ID A0A1W0A166_9STRA Unreviewed; 2522 AA.
AC A0A1W0A166;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN ORFNames=THRCLA_03720 {ECO:0000313|EMBL:OQS03997.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS03997.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS03997.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS03997.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQS03997.1}.
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DR EMBL; JNBS01000699; OQS03997.1; -; Genomic_DNA.
DR STRING; 74557.A0A1W0A166; -.
DR OrthoDB; 48003at2759; -.
DR Proteomes; UP000243217; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR049039; RMD1-3_a_helical_rpt.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
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; 2.
DR Pfam; PF21033; RMD1-3; 1.
DR Pfam; PF00083; Sugar_tr; 1.
DR SMART; SM01205; FKS1_dom1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS50005; TPR; 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:UP000243217};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OQS03997.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 413..434
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1292..1316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1357..1374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1386..1409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1449..1468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1489..1511
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1592..1612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1624..1646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1652..1670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1703..1721
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1741..1764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1792..1812
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1819..1839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1845..1869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1881..1901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1907..1928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1981..2001
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2013..2033
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2040..2059
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2071..2094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2106..2126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2141..2162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2270..2289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1742..2166
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REPEAT 2472..2505
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 2187..2209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2194..2209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2522 AA; 283962 MW; DF625E61DABAEF5A CRC64;
MALDRAGSNY FMLASDSKRS LGDTRYYRQG SSFRDRLELL DVLGDNPNDP SGSRYGINES
GSDPVGVFDD EISIDYCCDV LTKKFGFQEG SVNNQREHAL LLLANSKAQN RSNDVSNHIN
ILHRKLVGNY VEWCGFIQVE PAWYAGGVNE KLKNRMHMEL MLYLCIWGEA GNIRHMPECI
CYLYHQMMTM LNGDLNLSFT NPSLWYLESV IRPIWTECSG MQKKDALGKS LEHTKVRNYD
DLNEFFWKPT CIAVPVDRAG ETLKTHGKTY YEHRSIFTLV LNYYRIFHFN FMFLFALAVL
QYCVTISPKG AHSGFSQFTA LGQVVEPYTT RDLKLSLVFL VLMHAILSLL KCFLEVGHGW
HLLFGSTPGG ATSKSMTYGI ALSLRLLWNG AFAGLFVYMM IEGINTTTPV LDLFYIFAAA
FLGPSILLMI ATIFNHKTAL NTSFWAKFIR EGDSCYTGRH MTPPWSYRSV YIAYWLVLWT
LKAAVSYWIL ITPLMLPSLA IYNMPLQYTT SVVSMRNIGV IIALWAPVFF VFCYDTQIYF
TIFQALYGAY KGVRMRTGEY HGFAEISKAF RLLPQLFDSK VVTKDAIMLD SIPSADGHRK
SMLMARFVVV WNEVINFFRE GDLLDDKEAA ILQYDVAPHS GEIYKPVFLS AGKLEDAITS
VLKLHAKKGQ NGKRDLDGEL TVDLLLKDCI PSIKSCFNSV LYILDVMLDG SDAKVFEAMR
DIETITNNGQ FMATYEVTQI IHVKSALISF LEAVLDLPDP ITPTGHSSKA HSMPVIQEFV
RHFENFLNAV EMFCRSSPAI TAKLTHSNFT SSQNGYVIAA EGMLRLCTND SAMSNATRAL
LLLKLDTTEA MPRCSEAKRR LGFFMKSLMM DIPQLASVRE MKSFSVMTPF YAEGVLYSLE
ELNAPLVNHP IFAAAEEVGK NLTILKYLIT IHTAEWDNFL ERIGVNSEEE AFQQQPLELR
LWASYRGQTL ARTVQGMMLY EDAIKMLYWL EIGSSPNKTA EMKQRMLEDM VILKFSYICA
CQVYGKHRDE KKPQASDIDF LLKRYPNLRV AYVDTVKKDG KADYYSVLIK SESDKIVEVY
RYLLPGDPIL GEGKPENQNN ALPFTRGEFL QTIDMNQQHY FEECLKMPNL LMTADLHPSG
KPVSIIGMRE HIFTGNASSL SKFKSWQELV FVTLSQRVLA DPLYVRMHYG HPDIFDKVMC
LTRGGVSKAS KGINLSEDVF AGFNSTLRGG VVTHVEFMQC GKGRDVALSQ ISMFEGKLAN
GAGETCLARE GHRMGAFMDF FRLNSMYYSH TGFYFATWLT IVTAFVFIYC KVYLALTGVQ
TQIVYLMNDT TIIMKNSDKG FDTRVFNNLD NIVNTQYYIQ AGLFLTLPLM AVYFTEAGLR
RGFLRFFDMM ITAGWAFFTF QVGTTMHYFD TNIVHGGAKY QATGRGFKIT RETFVLLYKA
YSASHYRKAM ELIGLSIIYG TYGAFAICQK TPQSATNTFS QDFCSTSQGY GTQTFAIWFI
SILWLFSPFL FNTDGFDYEK SKVDILAWTK WMYMDEKDTD VDKVNNGGWI GWWKGDEEQY
HGTKPISRFT VVLRESRHFL LMWYVVTLRF KVVYLVVVCA AIIVTLALFQ LGHTGGGLRA
SAPIRATVYA VLIVVFGTLY FLGTMVYPWK MAWVDSLSLF FGYMAGLYGV NEMIRVFAFP
TVSIVNVGVF VQLAFFWDFL FGAVMLVPLM VFSCIPFMNV IQTRMMYNEG FSRVLSDSSQ
YAFSIAGVIG FIGAGSCGWL YYVLTTLDTS AGFLSYTNAF RIVIAEGTGS TAYYVILGSI
VGVLISAIVG FYIGRRLTIV VGGFVSFLGM SLLTAVSSYP SDGKVLMFCG LSAFGLSLGI
LFPAITCYCY EISTKEMRGK IMLLLAVGFL TGMLAASYFS YNTSIVWLWQ AFWCFLVFAC
LTPAINLLPE SPEWVLAREG KDACRACLVL LRRRQDVTAE LETLEENQQH QYSFGNGAYK
AIVGVIFMAI SSLSTLSLYT YTARVFIGFN RSMMLTNCLA TELLFAAFSF LYIERLTHKL
LLLISFALVA ITTGLLAAHD HFQIFGVQDQ TALEIILIVT FAIKGAAFPA TLWVSSVGLF
RTKGRFITAP LYFALYFALH IGTTYLRNNS TSTRSSQSKE YIWLFALSSL CVLGFFSAFG
LARRSNGMVC TSAEMEYELK QKEDARLREQ NASRSRAYSR QTSKRVTGNA TLSPHKSTQY
LHAENIDDTK LKSVMILVAR SVRVLKAAPF VRSFVSVSNR KDPFGAASKA ILPFVALTAF
SATIAMTTLC DSTNALRAEE LYNNAGYDRR DLLGFLKEKL ADNPRDAGIL WRLARAAYDV
ANLSSTPAAE KKELTYYAHD IIKKALDVTT EDFAVQKWSG IILSSIGDYE GTKVSLANSY
IVKEHWEKAV ALNPNDATSH HLLGRWSLTI ADISWIERKV AAALFGTPPQ ATYAEALAHF
VQADTISPGF WKKNTFMIGQ VYYKMSNYAE AKTWVEKAIA IETKSEEDAQ VHQEAIALLT
KL
//
