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Database: UniProt
Entry: A0A329SQZ8_9STRA
LinkDB: A0A329SQZ8_9STRA
Original site: A0A329SQZ8_9STRA 
ID   A0A329SQZ8_9STRA        Unreviewed;      2043 AA.
AC   A0A329SQZ8;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE            EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
GN   ORFNames=PC110_g5744 {ECO:0000313|EMBL:RAW38022.1};
OS   Phytophthora cactorum.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=29920 {ECO:0000313|EMBL:RAW38022.1, ECO:0000313|Proteomes:UP000251314};
RN   [1] {ECO:0000313|EMBL:RAW38022.1, ECO:0000313|Proteomes:UP000251314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10300 {ECO:0000313|EMBL:RAW38022.1,
RC   ECO:0000313|Proteomes:UP000251314};
RA   Armitage A.D., Lysoe E., Nellist C.F., Harrison R.J., Brurberg M.B.;
RT   "Draft genome of the strawberry crown rot pathogen Phytophthora cactorum.";
RL   Submitted (JAN-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:RAW38022.1}.
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DR   EMBL; MJFZ01000098; RAW38022.1; -; Genomic_DNA.
DR   STRING; 29920.A0A329SQZ8; -.
DR   Proteomes; UP000251314; 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:UP000251314};
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        699..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        724..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1558..1580
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1611..1629
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1636..1654
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1700..1719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1842..1860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1875..1896
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1916..1933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1939..1958
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1978..1996
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          249..352
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
FT   REGION          183..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..856
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2043 AA;  233543 MW;  E146EDD7B8015B71 CRC64;
     MNRRGHGNGN GNGSEREGSS VGLMTEALEM QRQMCDEAMS LVNAGVAMQN ASPPNVAEAE
     RKLTRAVDIM EQALSIRYRS ADEKDAADRL NNKMMRYVKM IKSQRAKSVV GGGPKGRNLI
     KHNILEMERL PEVYTPVLQL LNNSNQLGDI CESLKRTFGF QESSVLNQKE HLLLLLTNFK
     EQSGQDDGKK KKKKKKQDDT ETIDDYLRQR DPQLEMDLAN KGITRLHGRV FANYKKWCKY
     VSQKPKFSSD LLVDITLFFL IWGEAANFRQ MPECLCFLLH TMLPKVNSGG NEEPGTFLAN
     TIRPMYAELR RDSDKKTSKG ARAPHREIRN YDDFNEFFWT KKSLKYDYTN IGEAFANYDK
     KGRPKIVKKT FSETRSWTRA IISFRRIFLM NCALFLATLG FSIDMVLLCP DSAIMYGEDV
     QPSSETGVLE ILGKKYAATT GSSSVVNTDD SLSDDINTDS GAGSQCLYAK LATCLGVQYF
     TSASDTFGTL PQDFKELLEL VPFTDCVEKT VGRCKCYHDF IDDCFNDSGK ADEVSTEGSV
     ASITYDQSVC APAWMAQVNS ILDDEGDGLL NCGSCQIDIT SLAKKPTRIM DMLQGLIDFG
     RNDKGPMALL GGAAMIGLVC VCELQNRFFS GIGMGFVGRS MPVPMKTYCR YTCFWIVLYL
     VKLTFDYQFV VKTLVETTLF VYSAKSTDYL QYSHFMLQIT YHNIVYILFL WVPAWMVFLY
     DAQIFYSVLS VIYGSFAGFN LRIGELRSFR ILRLTFKSIP GVFNRKLVPN IVEEKAKKKK
     KKNKKNKNDK DEMAMPLRRF ERISMSQGAK PLTVKTQKYS SLLEQRDDDD VYSEMKTPNG
     TDEDMSSQSS RSSNIGSITG VSGAEFERTI PFAMAWNRCL TSLREADVIS DRELNVLSYL
     IDSKDTVGRK LYPPAFLTAG KLDESIDIVL ECSALYEKLK TDKKKKDKVL QKIETTMRER
     LTKDDLRVES ILGSYKFSSQ VLRILLGEEH KELDDCYNFI EEMASHQQIL KGLKLDNLYL
     CRAAAAELMK SILEVPKKST ETSIKFQRAL YKVIDSVESV INCLKMVLAK QENLVQMLND
     TPLKPNSFFF PGDSQHYASL QLQKIVNDEA ALDIVSRAYQ LLTVDNFDAE PRSEEGRRRL
     RFFANSLFMD MPEAKPIRKI RSLTVSTPYY NEIVMYSIKD LTAQNDDCIK LLYYLQTIYP
     FEWENLLERI QAKDMNEALK KNPEEVQLWA SYRGQTLART VRGMMYNAEA IRFLHWLEIG
     ENEPMHQVTC SCNKCCKLNE MVALKFNYVC TCQIYGKQKD EQKQQAQDID FLLRKHLNLR
     VAYVDGPKKV KDGPPKFFSV LIRSQDEKIV EIYRVELPGN PIVGEGKPEN QNHAIIFSRG
     ELLQCIDMNQ DGYLEEALKM PNLLSTMDRG TEKRPLTIIG FREHVFTGGV SNLASFMSIQ
     ELSFVSLGQR MLAINHVRQH YGHPDIFDKL FAMGCGGTAK ASKGVNLSED IFAGFNSTLR
     GGRVSHEEFI QVGKGRDVGM QQLALFEAKL SSGAGECVIS RDAMRMASRL DFFRLHSWFY
     GNLGWYFTQT MTVVGVYFFI YGKVYMALSG MDSFFLEKGG LGIGGTLNTS WAFQFGFLLV
     VPVVAVVGVE QGFRHGVTYL IWNIMTLGPL FFTFQMGTRM HYFDRTLIHG GAKYRATGRG
     FTIKHEKFAE LFRFYAFSHF YRGVELLFLL LMFYAYGTFS WCNCSWRLDA DFYNNVEPTD
     LEWRTRCYDD HYQSCVLPTN QNYGIMSYSL WIIAATWMWA PFFFNPSGLD WDKIIEDYND
     WQNWLKTTND SADSWFGWWS NEQEYLEHTT RGARFVAGIR KLRFLLVAIG MYLNMMYNAY
     FERPNRVITS DDDMLTYALS GLVVVIFVLL ICCGYIASRV TKKMSMKQRK LRKMKFLLSC
     CCFLISMLSL TVLSVGNLFA IFILLFVAVY WFMQMCILRL QYHHIVVRAL ARAYDRAVGW
     IVFGPIMIVS MFLPFISSFQ QRVMFNNAFT SGLEVSKLFA HDVAPAQVVK VKRVSKKKKN
     RDD
//
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