ID F8N1R8_NEUT8 Unreviewed; 2393 AA.
AC F8N1R8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=NEUTE1DRAFT_133661 {ECO:0000313|EMBL:EGO53194.1};
OS Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO53194.1};
RN [1] {ECO:0000313|EMBL:EGO53194.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO53194.1};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-alpha-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC alpha-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:19749, Rhea:RHEA-
CC COMP:11150, Rhea:RHEA-COMP:11151, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28100, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.183; Evidence={ECO:0000256|ARBA:ARBA00000687};
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC {ECO:0000256|ARBA:ARBA00006122}.
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DR EMBL; GL891382; EGO53194.1; -; Genomic_DNA.
DR RefSeq; XP_009856814.1; XM_009858512.1.
DR GeneID; 20825764; -.
DR KEGG; nte:NEUTE1DRAFT133661; -.
DR VEuPathDB; FungiDB:NEUTE1DRAFT_133661; -.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000008065; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0047657; F:alpha-1,3-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11323; AmyAc_AGS; 1.
DR CDD; cd03791; GT5_Glycogen_synthase_DULL1-like; 1.
DR CDD; cd06174; MFS; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013534; Starch_synth_cat_dom.
DR PANTHER; PTHR47182; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE AGS1-RELATED; 1.
DR PANTHER; PTHR47182:SF2; CELL WALL ALPHA-1,3-GLUCAN SYNTHASE MOK13; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF08323; Glyco_transf_5; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..2393
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003375649"
FT TRANSMEM 1062..1084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1967..1988
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2000..2018
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2030..2049
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2061..2079
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2091..2111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2136..2159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2180..2197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2217..2241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2261..2286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2292..2312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2319..2337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2366..2385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..516
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1621..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1683
