ID A0A5N6F6Q6_9EURO Unreviewed; 1898 AA.
AC A0A5N6F6Q6;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 02-APR-2025, entry version 14.
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=BDV33DRAFT_145369 {ECO:0000313|EMBL:KAB8224733.1};
OS Aspergillus novoparasiticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=986946 {ECO:0000313|EMBL:KAB8224733.1, ECO:0000313|Proteomes:UP000326799};
RN [1] {ECO:0000313|EMBL:KAB8224733.1, ECO:0000313|Proteomes:UP000326799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 126849 {ECO:0000313|EMBL:KAB8224733.1,
RC ECO:0000313|Proteomes:UP000326799};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Petersen T.I., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Pangilinan J., Riley R., Salamov A., Simmons B.A., Magnuson J.K.,
RA Henrissat B., Mortensen U.H., Larsen T.O., De vries R.P., Grigoriev I.V.,
RA Machida M., Baker S.E., Andersen M.R.;
RT "Fungal friends and foes A comparative genomics study of 23 Aspergillus
RT species from section Flavi.";
RL Submitted (APR-2019) 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) + UDP + H(+); 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:ARBA00047777};
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; ML733398; KAB8224733.1; -; Genomic_DNA.
DR Proteomes; UP000326799; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
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 GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IEA:TreeGrafter.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR056261; FKS1-like_dom2.
DR InterPro; IPR003440; Glyco_trans_48_dom.
DR PANTHER; PTHR12741:SF48; 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; PF23605; FKS1_dom2; 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:UP000326799};
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 484..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 523..544
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1327..1349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1382..1402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1473..1490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1496..1517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1588..1610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1630..1654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1666..1690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1696..1715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1763..1789
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1827..1847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 331..443
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..67
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..292
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1898 AA; 217904 MW; C7F7DDD0A4B5646C CRC64;
MSGYNQGGHY DDGYGQHGAH GDSYYQDEHH GQAYYDPNDY GDGYYDRGGY YPEGGQGYHQ
DGGYYDAGHQ DDYYGEPYYD QGNGQQRGRR RGDSEEDSET FSDFTMRSET ARAADMDYYG
RGDERYNSYA DSQYGGRGYG YRPPSSQVSY GGNRSSGAST PVYGMDYGNA LPAGQRSREP
YPAWSSDAQV PVSKEEIEDI FLDLVNKFGF QRDSMRNMYD HLLTQLDSRA SRMTPNQALL
SLHADYIGGD NANYRRWYFA AHLDLDDAVG FSNMKLGKAD RKTRKARKAA QKKAKENPEN
VEETLEALEG DNSLEAAEYR WKTRMNRMSQ HDRVRQVALY LLCWGEANQV RFLPECLCFI
FKCADDYYSS PECQNRVEPV EEFTYLNEII TPLYQYCREQ GYEISDGKYV RREKDHNQII
GYDDMNQLFW YPEGIERIVL EDKTRLVDIP TAERWMKLKE VNWKKVFFKT YRETRSWFHM
VTNFNRIWVI HLCSFWFFTA YNAPTLYTKN YQQQLNNKPP GSYYWSAVGF GGALACFIQI
FATICEWMYV PRRWAGAQHL TKRLMFLLLM FIINLAPGVV VFGFKKQIGE TIALIIGIVH
FIIALVTFFF FSVMPLGGLF GSYLKKHGRQ YVASQTFTAS WAHLQGNDMW MSYGLWVCVF
GAKLAESYFF LTLSFKDPIR ILSPMQIQRC SGVEYLGTKL CYIQPQILLG LMFFMDLTLF
FLDSYLWYII CNTVFSVARS FYLGVSIWSP WRNIFSRLPK RIYSKVLATT DMEIKYKPKV
LISQVWNAII ISMYREHLLA IDHVQKLLYH QVPSEQEGKR TLRAPTFFVS QEDQSFKTEF
FPPGSEAERR ISFFAQSLST PMPEPLPVDN MPTFTVLIPH YSEKILLSLR EIIREDEPYS
RVTLLEYLKQ LHPHEWDCFV KDTKILADET SQFNGETEKT EKDVAKSKID DLPFYCIGFK
SAAPEYTLRT RIWSSLRSQT LYRTISGFMN YSRAIKLLYR VENPEVVQMF GGNSEKLERE
LERMARRKFK ICVSMQRYAK FNKEERENTE FLLRAYPDLQ IAYLDEEAPE NEGDEPRLYS
SLIDGHCELL ENGMRKPKFR IQLSGNPILG DGKSDNQNHA IIFYRGEYIQ VIDANQDNYL
EECLKIRSVL AEFEELTTDN VSPYTPGLPS SDTHPVAILG AREYIFSESV GVLGDVAASK
EQTFGTLFAR TLAEVGGKLH YGHPDFLNGI FMCTRGGISK AQKGLHLNED IYAGMNAMVR
GGRIKHCEYF QCGKGRDLGF GSILNFTTKI GTGMGEQMLS REYYYLGTQL PLDRFLSFYY
AHPGFHLNNM FIMLSVQMFM IVLINLGALK HETITCRYNK DLPITDPLRP TFCANLVPII
DWVNRCVISI FIVFFISFVP LAVQELTERG VWRMATRLAK HFGSFSFMFE VFVCQIYANA
VHQNLSFGGA RYIGTGRGFA TARIPFGVLY SRFAGPSIYA GARLLLMLLF STSTVWSAAL
IWFWVSLLAL CISPFLFNPH QFAWHDFFID YRDYLRWLSR GNSRSHASSW IAFCRLSRTR
ITGYKRKLLG VPSEKGSGDV PRARITNIFF SEIVAPLVLV GVTLIPYLFI NSRTGTMEKD
RDPKNAIARI AIVAFGPIAI NAGVAGMFFG MACCMGPIFS MCCKKFGAVL AAIAHAIAVI
ILLVIFEVMF FLEGWSWPRC VLGMISAAAI QRFVYKLIIS LALTREFKHD QSNIAWWTGK
WYSMGWHSLS QPGREFLCKI TELGYFAADF VLGHLLLFIM LPALCVPYID KFHSVILFWL
RPSRQIRPPI YSLKQSKLRK RRVVRFAILY FAMLVLFLVL LIAPLVVRKM NISLPNIPMN
LLQPLDEKHN NTISQYTGNG LPGGSSGIPA SVLASATY
//
