(data stored in ACNUC7421 zone)

SWISSPROT: Q751P1_ASHGO

ID   Q751P1_ASHGO            Unreviewed;       533 AA.
AC   Q751P1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 92.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   ORFNames=AGOS_AGL352W {ECO:0000313|EMBL:AAS54139.2};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54139.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54139.2, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Splits internally a 1,3-beta-glucan molecule and transfers
CC       the newly generated reducing end (the donor) to the non-reducing end of
CC       another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC       linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC       cell wall. {ECO:0000256|RuleBase:RU361209}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU361209};
CC       Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU361209}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC       {ECO:0000256|RuleBase:RU361209}.
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DR   EMBL; AE016820; AAS54139.2; -; Genomic_DNA.
DR   RefSeq; NP_986315.2; NM_211377.2.
DR   STRING; 33169.AAS54139; -.
DR   CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR   CAZy; GH72; Glycoside Hydrolase Family 72.
DR   EnsemblFungi; AAS54139; AAS54139; AGOS_AGL352W.
DR   GeneID; 4622608; -.
DR   KEGG; ago:AGOS_AGL352W; -.
DR   HOGENOM; HOG000164982; -.
DR   InParanoid; Q751P1; -.
DR   OMA; AEYGCIE; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005621; C:cellular bud scar; IEA:EnsemblFungi.
DR   GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; IEA:EnsemblFungi.
DR   GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IEA:EnsemblFungi.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000936; C:primary cell septum; IEA:EnsemblFungi.
DR   GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0007568; P:aging; IEA:EnsemblFungi.
DR   GO; GO:0006342; P:chromatin silencing; IEA:EnsemblFungi.
DR   GO; GO:0030447; P:filamentous growth; IEA:EnsemblFungi.
DR   GO; GO:0071970; P:fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process; IBA:GO_Central.
DR   GO; GO:0031505; P:fungal-type cell wall organization; IBA:GO_Central.
DR   GO; GO:1905897; P:regulation of response to endoplasmic reticulum stress; IEA:EnsemblFungi.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR012946; X8.
DR   PANTHER; PTHR31468; PTHR31468; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q751P1.
DR   SWISS-2DPAGE; Q751P1.
KW   Glycoprotein {ECO:0000256|RuleBase:RU361209};
KW   GPI-anchor {ECO:0000256|RuleBase:RU361209};
KW   Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW   Membrane {ECO:0000256|RuleBase:RU361209, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Signal {ECO:0000256|RuleBase:RU361209};
KW   Transferase {ECO:0000256|RuleBase:RU361209};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT   CHAIN           19..533
FT                   /note="1,3-beta-glucanosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT                   /id="PRO_5005144201"
FT   TRANSMEM        511..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          378..467
FT                   /note="X8"
FT                   /evidence="ECO:0000259|SMART:SM00768"
SQ   SEQUENCE   533 AA;  57343 MW;  6688CF209BF90792 CRC64;
     MLFNKLAAVA ALGSLVTAAT SSSGEVPEIV IKGNKFFYSN NGTQFFMRGI AYQTDGHDGS
     GSNKYVDPLA DFKTCSRDIP YLQQLRTNVI RVYALDGKKD HTECMKALAD AGIYVIADLS
     EPSLSINRNS PEWSVELYDR YTQVVDELQK YKNVLGFFAG NEVTNEVNNT EASAFVKAAV
     RDTKAYIKQK GYRKIPVGYA ANDDAKFRDE ITAYFACGSN EERADFYGFN VYSWCGDSSF
     EKSGYSDRTK EFSRLPVPAF FSEYGCNEVK PRKFTDVAAL YGDQMTDVWS GGIVYMYFQE
     ANEYGLVTVK GDKVSTLSDF SYYSAQIAKA SPTGVQSASY TPSITSLECP TIADNWKAAS
     SLPPTPSKDA CKCMMDALSC VVNDSVDKED YGKLFGYLCG SDKKLCNGIA VDASKGEYGA
     FSYCSGKEKL SYLLNEYYKA NGKSSSACAF SGSASLRKPT EAATCAAVLS SASAGLPAGG
     NASGSSGAAT STGGSGEPKP SMGTANAKYN MLNVLISSAA TLSVFMGFGL IFI
//

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