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1917..1944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2393 AA; 268929 MW; ACF6F346490AB6A0 CRC64;
MAAVLLTLVL ATLVQGLRYD PDYVDYNLNQ NKDAVNPLDY SAPKRDNYTA SPKNWKFPFY
TLFLDRYANG DPTNDNINGT VYEQDPTSNQ LRHGGDVQGV IDSLDYIQGM GIKAIYIAGS
PFINLPWGVD SYSPIDLTLL DMHYGTIKDW QRMVDEIHKR DMYVMIDHTF STELSMSDLL
AFKGFENETA PFSLKEHKVH YKGNREYLDF APSNEYKDEC QYPRFWDETG MPVGEDVTSQ
LKGCYDSDFD QYGDMEAFGV HPDWQRSLAK FASVQDRLRD WAPSVRKRIE LFSCLSIRVL
DVDGFRFDKA TQVTVDAMAE HNEAIRKCAK EHNKDNFFMP GEITGGDGYG AIYIGRGRQS
NQRPSFPQVM NLTTKELSKN NSLVIRDEGK NGLDAAAFHY SAYRFLTRFA GMSGNLEAGY
DLPLNWVEMW NQMIITNDFV NPNTGLFDPR HMYGTMNQDV FRWSGIKQGT QRMLLGLFIM
TLHMPGIPLV FYGEEQEFYV LDSTADNYLF GRQAFSPTPG WMLHGCHVGN STQYVGWPIE
TSRTGCTDPR VALDHRDPSA PVRNIMKSMY HMRDTYETFR EAWLLQTLSS KVRNVTLEGS
TTSTEFGIWS VARAFMPSVQ KESYPAEPVW LVYHNEDKET EYTFDCSKKG QDFVSPFDAG
ATVKNLFYPY DEIKLEKSTQ SLGFANSHAV SGCLSNITMA PFEFRAYVLK EDWESPPPMI
TKFTPGHDAS VESYGNGKVD IQLEFSEEMD CEEVLNSISF TSTTEENASI KIDAHRCDNI
KASFIAEYVG TIPSTWRFNA TLSNVKDGIH RITVKDPQSG RNASTGTTDH FLLRVGSSNN
PLVNPMKANY SKTLVTKEGS DLFVNHAAAG ADKWRYSTNW GSTWSDWLEY KGGKEKIDKL
AWKGTKKQEW DGDHVMVQYW SQLLGSASFV QSGDSKETKT RRLPHLFAHG LFNKFGFDAG
VKNELKLVGD GLWEGHVMDE WPTHFQLNVW GMNPDQRPDA GWVFGDVDGD GVLDRMPPSS
LALNVINATE PPPMPALSWK LVFNDALLTF HKEPQGNMAV QIIMFILLAS LPIVGGLTAV
WTFMGSFYKV KVNKVGFKRR GRSPLRDIGK RISSTVSFEN FRHKDVGDTE LAVIPGKRRK
VIIATMEYNI DDWNIKIKIG GLGVMAQLMG KALEHQDLIW VVPCVGGIDY PIDQRAEPMY
VPIMGKEYEI EVQYHQVQNI TYVLLDAPIF RTQSKADPYP PRMDDMDSAI YYAAWNYCIA
EAIRRFNPDL YHINDYHGAA APLYLLPERT IPCALSLHNA EFQGMWPMRT PEESKEVCEV
FNLDPEIVKE YVQFGSVFNL LHAGASYLRV HQKGFGAVGV SKKYGDRSYA RYPIFWGLSK
IGQLPNPDPS DTAEWSRDEQ IQAKDVVVDL EAEAKRGDLR RQAQEWAGLE VNPDAELFVF
VGRWSLQKGV DLIADIFPSI LEKYPTTQLI CVGPVIDLYG KFAALKLAKL MEKYPKRVYS
KPEFTALPPC IFSGAEFALI PSRDEPFGLV AVEFGRKGAL GVGARVGGLG QMPGFWYTIE
STAPQHLIQQ FRGAIVSALE SKKKDRQMMR AWSAKQRFPV AQWVEDLDTL QTEAIRIHHK
EAKKRKRVPS GSLLTVPSSV DLHGNNTQRD YFDDAVSTPA GARSRTASTV STPGPQDGAT
HHRRTLSSPF DDDIPSIASP PPGTPGSPPT VNVDRVGDHS DHGGEDGADE PLMPPNPLFL
NPSASSSVTD VASIAANVYG HAGDRSSIDT FAMRMMSPDS SEIRPQAFGL LNPQARPGAE
ALYQARNRNS SRLSVIDVVG DRQDFRLQKV DPFFTDANGQ YYREFERKLN GLTAKNSETE
LCIEDYLKES EKEWFKEFRN AKLGRSRSPS RSRSPMPGLK IKKTRHASIG SVQSISPTED
DDRENEERNN SNNEGVGHHR DDQFLLGDGY KPPTGLKKLL SIRLGDWPIY SFIIALGQIL
AANTYQIVLL AGESGQTPTQ LYIVAGTYAL GSLLWWFMFR RLPALYSLSL PWLFYGLAFM
LLGVTPFMPE HVRFPVQNTA SALYAAGASS GSLFFAMNFG DEGGVPIMTW IFRAAIIQGI
QQVYILALWY WGSLLTAQTP TGSPHVGTWI ANKVPVALVI TVPIALIFWC LGVISFVGLP
DYYRQLPDKI PSFYKSLLRR HIVPWFLLMV VIQNYFLSAP YGRTWEFLFY SRAVPGWAIL
LLAIGFFVGV WCLLLWLFAY FTKTHPWIVP LFAIGLGAPR WAQMLWATSG IGLYLPWCGS
VVLSAIISRC LWLWLGLLDT VQGVGLGMVL LLTLTRQHVA ATLIGAQFLG AVFMMLARAT
APDKDGPGDV FPDFSAGVMP GLGRPWFWIV LGLQLVLPIG FFKFFRKEQV AKP
//
