLVPYWADR DLDLIQWPPF LLASKIPIAL DMAKDSNGKD
RELKKRISAD NYMHCAVREC YASFRNIINF LVEGDPEKTV IKHMFDEIDK HIEADSLISQ
LKMSALPSLY EHFVKLIKIL LENKQEDRDQ VVILFQDMLE VVTRDIMEDE ESTLDVLHQG
PYGRYEGMTP LDQQVQLFAS PGAIKFPIEE TEAWKEKVSI KRLFLLLTVK ESAMDVPSNL
EARRRISFFS NSLFMEMPAA PKVRNMLSFS VLTPYYTEDV LFSIHELEVQ NEDGVSILFY
LQKIFPDEWT NFLERIGCSN EEELRKADAL EEELRLWASY RGQTLSRTVR GMMYYRKALE
LQAFLDMAKD EDLMKGYKAA EFTTEEHSKD ERSLWTQCQA VADMKFSYVV SCQQYGVHKR
SGDPRAHDIL KLMSTYPSLR VAYIDEVDVT VKDKSKKGNQ KIYYSALVKA APKPINSSEP
QPVQNLDQVI YRIKLPGPAI LGEGKPENQN HAIVFTRGEG LQTIDMNQDN YMEEAFKMRN
LLDEFLKKHD GVRYPSILGL REHIFTGSVS SLAWFMSNQE TSFVTIGQRL LANPLKVRFH
YGHPDVFDRL FHLTRGGISK ASKIINLSED IFAGFNSTLR EGNVTHHEYM QVGKGRDVGL
NQISLFEAKI ANGNGEQTLS RDIYRLGHRF DFFRMLSCYF TTVGFYFSTL VTVLTVYVFL
YGRLYLVLSG LEEGLSTQPA IRDNKPLQVA LASQSIVQLG FLMALPMMME IGLERGFRTA
LSEFILMQLQ LAPVFFTFSL GTKTHYYGRT LLHGGAEYRA TGRGFVVFHA KFADNYRFYS
RSHFVKGIEI MILLVVYQIF GHTYRSALAY VLITISMWFM VGTWLFAPFL FNPSGFEWQK
IVDDWTDWNK WISNRGGIGV LPEKSWESWW EKEQEHLRHS GKRGIIAEIV LALRFFIYQY
GLVYHLNLTK NTKSVLVYGA SWLVIAVILL VMKTVSVGRR KFSADFQLVF RLIKGLIFLT
FIGILITLVA VPHMTPQDIV VCVLAFMPSG WGLLLIAQAC KPVVQRAGFW GSVRTLARGY
EVIMGLLLFT PVAFLAWFPF VSEFQTRMLF NQAFSRGLQI SRILGGQKKE RSASNKE
//
