ID A0A139GZE9_9PEZI Unreviewed; 1928 AA.
AC A0A139GZE9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 03-MAY-2023, entry version 19.
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=AC578_3255 {ECO:0000313|EMBL:KXS95583.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXS95583.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXS95583.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXS95583.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-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:KXS95583.1}.
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DR EMBL; LFZN01000209; KXS95583.1; -; Genomic_DNA.
DR STRING; 321146.A0A139GZE9; -.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000070133; 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:UP000070133};
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 491..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 536..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 665..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 708..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1342..1361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1394..1415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1511..1529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1601..1624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1644..1671
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1683..1705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1717..1740
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1777..1796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1840..1864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 345..457
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1928 AA; 220908 MW; 613867BCEA70AD41 CRC64;
MAHPHQGAGY DDGYGHQGAH DGYYQDDQAY YDQHAYGHQA QHDGYYDDNG YYQAGAHDGY
QHDGYYDAGQ QGYQDEYYND QYYDQGAPAA GQYQQQGRGQ AQRRSGRRGH DSEEDSETFS
DFTMRSDMAR AAEMDYYGRG DERYNSYGDG TGRGYRPPSS QVSYGGNRSS GASTPVYGMD
YTSALPAGQR SREPYPAWTS DAQIPLSKEE IEDIFLDLTA KFGFQRDSMR NMFDHVMTLL
DSRASRMSPN QALLSLHADY IGGENANFRR WYFAAHLDLD DAVGFANMKL GKANRATRKA
RKAAKKKAEA NPQNEEATLE SLEGDNSLEA AEYRWKTRMN RMSQHDRVRQ IALYLLCWGE
ANQVRYMPEV LAFIFKCADD YYHSPACQNR VEPVEEFTYL NNCITPLYNY CRDQGYEIFE
GKYVRKELDH QKIIGYDDMN QLFWYPEGIE RLSFEDKTRL VDLPPAERYE RLKDVVWKKA
FFKTYKETRS WFHMLTNFNR IWIIHVCIFW FYTAFNSPTL YTKNYQQQLN NQPKGSAHWS
AVALGGTLGC LIQIMATLTE WLYVPRRWAG AQHLTKRLLV LIVMFVINIG PSVYIFGVSQ
DGKIALILGV VQFLIALATV FFFAIMPLGG LFGSYLNGKR RQYVASQTFT ASYPRLTGND
MWMSFGLWVL VFAAKLAESY FFLTLSLRDP IRILSTMKIQ HCLGDKMIGT ILCYQQPTVL
LILMYFTDLI LFFLDTYLWY VIWNCVFSVA RSFYLGVSIW TPWRNIFSRL PKRIYSKILA
TTDMEIKYKP KVLISQIWNA IVISMYREHL LAIDHVQKLL YHQVPSEQEG KRTLRAPTFF
VSQEDHSFKT EFFPAMSEAE RRISFFAQSL STPIPEPLPV DNMPTFTVMI PHYSEKILLS
LREIIREDEP YSRVTMLEYL KQLHPHEWDC FVKDTKILAD ETSQFNGDYE KNEKDTQKSK
IDDLPFYCIG FKSAAPEYTL RTRIWASLRS QTLYRTISGF MNYSRAIKLL YRVENPEVVQ
MFGGNSDKLE RELERMARRK FKIVVSMQRY AKFSKEEREN AEFLLRAYPD LQIAYLDEEP
PQAEGEDPRL FSALIDGHSE IMENGMRRPK FRVMLSGNPI LGDGKSDNQN HCLIFYRGEY
IQLIDANQDN YLEECLKIRS VLAEFEEMTT DNVSPYTPGL PPTKFNPVAI LGAREYIFSE
NIGILGDVAA GKEQTFGTLF ARTLAQIGGK LHYGHPDFLN GIFMTTRGGV SKAQKGLHLN
EDIYAGMNAI LRGGRIKHCE YYQCGKGRDL GFGSILNFTT KIGTGMGEQM LSREYYYLGT
QLPLDRFLSF YYAHPGFHIN NLFVMLSVQL FMWCLLNLGA LRHETISCRY NRDVPETDPL
FPTGCANIIP IMDWVQRCIV SIFIVFFISF VPLTIQELTE RGFWRAATRL AKHFSSLSPL
FEVFVTQIYA YSLQQDLSFG GARYIGTGRG FATARMPFGV LYSRFASPSI YLGARLLMML
LFGTLTVWGY WLLWFWVSLL ALCISPFLFN PHQFAWADFF IDYREFLRWL SRGNTKAHSA
SWIGFVRLSR TRLTGFKRKV LGEPSSKLSG DTPRAKFTNI FFSEIIGPLV LVAATLIPYL
YINAGTGVIA ANNRGTDITP TNSLIRVAVV AFGPIGVNAG VAAGFFGMAC CMGPILSMCC
KKFGAVLAAI AHAIAVIMLL AFFEVMFFLE GWSFTKALLG MIAVVAIQRF VFKLIIALAL
TREFRADTSN IAWWTGKWYA LGWHTLSQPG REFLCKITEM GFFAADFCLG HVLLFFMLPP
LLIPYIDKFH SVMLFWLRPS RQIRPPIYSL KQSKLRRRRV IRYAILYFSM FVLFIVLIVG
PIIAKKFIGD IKLDVMNLQQ PSNWKNNDTS ASETGTAVAG GAKATASSTR GSSSSHNNQM
MARMLYGY
//
