ID J4KKQ1_BEAB2 Unreviewed; 1943 AA.
AC J4KKQ1;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 03-MAY-2023, entry version 36.
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=BBA_10207 {ECO:0000313|EMBL:EJP60844.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP60844.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP60844.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP60844.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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; JH725248; EJP60844.1; -; Genomic_DNA.
DR RefSeq; XP_008603526.1; XM_008605304.1.
DR STRING; 655819.J4KKQ1; -.
DR GeneID; 19893219; -.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; J4KKQ1; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000002762; 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:UP000002762};
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 482..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 569..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 610..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..751
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 1604..1630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1657..1684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1696..1721
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1727..1745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1853..1877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..448
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1943 AA; 221471 MW; 9D016BC823D0C115 CRC64;
MSGYQSGHHD QYDQGYGQAG HGDGYYQDDQ YYDNGHGDHG AHGAHGAQGD GYYDESGYYH
ADASNPYHQD GGYYDGHDQY QDDYYNNNNN QGYYDGDYNQ GYAQGGRHQS EEESETFSDF
TMRSDMARAA EMDYYGRGDE QYAGYGEGGR GYRPPSSQMS YGGNRSSGAS TPNYGMEYGN
GLPSQRSKEP YPAWTSDAQI PLSKEEIEDI FLDLTSKFGF QRDSMRNMYD HLMTLLDSRA
SRMTPNQALL SLHADYIGGD NANYRKWYFA AHLDLDDAVG FANASTKNRK RKAKKSKKKG
ADAANETETL QELEGDDSLE AAEYRWKTRM NRMSQYDRVR QIALYLLCWG EANQVRFMPE
CLCFIFKCAD DYLNSPTCQA LVEPVEEFTF LNNVITPLYQ YCRDQGYEIL NGVYVRRERD
HKHIIGYDDC NQLFWYPEGI ERIVLEDKSK LVDLPPAERY LKLKEVNWKK CFFKTYKESR
SWFHLLLNFN RIWVIHLTMF WFYTSHNAPS LITYKYEQQK DNQPPASKQF SIVGFGGAIA
SLIQIFATLA EWVYVPRRWA GAQHLTKRLL FLIVILVLNV APGIKVFMFH ANGKADDPEK
RNSDTPIDKA LGIVHFVIAI FTFLFFSVMP LGGLFGSYLT KKSRRYVASQ TFTASYPRLT
GNDMAMSFGL WLTVFGAKFG ESYVYLTLSF RDPIRYLSIM KIECLGDKMF GSSTETQQIL
CKHQPTIVLI LMTFTDLIFF FLDTYLFYVI LNTVFSIARS FYIGSSIWTP WRNIFSRLPK
RIYSKVLATT DMEIKYKPKV LISQVWNAIV ISMYREHLLA IDHVQKLLYH QVPSEQEGKR
TLRAPTFFVS QEDHSFKTEF FPSHSEAERR ISFFAQSLST PIPEPVPVDN MPTFTVMIPH
YSEKILLSLR EIIREDEPYS RVTLLEYLKQ LHPHEWECFV KDTKILADET AQMNGEPEKS
EKDTAKSKID DLPFYCIGFK SSAPEYTLRT RIWASLRSQT LYRTVSGFMN YSRAIKLLYR
VENPEVVQMF GGNSEKLERE LERMARRKFK LVVSMQRYSK FKKEEMENAE FLLRAYPDLQ
IAYLDEEPPL AEGEEPRLYS ALIDGHSEIM ENGMRRPKFR VQLSGNPVLG DGKSDNQNHA
IIFYRGEYIQ LIDANQDNYL EECLKIRSVL AEFEEMKPDN QSPYTPGVKN DVHTPVAILG
AREYIFSENI GILGDVAAGK EQTFGTLFAR TMAQIGGKLH YGHPDFLNGI FMTTRGGVSK
AQKGLHLNED IFAGMNALVR GGRIKHCEYY QCGKGRDLGF GSILNFTTKI GTGMGEQWLS
REYYYLGTQL PLDRFLSFYY AHAGFHVNNM FIMLSVQSFM LTLMSIGALR HETIRCDYNP
QKPITDPLYP TKCANTDELM GWIYRCIISI FFVFFISFVP LIVQELTERG VWRAALRFIK
QFCSLSPFFE VFVCQIYANS VQADLAFGGA RYIGTGRGFA TARIPFGVLY SRFAGQSIYF
GARLLMMLLF ATATAWQPAL TYFWIVLLGL IISPFLYNPH QFAWTDFFID YRDFLRWLSR
GNSRSHASSW ITFCRLSRTR ITGYKRKVMG DASAKMSADV PRAAVANIFL TEILTPLLLA
ATTTVAYLFI NAQTGVTDND TNSGVSPRFP IGPTGSLIRL AIVAFAPIGI NAGVLAAMFG
MACCMGPVLN MCCKKFGPVL AGIAHGAAAV FMILFFEVMY VLEGFNFARA LAGIIAATCI
QRFVFKLIVS LALTREFKTD QSNVAFWNGK WYSMGWHSVS QPAREFLCKI TELSMFSADF
ILGHWILFMM APLVLTPQID KIHSMMLFWL LPSRQIRPPI YSMKQSKLRR RRVIRFAILY
FILFVIFLAL VVAPGVIGKK VLGDMIFNAL GGGGSNGIGG MRLLQPWGLD NNNTEGRTET
GTKAGGGDAA ATSTDEASKL RLF
//
