ID W9YCD0_9EURO Unreviewed; 2454 AA.
AC W9YCD0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=A1O3_08275 {ECO:0000313|EMBL:EXJ79989.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ79989.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ79989.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ79989.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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:EXJ79989.1}.
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DR EMBL; AMGY01000007; EXJ79989.1; -; Genomic_DNA.
DR RefSeq; XP_007736563.1; XM_007738373.1.
DR STRING; 1182542.W9YCD0; -.
DR GeneID; 19172363; -.
DR eggNOG; ENOG502QSGC; Eukaryota.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000019478; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW 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..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2454
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004933509"
FT TRANSMEM 1080..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2029..2051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2063..2080
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2087..2110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2122..2142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2154..2175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2195..2219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2240..2259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2279..2302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2309..2328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2353..2374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2381..2401
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2427..2446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..518
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1706..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1980..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1706..1724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2454 AA; 274365 MW; ED88EFD896908AC9 CRC64;
MVFSAWGLVC ALLITISAAF RYDPAYIQYN LNQNQTANDP LDYWGEWTGH EYNPSPANWR
FPFYTLFLDR FVNGDPSNDN INGTSFEHDS NSNQMRHGGD IQGLLDTLDY LQGMGVKGLY
IAGSPFINMP WGYDQYSPLD LSILDPHFGD IDMWRTAIEE IHARNMYVVL DNTFATMGDL
IGFDGYLNTT TPFTLAEHQV QWKTDRHYQD FQIGNNYNKT CQYPRFWLET GYPVGEDVTK
DMVGCYDSEF DQYGDTEAFG LHPDWVRQLS KFASVQDRLR EWHEPVRRKL ENFYCILIAQ
LDVDGFRYDK ATQSTIDAMG FMNDAMRRCA KRYGKNNFFL PGEITGGNVF GSLYLGRGRQ
PDMVADNITM AVTMTNDSAS KYFLRGPDHG ALDAAAFHYT VYRTLTRFLG MDGNLEAGYD
APPNWVDMWN DFLITNDFVN ANTGLFDPRH LYGVTNQDVF RWPAITNGIE RQLLGHFITT
IELPGAPLLL WGEEQAFYVL DNTASNYIFG RQAMSSATAW LSHGCYSLDS TQFFKMPLNA
SRHGCEDEAV SYDHRDPSHP VRNIIHHMNQ LREQYPVLQD GFFLQQLSNQ TEHIQLPGSG
HVKTETGMWS VMRSGFPGVQ DLSATGAGNL QIWLLYSNAN TTRSYTFDCN NNATDLNTTS
LIAPYDAGTT VKNLFYPYDE HTLDDSVHSL GINGSTEPNG CLSGLQMQAY DFRAYVPLAQ
WVGPKPMITK FSPGHDVRLE SKVSANETER VDIEIQFSVD MDCDSVTNSI VFNSTTETGD
APTIDQHSIQ CGNLSSPQTP PYVGAISSTW SWSATLEGVA NGIHAISVRN ASSVSGEVTD
AIDRFLFRIG QRNNPMVFTT SANYSSSLLG KSDNGTLTLS HAAAGADKWR YSTNWGSSFS
PWMSYGGGKT QIEEQPWSGT DLQSWKGTHV RVEYFSRLAG SSDHIQQGDL DYDIPRRFPH
LFVNGPYNQY GYDAGLDNRM KLTTNSTWEH HFMTEWSLSG ALAQINVWGI NPDGKPDQTF
VMGDADGDSV LDRLPPSSLS SVVLNITQPP PKPYLGWRVV IHDGNLRFKL VPSGNMWSQL
ILYVLLWTVP VITAAFGVWS FMQAFYQVKF NQVGFSEKAA LIPAGLKKQF KKLVDEENSP
GLLSKFTRKP KFVQPTGTII DQQRRRTVLI ATMEYDIEDW AIKVKIGGLG VMASLMGKNL
GHQNLVWVVP CVGDIDYPVD QTADPMTVSI LGKPYEVQVQ YHVLRNITYV LLDAPVFRQQ
TKAEPYPPRM DDLPSAIYYS AWNQCIAQAV NRFPVDLYHI NDYHGSVAPL YLLPRTIPAC
LSLHNAEFQG LWPMRTRQER EEVCSVFNLS PEVVQKYIQF GEVFNLLHAG ASYLRVHQEG
FGAVGVSKKY GKRSYARYPI FWGLKKVGNL PNPDPSDTGE WDKKLPKDSD IRVDPEFEAR
RPELKRQAQE WAGLEQNPKA ELFVFVGRWS MQKGIDLIAD VFPSILDANP NVQLITVGPV
IDLYGKFAAL KLDRMMKLYP GRVFSKPVFT ALPPFIFSGA EFALIPSRDE PFGLVAVEFG
RKGALGVGAR VGGLGSTPGF FFTVESMTTG HLIHQFKLAI KEALSCKPET RALMRARAAK
QRFPVAQWVE DLEILQSTAT RIHDKVEATK RHSAAAEMMW PSSIWNTPAG SGAVTPRTPN
MPHSRASSYA ALHSLTSRLK NIGHNHEQSH RVGNLSSPGL SRSASLGSRR GPGHLAARDT
HDGSEPNSPA MLPPVPDMEG DDTGIGTAVS HYDNDRESDD EDEHGREAQL EDDSSDSEDE
STTMSTPNHG RYDGWAVQEE GYLPSRDNES PRLNRGLELE LSPLPKVRSG AFDSPPLPAS
PRPDLGLLVP PAALSESNYR LSSNSMLSVN SVVGEKQDFM LQKVDPFFTD SNGEFARAFE
KKLESLTGST SESAACIEEF LVKSEKKWFN TYRNAKLGRY NGSYAHSSFQ AHRESRATSA
AGSIYEENSE HSSGNEHDRS NLTDEFLLGT DYVAPSGLKK WMQLRVGDWP VYAFFMAFGQ
IIAANSYQIT LLTGEVGQTA DKLYAIASIY LVTSICWWIL FRRFSSVVCL SLPFFFYGLA
FLLIGVAHYV STASGRGWVQ NVGTGMYAVA SSSGSIFFAL NFGDEGGAQV KAWVFRACVI
QGTQQIYVVA LWYWGSYLNR RTTDGLVTTP DPVVSTWKIT AITLPIAMLL WAVGLLMWFG
LPKYYLQAPG RMPSFYHSML RRKIVVWFLV TVVIQNFFLS APYGRNWSFL WSSSHASTWQ
IFCLVILFFV FVWAGFLWLF ALLSKSHSWI LPLFAIGLGA PRWAQIWWGT SNIGVYLPWA
GGYTASALLS RSLWLWLGTL DAIQGVGLGM ILLTTLTRVH VAFTLLTAQV LGSVATIVAR
ACAPNKIGPG PISPDISGSL GTLWQPWFWV GLVANLSICV GYFMFYRKEQ LSKP
//
