ID A0A3M6VDM0_9STRA Unreviewed; 2450 AA.
AC A0A3M6VDM0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, 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=DD238_007582 {ECO:0000313|EMBL:RMX65128.1};
OS Peronospora effusa.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Peronospora.
OX NCBI_TaxID=542832 {ECO:0000313|EMBL:RMX65128.1, ECO:0000313|Proteomes:UP000282087};
RN [1] {ECO:0000313|EMBL:RMX65128.1, ECO:0000313|Proteomes:UP000282087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R14 {ECO:0000313|EMBL:RMX65128.1,
RC ECO:0000313|Proteomes:UP000282087};
RA Fletcher K., Klosterman S.J., Derevnina L., Martin F., Koike S.,
RA Reyes Chin-Wo S., Mou B., Michelmore R.;
RT "Comparative genomics of downy mildews reveals potential adaptations to
RT biotrophy.";
RL Submitted (JUN-2018) 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}.
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:RMX65128.1}.
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DR EMBL; QLLG01000265; RMX65128.1; -; Genomic_DNA.
DR STRING; 542832.A0A3M6VDM0; -.
DR VEuPathDB; FungiDB:DD237_007358; -.
DR Proteomes; UP000282087; 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 InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
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; PF00083; Sugar_tr; 1.
DR SMART; SM01205; FKS1_dom1; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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:UP000282087};
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 256..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..414
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1304..1325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1359..1377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1384..1403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1509..1530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1620..1640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1660..1681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1688..1708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1728..1754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1775..1803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1838..1858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1865..1883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1889..1912
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1924..1944
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1964..1984
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2037..2057
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2077..2094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2106..2124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2130..2152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2164..2184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2190..2211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..235
