ID G4UXE3_NEUT9 Unreviewed; 1955 AA.
AC G4UXE3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
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-D-glucan-UDP glucosyltransferase {ECO:0000256|ARBA:ARBA00031935};
GN ORFNames=NEUTE2DRAFT_95037 {ECO:0000313|EMBL:EGZ69697.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ69697.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ69697.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR EMBL; GL891258; EGZ69697.1; -; Genomic_DNA.
DR STRING; 510952.G4UXE3; -.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000844_0_1_1; -.
DR OMA; AWTDFFI; -.
DR Proteomes; UP000008513; 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 InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF29; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008513};
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 488..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 533..555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 575..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 725..746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1353..1372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1405..1426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1507..1540
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1616..1636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1657..1680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1700..1723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1732..1754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1854..1878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 342..454
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1955 AA; 223398 MW; 8FF99E7BA2AC961B CRC64;
MSGYPQQGGG GHHDDGYGHA PNANGNGDAY YNDDQQYYDN RNGGHAAGGQ HGEGYYDESG
YYNADPNNPY HQDGGYYDNH EGFQEGYDNG YYDQHGYDQA GGYRDNHAAR GSEEDSETFS
DFTMRSDMAR AAEMDYYGRG DERYDSQYGD QGGARGYRPP SSQISYGGNR SSGASTPNYG
MDYGNVLPAG QRSKEPYPAW TSDAQIPLSK EEVEDIFLDL CAKFGFQRDS MRNMYDHLMT
LLDSRASRMT PNQALLSLHA DYIGGDNANY RKWYFAAHLD LDDAVGFANI KGKKGNLKRT
KKKAKGDEPQ NEAEILQELE GDDSLEAAEF RWKTRMNRMS QHDRVRQLAL YLLIWGEANQ
VRFMPECLCF LFKCADDYLN SPACQNMVEP VEEFTFLNNV ITPLYRYCRD QGYEIYEGVY
VRRERDHEQI IGYDDCNQLF WYPEGINRIV LEDKSKLVDV PPAERYLKLK DVNWKKCFFK
TYRETRSWFH MLVNFNRIWI IHLTMFWFYT AYNMPTIITP MYEQQVNQSP PKAAMWSFVG
FGGAVASLIN FGATLAEWAY VPRRWSGAQH LSKRMLFMVF VLIINLAPGV YVFLPGLSGQ
ALIDHQNSTP VYIVGIVHFF IALVTFLFFA VMPLGGLFGS YLTKNSRKYV ASQTFTASWP
RLNGHDMAMS FGLWVVVFGA KFGESYVYLT LSIRDPIRYI GLMDTRSCLG DSILKTYLCP
YQPQITMGLM IFTGMIFFFL DTYLWYVLIN SVFSVARAFY LGSSIWTPWR NVYARLPKRI
YSKVLATTDM EIKYKPKVLI SQIWNAIVIS MYREHLLAID HVQKLLYHQV PSEQEGKRTL
RAPTFFVSQE DQSFKTEFFP QYSEAERRIS FFAQSLSTPI PEPLPVDNMP TFTVMIPHYS
EKILLSLREI IREDEPYSRV TLLEYLKQLH PHEWDCFVKD TKILADETSQ FNGETEKEKE
KEKEKETVKS KIDDLPFYCI GFKSSAPEYT LRTRIWASLR FQTLYRTVSG FMNYARAIKL
LYRVENPEVV QMFGGNSDKL ERELERMARR KFKLCISMQR FAKFKKEEME NAEFLLRAYP
DLQIAYLDEE PPLAEGEEPR LYSALIDGHS EIMENGSRRP KFRIQLSGNP ILGDGKSDNQ
NHAIIFYRGE YIQLIDANQD NYLEECLKIR SVLAEFEEMK TDNLSPYTPG VKNEVRHPVA
ILGAREYIFS ENIGILGDIA AGKEQTFGTL FARTLAQIGG KLHYGHPDFL NGIFMTTRGG
VSKAQKGLHL NEDIYAGMNA LLRGGRIKHC DYYQCGKGRD LGFGSILNFT TKIGTGMGEQ
LLSREYHYLG TQLPIDRFLS FYYAHPGFHL NNMFIMLSVQ LFMLCCVNIG VLRHETIRCE
YNREVPITDA LFPTGCSNTD ALLDWVYRCV LSIIFVLFLA FVPLIVQEMM EKGVIRSATR
FIKQILSLSP FFEVFVCQIY ANSVQQDLSF GGARYIGTGR GFATARIPFG VLYSRFAGPS
IYFGARLVMM LLFACLTVWH AALIYFWISL MALVISPFLY NPHQFSWGDF FIDYREYLRW
LSRGNSRSHA SSWITFCRLS RIRITGFKRK IIGDPSSKLS GDVARAAITN LFWSEMLTPF
ILVCLTTIPY LFINAQTGVK GDFGPHANDD SIQPTAALIR LLVVTFAPMA VNAGVLGGLF
GMACCMGPLL SMCCKKFGSV LAAIAHGMSV IILLVMFEVM FVLQNFEFTP TLLGMIAMVS
IQRFIIKMIV SLALTREFKT DTSNIAFWTG KWYSMGWHSV SQPAREWLAK ITELSMFGAD
FILGHLILFS MFPVLIIPKV DVLHSVILFW LRPSRQIRAP IYSLKQTKLR RRRVIRYAIL
YFVLLVIFVA LIVGPIVAGK QLPTDTLDVV NSFGGGSLIL RQYPWKLGPS GDNDDTRGRL
ETGTKATNYS GVWTPTTTSD YVAKATSKAE RRMAF
//
