ID   BTGC_NEOFI              Reviewed;         689 AA.
AC   A1DEV5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-MAY-2023, entry version 73.
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=NFIA_078520;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027696; EAW17912.1; -; Genomic_DNA.
DR   RefSeq; XP_001259809.1; XM_001259808.1.
DR   AlphaFoldDB; A1DEV5; -.
DR   SMR; A1DEV5; -.
DR   STRING; 331117.A1DEV5; -.
DR   GlyCosmos; A1DEV5; 5 sites, No reported glycans.
DR   EnsemblFungi; EAW17912; EAW17912; NFIA_078520.
DR   GeneID; 4585859; -.
DR   KEGG; nfi:NFIA_078520; -.
DR   VEuPathDB; FungiDB:NFIA_078520; -.
DR   eggNOG; ENOG502QTKT; Eukaryota.
DR   HOGENOM; CLU_011476_0_1_1; -.
DR   OMA; QYPDCLK; -.
DR   OrthoDB; 675117at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR16631:SF17; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE BTGC; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 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..689
FT                   /note="Probable glucan endo-1,3-beta-glucosidase btgC"
FT                   /id="PRO_0000395129"
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..689
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          128..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..365
FT                   /note="Disordered"
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..365
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   689 AA;  72601 MW;  BBFC912E985B68F4 CRC64;
     MSGPNRTYSF GEGDDGLAHP SSRTHAMHSQ YDDVSPISDG ARMNPMNGQG TDHGLASVPE
     DGHQGWGRGP EPSPSILTGS SATPGMDNLG PGAVGGGISG IALSVANSHD RLSGVEALMG
     TDGQEANIPA ERGFSTTGSD NPYVPAPPEH RYSYGSNIAL GAAAAPAGQL TPGQSVSHLS
     SSNPSQRNLY DIPYQGAGGL NAGPYQRHSA YSSNDLPVDI NPDEIVDDGD DGFVPAPNSS
     SSARKSQAIP AAAGGAAAGG FLGNLGGLFG GKSAADTSYG PVPGAGLEAG EKGRWVKPKP
     GGGSKKRGWI VGAILAFIII GAIVGGAVGG TIGHRGNEEP SSASSSSSSS TQTATDDTST
     NGDLDKNSAE IKALMNNKNL HKVFPGIDYT PWGVQYPLCL KYPPSQNNVT RDMAVLTQLT
     NNVRLYGTDC NQTEMVLHAI DKLEIKDMKI WLGVWIDSNI TTSRRQIDQL YKIIDDAKDT
     SIFNGAIVGN EALYRAGSDK TSAQTTLINY MQEVKDHFKK KNIDLPVATS DLGDNWDATL
     VQAADVVMAN VHPFFGGIPV DQAAAWTWQF WQDHNVALTK GTNKKQVISE VGWPSGGGND
     CGLGANCPND TAGAVAGVDE LNKFMEDWVC QALENGTDYF WFEAFDEPWK IVYNTANENW
     EDKWGLMDAA RNLKPGLKIP DCGGKTATR
//