ID A0A423XHH9_9PEZI Unreviewed; 1940 AA.
AC A0A423XHH9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 28-JUN-2023, 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=VPNG_02085 {ECO:0000313|EMBL:ROW15775.1};
OS Cytospora leucostoma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Cytospora.
OX NCBI_TaxID=1230097 {ECO:0000313|EMBL:ROW15775.1, ECO:0000313|Proteomes:UP000285146};
RN [1] {ECO:0000313|EMBL:ROW15775.1, ECO:0000313|Proteomes:UP000285146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYLt {ECO:0000313|EMBL:ROW15775.1,
RC ECO:0000313|Proteomes:UP000285146};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) 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:ROW15775.1}.
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DR EMBL; LKEB01000008; ROW15775.1; -; Genomic_DNA.
DR STRING; 1230097.A0A423XHH9; -.
DR InParanoid; A0A423XHH9; -.
DR Proteomes; UP000285146; 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:UP000285146};
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 483..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..589
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 720..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1344..1363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1396..1417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1487..1507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1513..1531
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1603..1624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1650..1677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1689..1715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1727..1746
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1788..1809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1846..1870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 337..449
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1940 AA; 220629 MW; 529370EA5AD8F2E9 CRC64;
MSGYPGHQDV DDGYGHQQGN TDSYYDNEHG QYYDNAHAAA DPHGAHAGQE GYYDESGYYN
ADPNNPHHQD GGYYEGQEQY QDGYYENGYY DQQPGFDQAG YAGQRPGNSE EDSETFSDFT
MRSDMARAAD MDYYGRGDER YSGYQDGNGA RGYRPPSSQI SYGGNRSSGA STPNYGMDYG
NVLPAGQRSR EPYPAWTSDA QIPLSKEEIE DIFVDLCNKF GFQRDSMRNM YDHLMTLLDS
RASRMTPNQA LLSLHADYIG GDNANYRKWY FAAHLDLDDA VGFANAKGSK SNKKKAKKKK
SKGDEPEEQT LEDLEGDTSL EAAEFRWKTR MNRMSQHDRL RQIALYLLCW GEANQVRFMP
ECLCFLFKCA DDYLSSPACQ NLVEPVPELT FLNNVITPLY QYCRDQGYEI SNGVYVRRER
DHNKIIGYDD CNQLFWYPEG IERIVLEDKT RLVDIPPAER YLKLQDVAWK KCFFKTYRET
RSWFHLLVNF NRIWIIHLTV FWMYTTHNAP SLLVPNYEQQ VNQSPPRSAQ WSIVGFGGGI
ASIIQILATL AEWAYVPRRW SGAQHLTKRL FFLIFVFIIN VAPGIYVFLP QASISEYIAH
QNTQACLALG IVQFFIALIT LLFFSVMPLG ALFGSYLTSK NSRRYVASQT FTASWPSLKG
NDMAMSYGLW VVIFGAKMGE SYGFLTLSFR DPVRYLSIMD VSSCLGDQII GRKLCQYQPM
ILLALMAITD MVFFFLDTYL FYVLLNAVVS IARSFYLGSS IWTPWRNIFS RLPKRIYSKV
LATTDMEIKY KPKVLISQIW NAIVISMYRE HLLAIDHVQK LLYHQVPSEQ EGKRTLRAPT
FFVSQEDHSF KTEFFPSQSE AERRISFFAQ SLSTPIPEPL PVDNMPTFTV LIPHYSEKIL
LSLREIIRED EPYSRVTLLE YLKQLHPHEW DCFVKDTKIL SDETAQYNGD EEKPDKDTAK
SKIDDLPFYC IGFKSSAPEY TLRTRIWASL RFQTLYRTIS GFMNYSRAIK LLYRVENPEV
VQMFGGNSDK LERELERMAR RKFKICVSMQ RYAKFKKEEM ENAEFLLRAY PDLQIAYLDE
EPPANEGEEP RLYSALIDGH SELMENGMRK PKFRIQLSGN PILGDGKSDN QNHSIIFYRG
EYIQLIDANQ DNYLEECLKI RSVLAEFEEM KTPSASPYTP GVKNEVHTPV AILGAREYIF
SENIGILGDV AAGKEQTFGT LFARTLAQIG GKLHYGHPDF LNGIYMTTRG GVSKAQKGLH
LNEDIYAGMN AVLRGGRIKH CEYYQCGKGR DLGFGSILNF TTKIGTGMGE QMLSREYYYL
GTQLPLDRFL SFYYAHPGFH VNNMFIMLSV HLFILCCVNL GALRHETIAC NYNRNVPITD
PLMPSGCQNT DALMDWVYRC VISIIFVIFL AFVPLCVQEL TERGVLRAST RLAKQICSLS
PFFEVFVCQI YANAVQNNLS YGGARYIGTG RGFATARIPF GILYSRFASP SIYFGARMLL
MLLFATLTIW QAALVYFWMS LLALCISPFL YNPHQFSWND FFIDYREFLR WLSRGNSVSH
ASSWISYCRL SRTRLTGYKR KLVGEPSGKL SADVPRAPIS NVFFTEVIAP LLLCVVTLIP
YLFINAQTGV HNTNPDLKDN DSDAVATNSL IRVAIVAFAP IGVNAGVCAM FFAMACCMGP
LFSMCCKKFG SVLAAIAHAV AVIILFVFFE VMYVLEGFNF TRTLSGMIAV VAVQRFILKL
IITFGLTREM KTDQANIAFW TGKWYSMGWG TLSQPAREWL CKMTELSFFA GDFILGHALL
FIMCPVILIP QVDKLHSIML FWLRPSRQIR PPIYSLKQSK LRRKRVFRYA VLYFVLLIIF
LVLFVAPSLA GKYVPTSMLD MLSSLHLVQP TGQNNNDTVS SQTGTGAKDY SGALQTMTSG
SGTGTAAASS TGDSAKIRLF
//
