ID   BTGC_ASPFU              Reviewed;         688 AA.
AC   Q4WUK5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Probable glucan endo-1,3-beta-glucosidase btgC;
DE            EC=3.2.1.39;
DE   AltName: Full=Endo-1,3-beta-glucanase btgC;
DE   AltName: Full=Laminarinase btgC;
GN   Name=btgC; ORFNames=AFUA_5G08780;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- FUNCTION: Glucanases play a role in cell expansion during growth, in
CC       cell-cell fusion during mating, and in spore release during
CC       sporulation. This enzyme may be involved in beta-glucan degradation.
CC       Active on laminarin and lichenan (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; AAHF01000003; EAL91721.1; -; Genomic_DNA.
DR   RefSeq; XP_753759.1; XM_748666.1.
DR   AlphaFoldDB; Q4WUK5; -.
DR   SMR; Q4WUK5; -.
DR   STRING; 330879.Q4WUK5; -.
DR   EnsemblFungi; EAL91721; EAL91721; AFUA_5G08780.
DR   GeneID; 3510833; -.
DR   KEGG; afm:AFUA_5G08780; -.
DR   eggNOG; ENOG502QTKT; Eukaryota.
DR   HOGENOM; CLU_011476_0_1_1; -.
DR   InParanoid; Q4WUK5; -.
DR   OMA; PLNTQYP; -.
DR   OrthoDB; 1163530at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
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:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Cell wall biogenesis/degradation;
KW   Glycoprotein; Hydrolase; Membrane; Polysaccharide degradation;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..688
FT                   /note="Probable glucan endo-1,3-beta-glucosidase btgC"
FT                   /id="PRO_0000395124"
FT   TOPO_DOM        1..307
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..688
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        491
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        590
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        431
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        609
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        635
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   688 AA;  72696 MW;  BFE0AA05F1D71214 CRC64;
     MSGPNRTYSF GEGDDSLAHP SSRTHAMHSQ YDDVSPISDG ARMNPMNGQG MDHGLASVLE
     DGRQGWGRSP EPSPSLLTGS SATPGMDNLG PGAVGGGISG IALSVANSHD RLSGVEALMG
     TDGQEANIPA ERGLSTTGSD NPYVPEPPEH RYSYGSNIAL GAAAAPAGQL TPGQSVSHLS
     STNPSQRNLY DIPYQDVGGL NAGPYQRHSA YSSNDLPVDI NPDEIVDDGD DGFVPAPNSG
     SGARKSQAIP AAAGGAAAGG VLGNLGGLFG GKSAADTSYG PVPGAGLEAG EKGRWVKPKP
     GGGNKKRGWI VGAILAFIII GAIVGGAVGG TIGHRGNEEP SSASSASSSS TQTATEDTSV
     NGDLDKNSAE IKALMNNKNL HKVFPGIDYT PWGVQYPLCL KYPPSQNNVT RDMAVLTQLT
     NNVRLYGTDC NQTEMVLHAI DKLEIKDMKI WLGVWIDSNE TTSRRQIDQL YKIIDDAKDI
     SIFNGAIVGN EALYRAGSDK TSAQTTLINY MQEVKDHFKK KNIDLPVATS DLGDNWDATL
     VQAADVVMAN VHPFFGGIPV DQAAAWTWRF WQDHNVALTK GTNKKQIISE VGWPSGGGND
     CGQGANCPND TAGAVAGVDE LNKFMEDWVC QALDNGTDYF WFEAFDEPWK IVYNTGKENW
     EDKWGLMDSA RNLKPGLKIP DCGGKTAT