ID A0A2T9Z549_9FUNG Unreviewed; 2029 AA.
AC A0A2T9Z549;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 03-MAY-2023, entry version 16.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN ORFNames=BB559_000456 {ECO:0000313|EMBL:PVU99735.1};
OS Furculomyces boomerangus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Harpellaceae; Furculomyces.
OX NCBI_TaxID=61424 {ECO:0000313|EMBL:PVU99735.1, ECO:0000313|Proteomes:UP000245699};
RN [1] {ECO:0000313|EMBL:PVU99735.1, ECO:0000313|Proteomes:UP000245699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AUS-77-4 {ECO:0000313|EMBL:PVU99735.1,
RC ECO:0000313|Proteomes:UP000245699};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PVU99735.1}.
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DR EMBL; MBFT01000022; PVU99735.1; -; Genomic_DNA.
DR STRING; 61424.A0A2T9Z549; -.
DR Proteomes; UP000245699; 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 Gene3D; 1.20.120.550; Membrane associated eicosanoid/glutathione metabolism-like domain; 1.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
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 Pfam; PF01124; MAPEG; 1.
DR SMART; SM01205; FKS1_dom1; 1.
DR SUPFAM; SSF161084; MAPEG domain-like; 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:UP000245699};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 685..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 741..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 854..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1477..1498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1534..1555
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1628..1645
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1652..1669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1738..1760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1792..1815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1835..1858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1865..1888
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1938..1956
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1990..2010
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 437..549
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 167..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2029 AA; 232807 MW; 9206BD6C68334336 CRC64;
MDKIVLSRDF AYDALVVVVM SIQCYASGMM GLKYRKKYNV HHPDMGCGRH AEKLTDEEWE
DFNSVIRVHQ NYVEQLPIVI SSVLIGGLYY PKIAAGMGGL YIVGRMVYIY GYVVHGASGR
MAGGLEDAAY INNYDENDPY GDMGYEEYNG HDSFDVSYYE QRESDYGDGA YYQSGNGDRS
IYPEAAGTPG GRRRRGNKRS GVESDAESIS DGDFSVRSSL VRTPASHGSV ADIDIFGEYR
SKNGNSGRYA NYAPSTDSLI NLIENKKTYH PTGSVASFSQ NSSWVSNQGR SGMDFAQAEL
ILNDSPYPSW SDPNQIPLSK EEIEDIFKDL TNRLGFQKDN MRNVYDMMMV MLDSRASRMS
PLMSLLTLHS DYIGGDHANY RRWYFSAQLD HDTPTIRQTT KNKKYNTETT EEEPLENDTI
SNFVENWRAK MNSMSQHDKA RQIALWLLIW GEAGNLRFCG ELVAFLFKLA EDYYKSPYCQ
QRVEPEREGY YLQNIVTPIY NFLRDEGYQL INGKYFKRER DHDTTIGYDD LNETFWTPEG
LRQLQFEDKT LLMDLPVEQR WHRLKDVFYK KSIKKTYKEK RSMLHFLTNF NRIWVMHVVV
YYYYIIFVAD FLYDNLFELR NSSNPSSVTK SVEQRLPDIT PRRFSLIAAG GAIAPLIGII
GTFAEMTYLK LSKPIFKTLM MRIMLLLLFF VIDIGPLYFC WTYGNDPTFK VTQSSTTKYS
YTATPIAAAN VNSSKLAMFK IARIIAIVQF IFSILITVYL SIVPPGTMFQ SKKLSRSSRG
LVNRTFTANF PPLKRSSRAT SVSLWFIIFL CKYIESYFFL ARSFKDPFRW LYQYNPIDCQ
EKFLGNILCK NQNYITLGIM LTLDLLLFFL DTYLWYVIWN TMFSVGRSFY MGISIWTPWR
NIFSRLPKRI YTKILATADM EVKYKPKVLC SQIWNAIIIS MYREHLLSIE HVQKLLYQQV
TSDDSGKRTL KPPTFFVAQD DASFEQEFYP PHSEAERRIS FFAQSLSTVL PEPVPVENMP
TFTVLTPHYG EKILLSLREI IRESDKYSRV TVLEYLKALH PDEWDNFVKD TKILAEESAG
LESNVGSRAF EDKGETKGKI DDLPFYSVGF KSASPEFTLR TRIWASLRSQ TLYRTISGFM
NYAKAIKLLY RVENPEMVLL FGGNGSLKLE KELERMANRK FRFVVAMQRY MKFNKEEHES
ADFLMKTYPS LQIAYLDEEL SPDGKSSRVY SCLVDNECEV LSNGARRPRY RIQLPGNPIL
GDGKSDNQNH AMVFVRGEYT QMIDANQDNY LEECLKIRNM LGEFEEYNPP TVSPYSPASE
PQGPPVAIVG AREYIFSESV GVLGDVAAGK EATFGTLTQR MMAEIGGRLH YGHPDFINFI
FMSTRGGFSK AQKGLHLNED IYAGMNAFSR GGRIKHTEYF QCGKGRDLGF CSTLNFITKI
GTGMGEQMLS REYYWLSCFL PLDRFLTFYY AHPGFHINNL MIMASVQLFM LSVMFVGTMN
ITFNICIKYV LSDPNYYQQV LSAQCLMLQP VQDWVGRTTL AILVVLLIAF LPLFLQMLTE
QGFSHAMTRL GKQFVSLSPM YEVEVTQIYA YSISSNMSFG GARYIGTGRG FATSRLSFAT
LYSRFSEASI YFGFRLLLIL CFITATTWQW QLVYFWFSIS ALCISPFVYN PHHFVKTDFI
LDYRDWLRWL GAGNSSPEAH SWVSHCRLSR IRITGYKRKR LGEKTPSTGY VPRAKKSVIV
FSEVLTPIIM ALLFIIAYSF TNSRWGLSPY SDANNTKRNN TAINKNNVKS SIIAMLIVSL
APVAINAGLT IAMFAFSFFA GPLLSSCIPG FGKTMAGICH TVATVIQIAM FFVFYFLNGN
SVGRAILGII GSVFIQRALF SVLLSLFLTR EFGEDETNIA WWTGRWYDKG MGAWVPTLIL
REWVCKIIEC SIFTADVLIG HVIFFFLFIF TLIPWIDKWH SAMLFWLRPS RQIRPPIYSL
KQRKQRQRIA FFYSIILSAL FIVFIGLLIV PNLSFVKNMK LSVLNSLYL
//