ID A0A137QPX4_9AGAR Unreviewed; 1755 AA.
AC A0A137QPX4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 03-MAY-2023, entry version 18.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN ORFNames=AN958_06023 {ECO:0000313|EMBL:KXN89269.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN89269.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN89269.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN89269.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) 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: 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; KQ962096; KXN89269.1; -; Genomic_DNA.
DR STRING; 1714833.A0A137QPX4; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000070249; 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:UP000070249};
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 381..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 422..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..652
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1224..1244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1277..1298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1382..1412
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1488..1508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1520..1548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1560..1584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1591..1615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1665..1694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1715..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 234..346
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 COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1755 AA; 199965 MW; F95E3C60BB7A59DF CRC64;
MASPGYPRPT DPRNTPYTPQ HQGTLQSGPP FPSPRREYDE SSELGEHYNS VNSSTARLAG
SPGYYDQSNE SGEYGRYNPS VDSHASFPSV SPFTDPGFGS TEHYPAWSAD RQIPMSTEEI
EDIFLDLTQK FGFQRDSMRN MFDFLMHLLD SRASRMSPNQ ALLTVHADYI GGQHANYRKW
YFAAQLNLDD AVGQTQNPGL QRLKSMKGAK PVGSKSLDSA LNRWRNAMNN MSQYDRLRQI
ALYLLCWGEA GNVRFVPECL CFIFKCADDY YRSPECQNRV DPVPEGLYLN SIIKPLYRFM
RDQGYEVVDG KFVRKEKDHD QIIGYDDINQ LFWYPEGLAK IVLQGGQRLI DIPPTQRFMK
LGKVEWQRTF FKTYFEKRST AHLLVNFNRI WIIHVAIFYF YTAFNSPKVY APRNKAFPSA
PMTWSATALG GAVATGIMIL ATLAEFSYIP TTWNNASHLT TRLIFLLVIL ALTAGPTFYI
ALVDGRPTSA NSQIPLIIGI VQFFISAVAT LAFAIIPSGR MFGDRVAGKS RKYMASQTFT
ASYPALPRSA RTASIVMWLL IFGCKFTESY FFLTSSFSSP IAVMARTKVQ GCSDKIFGNA
LCTNQVPFAL AIMYVMDLIL FFLDTYLWYI IWVVIFSIGR SFSLGLSIWT PWKDIYTRLP
KRVYAKLLAT AEMEVKYKPK VLVSQIWNAI IISMYREHLL SIDHVQRLLY HQVDGPEGRR
TLRAPPFFTN QDGSKDTFFP AGGEAERRIS FFASSLTTAL PEPLPVDAMP TFTVLVPHYS
EKILLSLREI IREEDQNTRV TLLEYLKQLH PVEWDNFVKD TKILAEESEA MDGTASQHNE
KSNKIDDLPF YCIGFKTSSP EYTLRTRIWA SLRAQTLYRT VSGMMNYSKA IKLLYRVENP
DIVHNFGGNT ERLEKELERM ARRKFKFAIS MQRFSKFNKE EQENAEFLLR AYPDLQIAYL
DEEPGPKGGE ARLFSALIDG HSEIDEKTGK RKPKFRVELP GNPILGDGKS DNQNHAIIFY
RGEYLQLIDA NQDNYLEECL KIRNILGEFE EYSLSSQSPY AQWGHKEFNR SPVAIVGTRE
YIFSENIGVL GDIAAGKEQT FGTMTARALA WIGGKLHYGH PDFLNATFMT TRGGVSKAQK
GLHLNEDIFA GMNAFGRGGR IKHSEYYQCG KGRDLGFGTI LNFQTKIGTG MGEQMLSREY
YYLGTQLPID RFLTFYYGHP GFHINNILVI YSIQVFMITL LYIGTLNKQL AICRVDGQGN
VIGGQPGCYN LIPVFDWIKR CITSIFLVFF IAFLPLFLQE LVERGTGKAI LRLAKHFLSL
SPIFEVFSTQ IYSNSILSNL TFGGARYIAT GRGFATSRIS FSILYSRFAG PSIYMGMRNL
LLLLYATMSI WIPHLIYFWL SVLSLCIAPF LFNPHQFSFA DFIIDYREFL RWMSRGNSRT
KASSWYGYCR LSRTMITGYK KKKLGHPSEK LSGDVPRASW RSVIISEIIW PICMAIILVI
AYMFVKSFPD KNGQFGPSPL IRIAVIGIGP VVWNAAVLIS LFFISLFLGP MMESWTKFGS
VMAALAHVLG LVGLVAFFEF FWFLELWDAS HAVLGVIAII AIQRAIQKFF IAVFLTREFK
HDETNRAWWT GKWYGRGLGN SAMSQPAREF IVKIVEMSLW TSDFLLAHIL LIILTPPTLI
PFFNSIHSTM LFWLRPSKQI RPPLFSTKQK RQRRWIVVKY TVVYVIMVSI LAALIVLPAL
FRDRITFDCA ICRNI
//
