ID A0A0H1BFH2_9EURO Unreviewed; 1904 AA.
AC A0A0H1BFH2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 03-MAY-2023, entry version 27.
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=EMPG_14357 {ECO:0000313|EMBL:KLJ10244.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ10244.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KLJ10244.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDEV01002115; KLJ10244.1; -; Genomic_DNA.
DR STRING; 2060906.A0A0H1BFH2; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000053573; 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:UP000053573};
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 479..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..620
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 653..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1384..1405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1501..1519
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1590..1612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1632..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 1823..1847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 333..445
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 135..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1904 AA; 217522 MW; 0D52F3AF9006D506 CRC64;
MSAQPQGGGG AHNGYGDGYA QNTQGDSYYQ DGYYEQNDYS QHEGYHDNQG YGDQYQQDGY
YDNQQGYDDE YYNDQYYDQG TAGYHNGAQP GRRRGHDSEE DSETFSDFTM KSETARAADM
DYYGRGDERY NSYNEHQMGG RGYRPPSSQI SYGANRSSGA STPVYGLDYG NALPAGQRSR
EPYPAWTSDA QIPISKEEIE DIFLDLVNKF GFQRDSMRNM YDHFMTLLDS RASRLTPNQA
LLSLHADYIG GDNANYRRWY FAAHLDLDDA VGFANMKLGK ANRKTRKARK AAKKAAGNDP
KNEEETLADM EGDNSLEAAE YRWKTRMNRM SQHERARQIA LYLLCWGEAN QVRFMPEALC
FIFKCADDYY HSPECQNRVE PVEEFTYLND IITPLYQYCR DQGYEIFDGK YVRREKDHNK
IIGYDDINQL FWYPEGIERI VMNDKSRIVD IPPAQRYQQL KDVNWKKVFF KTYKETRSWF
HMMVNFNRIW VIHVGAFWFY TAFNAPTLYT RDYKQLENNP PTAASRWAAT GLGGAVATFI
MIFATICEWC YVPRAWAGAQ HLTKRLIFLL GIFCINIGPA VFVFGVTQDH KASHVLGVVS
FFVNLATFFF FSVMPIGGLF GSYMKKNSRQ YVASQTFTAS YPRLRGNDMW MSYGLWICVF
GLKLAESYFF LTLSFRDPIR ILSQMQIKQC AGEKLFGASA NVLCKEQPRI LLGLMFFTDL
SLFFLDTYLC YVILNAVFSV ARSFYLGVSI WTPWRNIFSR LPKRIYSKVL ATTDMEIKYK
PKVLISQVWN AIVISMYREH LLAIDHVQKL LYHQVPSEQE GKRTLRAPTF FVSQEDHSFK
TEFFPSQSEA ERRISFFAQS LSTPIPEPVP VDNMPTFTVL IPHYSEKILL SLREIIREDE
PYSRVTLLEY LKQLHPHEWD CFVKDTKILA DETSQFNGDE KSEKDAAKTK IDDLPFYCIG
FKSAAPEYTL RTRIWASLRS QTLYRTISGF MNYSRAIKLL YRVENPEVVQ MFGGNSEKLE
RELERMARRK FRIVVSMQRF AKFNKEEREN TEFLLRAYPD LQIAYLDEEP PANEGEEPRL
YSALIDGHSE IMENGLRRPK FRIQLSGNPI LGDGKSDNQN HAIIFYRGEY IQLIDANQDN
YLEECLKIRS VLAEFEEMNP ENVSPYVPGL PPAKTNPVAI LGAREYIFSE NIGILGDVAA
GKEQTFGTLF ARTLAQIGGK LHYGHPDFLN GIFMTTRGGV SKAQKGLHLN EDIYAGMNAL
LRGGRIKHCE YYQCGKGRDL GFGSVLNFTT KIGTGMGEQM LSREYYYLGT QLPLDRFLSF
YYAHPGFHIN NIFIMFSVQM FMICLTNLGA LRNQTIPCIV TKGVPITDRL LPTGCSDTDP
IQAWVNRCIA SICIVFLLSF FPLIVQELTE RGAWRAVTRL AKHFGSLSPF FEVFVCQIYA
NSLHNNLSFG GARYIGTGRG FATARIPFGV LYSRFAGPSI YLGARLLMML LFSTLTVWSG
WLLYFWASLL ALCISPFLFN PHQFAWNDFF IDYRDYLRWL SRGNSRSHAS SWIAFCRLSR
TRITGYKRKV LGTPSEKLSG DAPRAQLTNI FFSEIVGPLV FVAVTLIPYL FINAQTGVPD
AKPTSSLIRL AIVAFAPIAI NAGCLAVLFG MACCMGPLLS MCCKKFGSVL AAIAHGVAVV
MLLAFFEVMF FLEGWVFAKA LLGMITVVAI QRFFYKLIIS LALTREFRQD TSNVAWWTGK
WYSMGWHSMS QPGREFLCKI TELGMFAADF ILGHVLLFFM LPPLCIPYVD KGHSVMLFWL
RPSRQIRPPI YSLKQSKLRK RRVIRFAILY FFMLVIFLGL IVGPVVAGPR IGEIALPGLI
NDLSLLQPTG QDINDTTTSL TGKALNDPEP KSTGSSNDRM ARLF
//