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1558..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2320..2339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2320..2336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2450 AA; 275202 MW; 6E246AFC74721007 CRC64;
MAIGPDGRTP VRRQAESNYL DVNREMALHR LESFHAAAYG PFELLQSKFG FQTSSVANQK
ENLGCWVTNY QMRVRYEAPE GATQSNEFIT KTALSRVHTK FFKNYLMWCK YLRTPPRASN
MEKEVTTSRM EKELALFLLL WGEAGNLRFM PECICFLYHK MAQKLDILDT LPNVEEGFYL
NEIVRPVYYV IAKMGSAKAP KGKRPLDHKD TTNYDDVNEF FWTAKCLDCD EMDVARMLEV
HDPKTFKEKR SVFNPVLAFF RIWYFLVVMF HIMIVITYVS YMAEGDDDGG LGFFLRIFTS
NQNKIRAHAS YTIFLTVTGL MAIKAVLQIW LYGSRLYKDS WMALGVFCRL FWHSFFFGLF
MAVHFSPDAS ALLGSKSSFL PGGGTQGSYL SMGLVYLVIY CIPVLIAAMC QAFLPRLIRC
IGIMNALNGT GRQYVGRYTS QPWKNYSRYS MSWYMIFFGK FFFALQFMIR PLMAPSIDIY
NISIDDNGVF QSGRNIMFIL ALWAPVFVVY MYDTQIWFIL YQSIIGLIMG KRMNIGHYVG
LAQLKTGMAG APKLFDDKVV SLKTKQPPSD GMAPVPDSGD AGELHHRDVV RLRFAIIWNQ
VVDNFRLNDL LDDRETVILQ YRILNKGERI QEPIFLLAGK LSKAVEVAAK SRSNKWATTT
LIKNIATADA LEGMQNGLEL SRGIFYLLLG GEEQKEVMSV LDYIYSSPDI VNLLDLTYLP
QLADNMVELL AVILDMPEEV SAIDGVETAT EELRMELHVQ VAQVVDRMRS IVLTLELMLN
DDTVSRKLHQ CRFLQTTADL EFQTWQLIKL YRADAAAETG LIAVHPGEGP ATPPPRFSPE
DFVSSCTRLF FLLRLDVANS LPRCEDAKRR MGFFLHSLSM EMPRVVSMEA MPSFSVMTPY
YSETVLFTLD ELNNPVHSNP LFAELEKKQK AKGWTELTIM KYLITFHAEE WSNFLERMGA
ASLEEALEIN STEVRLWASM RGQTLARTVH GMMLYEDAIR LLRWLEVYSL RDMSVQEKLD
EMNRISALKF SYITGCQIYS KQVANGDPRA ADIDYLMKKF PSWRVSFVDS ITEKDGDKEI
NRFDCVLVKA EADEIVEVYR YELPGNPILG EGKPENQNVA LPFTRGEYLQ TIDMNQEHYL
EECLKMPNFL ATATSTGEEV TVIGMKEHVF TGRASSLARF MTLQELVFVT LTQRVLAKPL
RSRMHYGHPD VFEKSFVVTS GGVSKASKGI NLSEDVFSGY NVTLRGGLVS HIEFMQCGKG
RDVTLSQINA FEAKLSNGCA ESCLSREGHR LTNSLDFPRL NSMFYGHFGF YICNVLTVFC
VYVYAYCKLY VATHSEVALT AVMTTGSLDS LASVMTTQYV LQFGMLTTLP LFATLFVEFG
FKQALLKVIE LISTLGIVFY VFLTGTKAHF YDVALIRGGS KYRGTGRGFS ITRDPMVNFF
KEYAVSHFRK AVELIGIMIL FGIYGTFDIG SGALEDFCAT AEFDCEKDPD LIPANITSLA
GFSNHPQSYG IASFAVLFLG ACWLMAPFVF NTDGLVFQKS KVDIANWFAW MMQSHQKEDA
NNQEADKQTS SGPKDGWDDW WKSDVDLMLP LGGMGRLTYC IRELRHPLAM YYVFMTEFEL
VWFALLFTAI GVTWVLLWFG NRVHHCVSKH RKLSSLTVQG IMYMVCVIGG ILLIPLIGSV
GGWSVQKCLT FSIAMFLGFN SIVQYALAFN GVFGMEVAMW SPVMALGFLM DMIVGLFLVI
PLFLLSVLPF MRILQTRAMY NGGFSRALSS GSEVAASLCI LLGLLGGFIH GFMTSFLYTL
GYINDPNDKF MNRSFYYFVT TELSNKGSGM LSYMENGYLK IICAAVSIFA VLLSLLIGRV
LGRRANMAIG GSLMFISLGL NFIASMSVII VSCGLAAMGS SMVAMNYLLY SFEICTKGWH
GKSVTIFLMG SMIGWFVHSL LMANTNATSI AEDYDNKPTN MWRFQPLFVL PALIIGFFGI
LRFVPESPVW LLAHKHEELA RAVLIRLRRR VNVNPEIVLI QAELAQKTRA NHLKFRLSIV
FALQAVFGLV MSQTILLRRT LKVTASNSGN ANNYWEVYFA LCCATGYAFG SFLVDNVRRK
TILKEFLPFV SLMAFTCGVV GAVSRADGGF VQALLCLLYI SASLSLMSVT WLSALEMFPA
SRRPLYWTLS LCVYYAVQII VYWLNPGFSL SSFILSGCCA VLTFVLFMFC ASTKLGAIQT
KAEKKYQRSM RESAPEKALV TDEDEFVVDE MHKQQTRIAQ TSAAMNRSAG MASTNPASSA
VNVKFGPSGV SNRNFGPPPN SAASNAMANA MQFGFSGINI AQSGDSARPG PTSRSDKDNF
SFRRLGSLEE LSPAGGGLQY GLSTGLSGVE SSKASSAEWQ VAEPVARPGQ LTSHLSSTFD
FEAEFEAEHL EDLRQGQISY PRNQPRSISF LQSQQYPDAD LHAETQSVRL
//
