ID W9CNE9_SCLBF Unreviewed; 1942 AA.
AC W9CNE9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 03-MAY-2023, entry version 28.
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=SBOR_3459 {ECO:0000313|EMBL:ESZ96184.1};
OS Sclerotinia borealis (strain F-4128).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ96184.1, ECO:0000313|Proteomes:UP000019487};
RN [1] {ECO:0000313|EMBL:ESZ96184.1, ECO:0000313|Proteomes:UP000019487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT pathogenic fungus.";
RL Genome Announc. 2:E0117513-E0117513(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:ESZ96184.1}.
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DR EMBL; AYSA01000149; ESZ96184.1; -; Genomic_DNA.
DR STRING; 1432307.W9CNE9; -.
DR HOGENOM; CLU_000844_0_1_1; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000019487; 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:UP000019487};
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 506..529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 550..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 593..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..643
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1359..1378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1411..1432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1528..1546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1614..1640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1660..1688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1700..1725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1731..1749
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1797..1820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1857..1881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 360..472
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1942 AA; 220967 MW; 2116512E04C03351 CRC64;
MSGHPQPAGQ YDEGYDHQPG NTDSYYQDEH GGQQYYDNNG GYEQGHGAQP PQQQHQGGEG
YYDESGYYNA DANNPYQQEG GYYEGGEHPQ GQGQGQYQDE YYNDQYYDQG AAAGGEAPPG
KRRGDSEEDS ETFSDFTMRS DMARATDMDY YGRGDERYNS YNESQMGGRG YRPPSSQVSY
GGNRSSGAST PNYGMDYNNV LPAGQRSKEP YPAWTSDAQI PLSKEEVEDI FLDLTAKFGF
QRDSMRNMYD HLMTLLDSRA SRMTPNQALL SLHADYIGGD NANYRKWYFA AHLDLDDAVG
FANMKLGKGD RRTRKARKAA KAAAADPQNE AQTLEQMEGD NSLEAAEYRW KTRMNRMSQH
DRVRQLALYL LCWGEANQVR FMPELLCFIF KCADDYLNSP ACQNLVEPVE EFTYLNQIIT
PLYQYCRDQG YEIQDGKYVR RERDHNEIIG YDDCNQLFWY PEGIERIIME DKSRLVDVGP
AERYLKLKDV NWNKVFFKTY RETRSWFHML VNFNRIWVIH ISAFWFFTAK NSPTLLEKHY
EQQKNNQPPA SAQWSAVALG GAVASLIMVV ATICEWSYVP RRWAGAQHLT KKLLFLLAVL
AINVAPSVYI FIIPDTQHTK IALILGIVQF FIALVTYFFF SIMPMGGLFG SYLTRNSRQY
VASQTFTASY PRLTGNDMWM SYGLWITVFG AKLAESYVFL TLSFRDPIRY LDSMQISTCV
GDAIIGDVLC KLQPKILLGL MFVTDLTLFF LDTFMWYIIM NTIYSVARSF YLGVSIWTPW
RNIFSRLPKR IYSKVLATTD MEIKYKPKVL ISQIWNAIVI SMYREHLLAI DHVQKLLYHQ
VPSEQEGKRT LRAPTFFVSQ EDHSFKTEFF PNQSEAERRI SFFAQSLSTP IPEPLPVDNM
PTFTVMIPHY GEKILFSLRE IIREDEPYSR VTMLEYLKQL HPHEWDCFVK DTKILADETS
QFNGDYDKEE KNTAKSKIDD LPFYCIGFKS AAPEYTLRTR IWASLRAQTL YRTISGFMNY
SRAIKLLYRV ENPEVVQMFG GNSDKLEREL ERMARRKFKL CVSMQRYAKF KKEEMENTEF
LLRAYPDLQI AYLDEEAPLV EGDEPRLYSA LIDGHSEVME NGMRRPKFRI QLSGNPILGD
GKSDNQNHAI IFYRGEYIQL IDANQDNYLE ECLKIRSVLA EFEEMTTENV SPYTPGVSNP
KIAPVAILGA REYIFSENIG ILGDVAAGKE QTFGTLFART LAAIGGKLHY GHPDFLNGIF
MTTRGGVSKA QKGLHLNEDI YAGMTALLRG GRIKHCEYYQ CGKGRDLGFG SILNFTTKIG
TGMGEQMLSR EYYYLGTQLP IDRFLSFYYA HPGFHLNNMF IMLSVNLFMI CLINLGALRN
QVIECTYNTN VPITDPLYPT GCANIVPITN WVYRCVISIF IVFFISFVPL TVQELTERGF
WRAATRLGKQ FCSLSPFFEV FVCQIYANAV QQDLSFGGAR YIGTGRGFAT ARIPFGILFS
RFAGPSIYLG ARLLMMLLFA TITVWQAALV YFWVTLLALC ISPFLYNPHQ FAWNDFFIDY
RDYLRWLSRG NSRSHASSWI AFCRLSRTRI TGYKRKILGD PSAKMSGDTA RATFSNLFFG
EIVGPLMIVA LTLIPYLFIN SQTGVTAELN DGVAPVATNA LIRVGIVALA PIAVNAGVLA
GMFGMACCMG PVLGMCCKKF GSVLAAIAHA IAVVMCLVFF EVMFFLEGFN LAKALLGMIA
SAAIQRFVYK LIISLTLTRE LKTDTSNIAF WTGKWYSMGW HSVSQPGREF LCKITELGMF
AGDFVLGHLI LFIMLPIIAI PQVDKLHSVM LFWLRPSRQI RPPIYSLKQS KLRKRRVWRY
AIIYFVLFII FLALLIGPLI AGKKILTKSL TDKIPLKLYQ PTGQNNNDTQ GYNQTGTGCT
TCTGVSATSS ASSTAAARVR LF
//
