(data stored in ACNUC7421 zone)

SWISSPROT: Q751S4_ASHGO

ID   Q751S4_ASHGO            Unreviewed;       554 AA.
AC   Q751S4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 2.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   ORFNames=AGOS_AGL351W {ECO:0000313|EMBL:AAS54140.2};
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:AAS54140.2, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54140.2, 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; AAS54140.2; -; Genomic_DNA.
DR   RefSeq; NP_986316.2; NM_211378.2.
DR   STRING; 33169.AAS54140; -.
DR   CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR   CAZy; GH72; Glycoside Hydrolase Family 72.
DR   EnsemblFungi; AAS54140; AAS54140; AGOS_AGL351W.
DR   GeneID; 4622609; -.
DR   KEGG; ago:AGOS_AGL351W; -.
DR   HOGENOM; HOG000164982; -.
DR   InParanoid; Q751S4; -.
DR   KO; K22832; -.
DR   OMA; KYTDPLA; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
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   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; Q751S4.
DR   SWISS-2DPAGE; Q751S4.
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..19
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT   CHAIN           20..554
FT                   /note="1,3-beta-glucanosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT                   /id="PRO_5005144167"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          401..492
FT                   /note="X8"
FT                   /evidence="ECO:0000259|SMART:SM00768"
SQ   SEQUENCE   554 AA;  59381 MW;  9A1A36069D9F905F CRC64;
     MLQTAIYGTV ACLLQAVVAQ RNNGGAALSA TAGTAPSIAT SSPSTNKVPP IEIHGNKFFY
     SNNGSQFYMK GIAYQAETSD ASASATINDP LADYESCSRD LPYLLELNTN TLRVYAVNSS
     LDHSRCMELF ESNGIYIVAD LSEPALSINR NNPEWSLKLF ERYAGVVDEM QKYSNVLGFF
     AGNEVTNEIN NTAASAFVKA AIRDTKAYIK EKGYREIPVG YSTNDDSNFR QEIADYFACG
     SQEEKADFYG FNVYSWCGDS TFEKSGYSDR TKEFSNLGIP VFFSEYGCNE VRPRKFGEVS
     ALYGSDMTDV WSGGIVYMYF EETNQYGLVT VDSSGRVSTN DDYNNLKTAL ATISPSSANK
     DSYTASSGSV ACPTTGSNWQ AATSLPPSPQ KDVCDCIKSA LRCVISPDVD QKDYSELFGY
     LCSEADVDCS DISADGTTGN YGAFSFCDDE TKLSYLLNKY YQEKGRSSSS ACDFSGSATL
     VSATGTASTC VPTSTGINLG SSSSNSGSGR GDSTTATSSA AAAADAIQPN TFSMALFIPT
     ALVFMLTGFG IAMS
//

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