ID Q0CRR2_ASPTN Unreviewed; 2435 AA.
AC Q0CRR2;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=alpha-1,3-glucan synthase {ECO:0000256|ARBA:ARBA00012688};
DE EC=2.4.1.183 {ECO:0000256|ARBA:ARBA00012688};
GN ORFNames=ATEG_03622 {ECO:0000313|EMBL:EAU35424.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU35424.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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 ---------------------------------------------------------------------------
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; CH476598; EAU35424.1; -; Genomic_DNA.
DR RefSeq; XP_001212800.1; XM_001212800.1.
DR STRING; 341663.Q0CRR2; -.
DR EnsemblFungi; EAU35424; EAU35424; ATEG_03622.
DR GeneID; 4318381; -.
DR VEuPathDB; FungiDB:ATEG_03622; -.
DR eggNOG; ENOG502QSGC; Eukaryota.
DR HOGENOM; CLU_000488_0_0_1; -.
DR OMA; AWRDHGC; -.
DR OrthoDB; 141134at2759; -.
DR Proteomes; UP000007963; 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; 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 SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007963};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2435
FT /note="alpha-1,3-glucan synthase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004170385"
FT TRANSMEM 1080..1102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2009..2031
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2043..2060
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2067..2086
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2098..2121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2133..2154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2184..2205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2225..2245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2257..2280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2289..2310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2334..2354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2361..2383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2403..2427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..519
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT REGION 725..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1654..1683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1710..1783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1801..1861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1835..1858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2435 AA; 273647 MW; A59680B60C389A35 CRC64;
MWRTSIGVVA LLASVASCWP YDESLLDYNI NQNKSATNPA DYWGEWPDHQ GAYHPSPDNW
RFPFYTLFMD RFVNGDPTND NINGSQFEHD LNSNQMRHGG DVAGLLDTLD YLQGMGIKGL
YLAGTILMNQ PWGSDGYSAL DTTLLDQHFG TLETWRNAIT EIHKRGMYVV LDNTIATMGD
LIGFEGHLNT STPFSEKEYK AVWKSDRRYV DFDIGNEYNA TCDYPRFWYE DGMPVNASLT
SGLVGCYNSD FDQYGDIEAF GVWPDWKRQL AKFASVQDRL REWHPTVRER LIRHSCMIIA
SFDIDGFRYD KATQSTVDAL GEMSKAYREC ARKVGKKNFF IAGEITGGNQ FGSIYLGRGR
QSNQKVDDIM EAMNLTSDSD PQHFLREAGH EAIDGAAFHY SIYRSLTRFL GMDGQLDAGF
DLQVDWVNAW NEMLQTNDLI NANTGKFDPR HMYGVTNQDV FRWPAIQYGV ERQLLGTFIT
TLMLPGIPLL LWGEEQAFYV LDATATNYIY GRQAMSPATA WRTHGCFSLD SSQYYKWPIE
AGRNGCNDET VSYDHRDPSH PVRNILKHMY QMREDFPMLN EGYLISTLSK KTESVYYPGS
NDTATETGMW SVRRDINPNV QDLGSVDKNQ MVWLVYQNVN RTMSYEFNCT DNDDALIAPF
PAGTHVKNLF YPYDELKLEA STQKLGFGGS KEFNGCYPNL TMDRYEFRAY VPSKLFKKPR
PMITKFQPSD NENAGHDSPL RSTVAPDASE TVPLELQFSE EMDCDAVTKA ISFNSSTEIG
KTPSIDLNTV HCSTIPEQKG KLTGQIPGVW QWTASLTGVY NGVHRITVNN ATNADGSAST
NAVDHFLFRI GQIDNPMVFH SANYSSSLLH QEDNGTLFIQ HHAAGADMYR YSTNWGTSFS
DWIPYKGGND TINALEWSGT SKQAWKGHHV RVEYWSRWTG SSDYVQEGDY GWDHNVQRRF
PHVFFNGPYN QYGFDGGLDN EVDLDTKDGY WKYHFTSEWP AVGQLNVWGM NPDGQPDQSW
VLGDTDNDYI LDRLPPSSLS ATLINITDHP PSPYLSWKFY ISDARLHYQL VPVGHQSVQI
AMFVLFWIIP VITASACVYI FMKSFYKVKF NQVGVSETHS MIPLALRRKF KQMQAGKTGP
PNPLMRLAEK SGFMQSTTAL GAAAAGKRRM VLIATMEYDI EDWAIKIKIG GLGVMAQLMG
KTLGHQDLIW VVPCVGGVDY PVDTPAEPMT VTILGKSYQV EVQYHILNNI TYVLLDAPVF
RQQTKSEPYP ARMDDLESAI YYSAWNQCIA ETIRRFPIDL YHINDYHGSL APLYLLPETI
PACLSLHNAE FQGLWPMRTQ KEKEEVCSVF NLDLETVRSY VQFGEVFNLL HAGASYLRVH
QQGFGAVGVS KKYGKRSYAR YPIFWGLRKV GNLPNPDPSD VGEWTKESGL PKDEDIQVNA
DFEAARGELK RQAQEWAGLE QNPDADLLVF VGRWSMQKGV DLIADVMPAV LEARPNVQLI
CVGPVIDLYG RFAALKLDRM MKVYPGRVFS RPEFTALPPY IFSGAEFALI PSRDEPFGLV
AVEFGRKGAL GIGARVGGLG QMPGWWYNVE SVSTSHLLVQ FKLAIEAALS SKQETRAMMR
ARSAKQRFPV AQWVEDLEIL QSTAIQVHNK QVTKGHGLPM TPSSSMTPTG ALTPSTRPSS
PLMMQKMNRS IPHSRDSSYS NLNHLAASPI PQKNIYSRDP SPGDAVKPSG LQRSLSLGVR
SGPGHVSRRG RGRRGQDAEN IAEEDENSAE HSDGEAGSDT DSILSFYGDE EYTLTPAQIE
ESRRAQAVQS PGSRVVSTPR RYSEDSLHPH HSVMPPLSPA TPPSADQTLL PPPKPFAEPG
NRLSSASVLS LDTVVGNKKD FKLQKVDPFF TDSNGEYYKE FERRLEGLNG SNSETQFCIE
EYLIKSERKW FDKFRDARLG RIKSPTPSVY RDKHNASPGG SFYADDAASR HSGHDFHDDD
DTDDEFLLGK DYVPPTGLKK WMQIKIGDWP IYTIFLALGQ IVAANSYQIT LLTGEVGQTA
EKLYGIATVY AITSACWWLV FRYFKSVVCL STPWFLYGIA FLFIGSAHWE GDSFTRGWIQ
NIGSGFYAAA SSSGSIFFAL NFGDEGGAPV KKWIFRACVI QGIQQAYIIV LWYWGSTLSK
ASSEGLLVAE NQISNTWKMT AICYPIAMLL WAIGLLLIFG LPNYYRQSPG KVPSFYKSLF
RRKIVLWNFV AVILQNFFLS APYGRNWSFL WTSIHTHAWQ VVILCIVFFG FVWVAFLYLV
SQFSKQHSWF LPVFACGLGA PRFIQIWWGV SGIGYFLPWV AGGYTGGALV SRSLWLWLGV
LDTIQGLGFG IILLQTLTRM HMCFTLIVSQ ILGSIATICA RAFGPNNVGP GPISPDVTKG
ADAVANAWFW VALFCQLLVC AGFLLFFRKE QLSKP
//
