ID A0A0A2IL28_PENEN Unreviewed; 1950 AA.
AC A0A0A2IL28;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 08-NOV-2023, entry version 36.
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=PEX2_104620 {ECO:0000313|EMBL:KGO49829.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO49829.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO49829.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO49829.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(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:KGO49829.1}.
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DR EMBL; JQFZ01000372; KGO49829.1; -; Genomic_DNA.
DR RefSeq; XP_016593218.1; XM_016747731.1.
DR SMR; A0A0A2IL28; -.
DR STRING; 27334.A0A0A2IL28; -.
DR GeneID; 27683152; -.
DR HOGENOM; CLU_000844_0_1_1; -.
DR OrthoDB; 354539at2759; -.
DR PhylomeDB; A0A0A2IL28; -.
DR Proteomes; UP000030143; 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:UP000030143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGO49829.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 515..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..573
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 594..613
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 625..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..709
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1364..1383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1416..1440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1507..1526
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1533..1551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1622..1644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1664..1694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1700..1726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1738..1757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1809..1834
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1857..1881
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 359..471
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1950 AA; 221417 MW; C3941DCDC254BA4B CRC64;
MSGYAGGGHY DDGYAQQGQA QGQAHGDSYY QDEHSQGYYD NQGYGDGYYD QGNGYYGAED
GHGADAAHAD GAQHADAGHG YADGGYYEAG HQDQYYGGAA GAGGDQYYDQ GQGQPRGRRG
NDSEEDSETF SDFTMKSETA RAADMDYYGR GDERYNSYSD SQYGGAGGYR PPSSQVSYGG
NRSSGASTPV YGMEYGNALP AGQRSREPYP AWTSDAQIPL SKEELEDIFL DLVNKFGFQR
DSMRNMYDHM MTMLDSRASR MTPNQALLSV HADYIGGHNA NYRRWYFAAH LDLDDAVGFA
NMKLGKGDRK TRKARRAAAK AAKQNPENEE ETLEALEGDT SLEAAEYRWK SRMNRMSQHD
RARQIALYLL VWGEANQVRF MPEIICFIFK CADDYYTSPE CQARVEPVEE LTYLNEIITP
LYHYCRDQGY EIMDGKFVRR EVDHNKIVGY DDMNQLFWYP EGIERIGFED KTRLVDIPIA
ERWPKLKDVV WKKAFFKTYK ETRSWFHMIT NFNRIWVIHL GAFWFFTAYN APTLYTINYQ
QQVDNKPDSP KYLAAVGFGG ALVSFIQILA TIFEWMYVPR RWAGAQHLRK RFMFLLVVFI
INLAPGIVIF SILPSLTMSE STKHGIGLAL GIVHFVLAVL TAAFFAIQPL GALFGNYMKK
GGRQYVASQT FTASFPRLSG NDMWMSYGLW VCVFGAKLAE SYFFLTLSLK DPIRILSPMQ
IHQCTGAKYI GNVLCHRQPQ ILLGLMGFMD LTLFFLDSYL WYIICNTIFS VARSFYLGVS
IWSPWRNIFS RLPKRIYSKV LATTDMEIKY KPKVLISQVW NAIIISMYRE HLLAIDHVQK
LLYHQVPSEQ EGKRTLRAPT FFVSQEDQSF KTEFFPQGSE AERRISFFAQ SLATPMPEPL
PVDNMPTFTV LIPHYSEKIL LSLREIIRED EPYSRVTLLE YLKQLHPHEW DCFVKDTKIL
ADETSQFNGD YEKPEKDAAK SKVDDLPFYC IGFKSAAPEY TLRTRIWASL RSQTLYRTVS
GFMNYSRAIK LLYRVENPEV VQMFGGNSEK LERELERMAR RKFRICVSMQ RYAKFNKDER
ENTEFLLRAY PDLQIAYLDE EPPVNEGDEP RIYSALIDGH CELLENNLRK PKFRIQLSGN
PILGDGKSDN QNHSIIFYRG EYIQLIDANQ DNYLEECLKI RSVLAEFEEL TTDNVSPYTP
GVASPEHDPV AILGAREYIF SESVGVLGDV AASKEQTFGT LFARTLAQIG GKLHYGHPDF
LNGTFMTTRG GVSKAQKGLH LNEDIYIGMN ALLRGGRIKH CEYYQCGKGR DLGFGSILNF
TTKIGTGMGE QMLSREYYYL GTQLPLDRFL SFYYAHPGFH LNNMFIMLSV QMFMFVLINL
GALKHETIMC HYNSDLPITD PLTPTLCANL VPILNWVNRC VISIFIVFFI SFVPLAVQEL
TERGVWRMAT RLAKHFGSFS FMFEVFVCQI YANAVHQNLS FGGARYIGTG RGFATARIPF
GVLYSRFAGP SIYLGARLLL MLLFSTTTVW SPALIWFWVS LLALCISPFL FNPHQFAWND
FFIDYRDYIR WLSRGNSRSH ASSWIGFCRL SRTRITGYKR KVLGVPSEKG SGDIPRAPIT
NIFFSEIVSP LLGVAVTLIP YLYINSRTMY SDDVKWAANP ILRVAIVGLA PVGVNAGVAG
MFFGMACCMG PLFGMCCKKF GAVLAAIAHA IAVIVFLLLF LAMFFLESLS WARTISGMIA
AMALQRFIYK LIISLALTRE FKNDQSNIAW WTGKWYNMGW HTLSQPGREF LCKITELGYF
ANDFFLGHIL LFAMLPVLAM PYADTFHSVI LFWLRPSSQI RPPIYTLKQS KLRKRRVVRF
AILYFTMLLI FIVIVAAPVV LRNTNQLDSI LSGGIWKSLG VASTTGIGLL QPLDRGLNDT
VSWYTGSNIP KGYTSGTIPA ASEGTGVWSI
//
