ID A0A1Y1ZT35_9PLEO Unreviewed; 2395 AA.
AC A0A1Y1ZT35;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=BCR34DRAFT_535653 {ECO:0000313|EMBL:ORY13406.1};
OS Clohesyomyces aquaticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY13406.1, ECO:0000313|Proteomes:UP000193144};
RN [1] {ECO:0000313|EMBL:ORY13406.1, ECO:0000313|Proteomes:UP000193144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY13406.1,
RC ECO:0000313|Proteomes:UP000193144};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORY13406.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCFA01000042; ORY13406.1; -; Genomic_DNA.
DR STRING; 1231657.A0A1Y1ZT35; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000193144; 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; 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:UP000193144};
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..2395
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011007312"
FT TRANSMEM 1076..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2006..2024
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2031..2053
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2065..2085
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2097..2118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2138..2162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2185..2205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2217..2238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2250..2269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2321..2344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2364..2387
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..519
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 1653..1742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2395 AA; 267856 MW; 42837FAA92C6B472 CRC64;
MGADRNLLTL FCLVVSVLSL RWDPAHEGWN LNLNQSAVNP LDYWGEWDNH TFHPSPKNWR
FPFYVLTLDR YVDGDPTNNQ ANDSRWEHDW TSNQFRFGGD AKGLMNNLDY IQGMGIKVRA
VYLSGTPFIN MPWSSDGFGA LDFTLLDHHH GLIDDWRALI TEIHSRGMYV ILDNTLGTMG
DLLQWVGHEN ETAPFLWSEY DVRYKTSREY LDFHVSNDYN TTCQYPRLWG EDGFPLNNKT
VLDAMPKVCK ASEFDQYGDM KGVGEVPVYQ TQLAKFAGVQ DRLRTWRDDV LDKIMHFSCM
QIAMLDIDGF RMDKAAQTPI DIHAKWSDNQ RACARRHGKD NFLIVGEVVS KIPYASLLIG
RGKQPDQAFD NMSQAVSGRD LSNDNNYLRP FGSTALDGDA FHYPFYGAMT RFLGLDGPIG
LEGVDFVELW HNLLLHEDMV NANTGEFDPR HLWGMTNQDV FRWPALANGT QRHLLGLFIA
NLMMPGAPFQ LWGEEQEFYV LENQAADYVF GRTPMSSSRA WQLHGCYKLG EEVYVDIPFD
KALRGCEDDS VSLDHRDPSH FIRNILKRHY ELRLQYPVLN DGAQLETLSS QTRDIYLPGS
LGMPSPTGIW SIYRGPYEGV QDFSDAGDLG NQAVWIIYSN ENKTVNYTFN CRNETEGLIS
PFPENTAVKS LFYPYEEYTL ETSPARLSIQ NSSEPNGCLA SIEMQSWDYK MFVPKTKWVL
PGPTITQVIP GHDARILSQL ADHEAQTIPF EVHFSSEMSC ETVVRNFTVQ STTSNGEIAR
LNTSSVSCSA VQSDKQEYVG QVGTEWILEG ELENVYNGIH IYTINNVSTE STNLYTNAVD
HFMFRIGQAD NPMVFPATAN YSKSLLHRDE QTGALTVTHR ATGANKWQYT LNWEGTWSEW
QDYSPSATLT QQPWTGTKDQ QWTGEHVMVR YWSEMAGSME HVQHGDVGFD TPRRWPHMHI
TGPWNQYGFD SGLSDKMHDT GTGDWHFSIM TEYPERVSLS MWSINPDGQP DKRHRSKIYG
DVDQDSVLDW LPPTSLGMNL INITNPGMPY VGVKIIANDG DLRYTFVPVG SAWRQLIVAI
FLALIPVGTG AMAVWLFVKA FYDVKFNEHG ASGSPQTIVN AVTMLPGAMI KRKANSLNLF
NSSRSTAVTN PQRQEGFATD DEHSRRTCLI ATMEYDIQDW DVKIKIGGLG VMASLMGQNL
QHQNLIWVVP CVGGINYPVD QIAEPMQITV MGQSYDVSVQ YHRYQNITYV LLDAPVFRTQ
TKSDPYPARM DDMDSAIYYS AWNQCIAETI RRFPEIDIYH INDYHGALAP LYLLPDSAPP
CCLSLHNAEF QGLWSIKRWK DMEEICQVFN LSKDIVVKYV QFGEVFNLLH AGASYLRIHQ
RGFGAVGVSE KYGKRSFARY PIFWGLHKIG SLPNPDPSDT AAWSKDDVLP SASIDLEQES
QRGLLRTQAQ EWAGLRIDME AQLFVFVGRW SMQKGVDLIA DVFPSILEEN PKTQLICIGP
VIDLYGRFAA LKLRKLMELY PDRVCSKPEF TVLPPYVFSG AEFALIPSRD EPFGLVAVEF
GRKGALGVGS RVGGLGSMPG WWFTIESIAT KHLIRQFQSA IKAALTSSRE MRAEMRARSA
LQRFPVAQWL AGLEKLQSSS IKVHQRVMGA RSTPVSSSAS SMFSPLPSAA GSTFASPSNT
RPSSRIGSRV GSRVQSRASS PIREESEIVN QVPRPAASFS HGKSHRRPPP LSLNMTTVSG
TSTPALGSPV AVAASPTGVH GLRLFPIPSE TGPRALPEPS GSGGIDLRKV AGRAAPPLSR
QNSQDSNTSL SSFSNASPST SQHPSRPELP RNQPLSNRSS MLSLKSVIGD EKDYRLQRVD
PFFTDAQGVY TRQFGRMLDD LSGRTSTSQL CIEEFLVKSE KNWFGRFYDA KLGIRGSSTK
VLSVPDSNTS DGTISRTGSV IETTGQSEFQ LGTDYAPPKG FRKLVQTRIG DWPIYSLLLA
LGQILASNSY QITLLSGEIG QTATKLYIIA SIYLAASILW WTLFRVVQSR YVIALPFACY
GLAFFILGIA PYGRSYVARG WIQNVATGFY ALASGSGSLF FALNFGSEGG TATHTWVFRA
CVVQGTQQIY VTVLWYWGSY LSNLSATGRN PTGFASSPYI TAVTTPVAIV LVFIGIALYI
GLPDFYRSNP GNVPSFYQSL RRRKIILWFF VVVVIQNYFL SAPYGRNWRY LWSSQLVPAW
GIVILVFMFF VLVWIALFTI FRRLSIEHSW ILPIFAIGLG APRWAQMLWG TSGMGLFVPW
AGTPAIGAVL GRALWLWLGV LDALQGVGFG MILLQTMTRF HVAFTLTAAQ VIGSIATMAA
RATAPNRLGP GAVFPNLALS TDGLGNAIFW VALLLQGVVC VGFFTFFRKE QLFKP
//
