ID A0A2S6C473_9PEZI Unreviewed; 1934 AA.
AC A0A2S6C473;
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};
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase {ECO:0000256|ARBA:ARBA00031935};
GN ORFNames=CBER1_02494 {ECO:0000313|EMBL:PPJ54510.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ54510.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ54510.1}.
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DR EMBL; PNEN01000562; PPJ54510.1; -; Genomic_DNA.
DR STRING; 357750.A0A2S6C473; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000237631; 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:UP000237631};
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 510..531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 543..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 586..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1350..1369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1402..1423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1519..1537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1613..1634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1654..1680
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1692..1712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1724..1749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1790..1815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1849..1873
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 353..465
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1934 AA; 221685 MW; E0198E1CB72090F4 CRC64;
MAHPQQQGGY DDGYGAQHPH DAHGAQDGYY HDDQAYYDQQ GGGYGQGHDG YYDDNGYYQG
GQDGYGQDGY YDAPGQQGYQ DEYYNDQYYD QGAPAAGQYQ QQGRGYGGQR RSGRRGHDSE
EDSETFSDFT MRSDMARAAE MDYYGRGDER INSYGDGTGR GYRPPSSQVS YGGNRSSGAS
TPVYGMDYTS ALPAGQRSRE PYPAWTSDAQ IPLSKEEIED IFLDLTAKFG FQRDSMRNMF
DHFMTLLDSR ASRMSPNQAL LSLHADYIGG ENANFRRWYF AAHLDLDDAV GFANMKLGKA
NRATRKARKA AKKKKQETGP ENEEATLESL EGDNSLEAAE YRWKTRMNRM SQHDRTRQIA
LYLLCWGEAN QVRYMPEIMA FIFKCADDFY HSPACQNRVE PVEEFTYLNR CITPLYNYCR
DQGYEIFDGK YVRKERDHQK VIGYDDMNQL FWYPEGIERI VFEDKTRLVD LPPAERYERL
GDVIWKKAFF KTYKETRSWF HMLTNFNRIW VIHVCVFWFY TAFNSPTLYT ANYQQQLNNK
PNAAAQWSAV ALGGTLACLI QIFATLVEWM YVPRRWAGAQ HLTKRLFFLL GMFALNVAPS
VYIFIVSQTG KIALILGVVQ FLIALATVFF FAIMPLGGLF GSYLNGKRRQ YVSSQTFTAS
YPRLTGNDMW MSYGMWVLVF AAKLAESYFF LTLSFRDPIR ILSTMKIENC LGDKIIGTIL
CYHQPTVLLI LMYFTDLILF FLDTYLWYVI WNCVFSVARS FYLGVSIWTP WRNIFSRLPK
RIYSKVLATT DMEIKYKPKV LISQIWNAIV ISMYREHLLA IDHVQKLLYH QVPSEQEGKR
TLRAPTFFVS QEDHSFKTEF FPAQSEAERR ISFFAQSLST PIPEPLPVDN MPTFTVMIPH
YGEKILLSLR EIIREDEPYS RVTMLEYLKQ LHPHEWDCFV KDTKILADET SQFNGDYEKN
EKDTQKSKID DLPFYCIGFK SAAPEYTLRT RIWASLRSQT LYRTISGFMN YSRAIKLLYR
VENPEVVQMF GGNSDKLERE LERMARRKFK IVVSMQRYAK FSKEERENAE FLLRAYPDLQ
IAYLDEEPAT EEGEDPKLYS ALIDGHSELM DNGMRRPKFR IMLSGNPILG DGKSDNQNHC
LIFYRGEYIQ LIDANQDNYL EECLKIRSVL AEFEEMTTDN VSPYTPGLPP TKFNPVAILG
AREYIFSENI GILGDVAAGK EQTFGTLFAR TLAQIGGKLH YGHPDFLNGI FMTTRGGVSK
AQKGLHLNED IYAGMNAILR GGRIKHCEYY QCGKGRDLGF GSILNFTTKI GTGMGEQMLS
REYYYLGTQL PLDRFLSFYY AHPGFHINNL FVMLSVQLFM WVLLNLGALR HETISCRYNR
DVPITDPLFP TGCANIVPIM DWVQRCIVSI FIVFFISFVP LTIQELTERG FWRAATRLAK
HFSSLSPLFE VFVTQIYAYS LQQDLSFGGA RYIGTGRGFA TARMPFGVLY SRFAGPSIYL
GARLLLMLLF GTLTVWGYWL LWFWVSILAL CICPFLFNPH QFAWADFFID YREFLRWLSR
GNTKAHSASW IGFVRLSRTR LTGFKRKALG EPSAKLSGDT PRSKFTNVFF SEIIGPLVFV
AVTLIPYLFI NAGVGVIDDN NQDGQDITPT SSLIRVGICA FGPIGVNAGV AIGFFGMACC
MGPVLSMCCK KFGAVLAAIA HAIAVIMLLA FWEVMFFLES WSFAKALIGM IAVVAIQRFV
FKLIICLALT REFRADTSNI AWWTGKWYAL GWHTISQPGR EFLCKITEMG FFAADFCLGH
ILLFFMLPAL LIPYVDKFHS VMLFWLRPSR QIRPPIYSLK QSKLRRRRVI RYAILYFSMF
VLFLVLVVGP VIVNKFMKIP KIDIMNLQQP NDWNNNDTSA SETGTAVNGG AEATASSDAS
RMMARMMQHA YQQM
//
