ID A0A166M7B1_9PEZI Unreviewed; 2521 AA.
AC A0A166M7B1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
DE Flags: Fragment;
GN ORFNames=CI238_03773 {ECO:0000313|EMBL:KZL64371.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL64371.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL64371.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL64371.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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}.
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:KZL64371.1}.
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DR EMBL; LFIW01002705; KZL64371.1; -; Genomic_DNA.
DR STRING; 1573173.A0A166M7B1; -.
DR Proteomes; UP000076584; 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 Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1233..1259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2097..2117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2129..2148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2155..2178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2190..2210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2222..2242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2262..2287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2308..2325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2345..2366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2373..2390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2447..2465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2493..2513
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 237..696
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1834..1890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2022..2066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1866..1889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KZL64371.1"
SQ SEQUENCE 2521 AA; 281365 MW; 47A36437E6C2E256 CRC64;
LRPASHYPSP LPPKTADRET GALRGEADGT DPSWTVLWPQ PLWSLLCHCL RLCLCPCLYL
SASDTPFRLQ PGAYCIWADP SSHEITPFST GTNVVLTAEF SSHPSRALHC VSSRHSFLLA
CWSASRPFSP PPTHHHHHTP SSFSSSLIPV LFFCCTILLT RPSRRVRVTM SNSVLAWALT
LLTTSSTLVS GLKYTASEVD YNLNQNRLAK NPYEYSGKRD NHTFAKSPPN WRFPFYTLFI
DRFVNGDPDN DNANGTVFEH DIMSNQLRHG GDLAGLVDTL DYIQGMGIKA LYIAGSPFIN
DPWKADSYSP LDLTLLDKHY GNITAWQEAI DAIHARGMYV VLDQTMATMG DLIGFEGYLN
ESTPFQTEEH KVQWKTSRRY LDFDIGNEYN ESCEYPAFWF EDGKPVGQDV VAQLKGCYNS
DFDQYGDIEA FGVFPDWQRQ LAKFASVQDR LREWVPSVRQ RLELYSCMTI QMLDIDGFRI
DKAVQVTVDA QAEWSTAMRK CAKDLGKDNF MVVGEITSGN TLGSIYLGRG RTPDMASALN
LADAVALDST SASTSGSFIR EHGKSALDAG AFHYSIYRFM TRFLGLSGNL EAGYDLPTDW
VQTWNQMILT NDFYNANTGE FDPRHLYGVT NQDVFRWPAI ELGTERMLLA YFITTMLLPG
APLVYYGEEQ NFYVLDNTAE NYVFGRQAFS AAQAWKIHGC YAGDNSVYVG WPINKGRRGC
EDETVAYDHR DPSASVRNWM KRLFSFRDEY PVLENGWLLE QLSNKTHGVQ YNGSGVATET
GIWSVARGYL SNQNETGDPV WLVYHNSPNE TTYEFDCSNE ADAFLSPFDG NTKVRNLFST
DGAITLESST KENGFKGAGH KAGCISSITM SPFEFRAYVP DKEWLEIAPS ITGFEPGHDA
PIDSTDANGK IPIAFKFSTE MDCDTVTKSI SARVTVDANT ETDVTFDTPV CGAMDPIEKE
SWTGAVASVW KWSANLQNVP DGIVKVTANN TAAPGGKKTN AVDHFLVRFG KPYNPVVFPA
SANYSRSLMQ ESNGVYFINH AAPGANKWRY STNWGSTWSN WMPYTGARQR MIPQAWEGTD
LQKWEGEHLM VQYFSKPLGS SSFIQHSDSS DIPFSRRWPH IFLHGPFNKW GYDAGLPNLM
TQVGDNRWEL HFMHEWPAQI QLNLWGINPD NQPDASFIYG DPNGDGVLDR LPPSSLSDNV
VNLTSPPPMP ALSYKLVLND ANWNYEAVPQ GNMWIQILFF FLLGLLPIVL AGLAGWIYMK
GFYQVKINKS GFSKKGWLPL KLGNESNINF GEKGKSLEMS QIPPSPVVTP AAAAATGGAP
RRKVLIATME YNIDDWKISI KIGGLGVMAK LMSQALSHVD LIWVVPCVGD VDYPLENEAE
PMFVEIMGES YEVKVYYHIY KNITYVILDA PIFRQQTKAD PYIARMDDLE SAILYCAWNS
CIAESIRRFN ADIYHINDYH GAAAPLYLLP QTVPVCLSLH NAEFQGMWPM RTEEEQKEVY
SVFNLPPKVV KDYVQYGSAF NLLHAAASYL RIHQRGFGAV GVSKKYGDRS LARYPIFWSL
KNIGQLPNPD PSDTGEWNPE EDISNHQDDI KIDETFEANR ATLRRQAQEW AGLEVNPNAD
LFVFVGRWSL QKGVDLIADL FPSILEKYPS VQLICVGPVI DLYGRFAALK LNKLMEKYPG
RVFSKPEFTQ LPPYIFSGAE FALIPSRDEP FGLVAVEFGR KGALGVGARV GGLGQMPGFW
YTVESMSPAH LLQQFKQAIA SALSCKPRKR ALMRAWSAKQ RFPVAQWIRQ LDTLYNDSIK
VHNKEAAKQK KAGGIRNLTD SSLRSSVAVS EYGAELTPTG SRAPSPLPPP SRIASPAGRI
NSPDLGTPNM PWTNIPSSRR SSFSSSIGGR DSMLAPRESM FASGRESMVS VDSFAIRAQN
DVSSPQTPGF DGLGLPQPSF YKQQRNSSQL SLPDVVGDRH DLKLQNVDQN FTDKNGEFYA
EFEQMLNNLT AKNSGNDLCI ENFLKKSEKK WFARYRDAKL GRRDHSRSRS PAPSRPGSSK
GLGAKFDGER GRSRTPSGLT SASRYDDSPV DDEFLLGDNY NAPTGLKKIL SIRIGDWPIY
AFFLAFSQVI SINSYQIVLL TGETNQTPLK LYIVAATYLV TSAFWWIMVR FTKSVYALSL
PWAFFGLAFL LLGLSPYMTP WQSRAAMQDA ATALYAAGAS AGALSFALNF GDEGGAPTKQ
WITRALAVAG VAQVYSLMLW YWGSLTHTPE TSPMAFFDGT SIPKALVVCV PVAIMLWAIG
LILFFGLPDY YRQAPDNIPG FYISLVRRKL VPVFFVMIII QNYWLSAPYG RNWQFLFASQ
FIPGWGVVLL ALGFFVVLWA IILYVFSFFS ESHTWLLPIF AIGLCAPRWA QMLWGTSSMG
LYLPWAGGPV GSAILSRCLW LWLGLLDNIQ GVGLGMMLLA TLTRQHVLAV LIGAQIVGSA
FTMLARATSP NALSPNTTFP DFSQGLMPGV SSYWFWICLG FQLVIPVLFF KFFRKEQVSK
P
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