ID   BTGC_EMENI              Reviewed;         649 AA.
AC   Q5B430; C8VAX6; Q1HFT1;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=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=AN4700;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16844780; DOI=10.1073/pnas.0604632103;
RA   Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.;
RT   "Development and application of a suite of polysaccharide-degrading enzymes
RT   for analyzing plant cell walls.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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. {ECO:0000269|PubMed:16844780}.
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; DQ490493; ABF50869.1; -; mRNA.
DR   EMBL; AACD01000080; EAA60742.1; -; Genomic_DNA.
DR   EMBL; BN001303; CBF76969.1; -; Genomic_DNA.
DR   RefSeq; XP_662304.1; XM_657212.1.
DR   AlphaFoldDB; Q5B430; -.
DR   SMR; Q5B430; -.
DR   STRING; 227321.Q5B430; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   CLAE; LAM17A_EMENI; -.
DR   GlyCosmos; Q5B430; 4 sites, No reported glycans.
DR   EnsemblFungi; CBF76969; CBF76969; ANIA_04700.
DR   GeneID; 2872500; -.
DR   KEGG; ani:AN4700.2; -.
DR   VEuPathDB; FungiDB:AN4700; -.
DR   eggNOG; ENOG502QTKT; Eukaryota.
DR   HOGENOM; CLU_011476_0_1_1; -.
DR   InParanoid; Q5B430; -.
DR   OMA; QYPDCLK; -.
DR   OrthoDB; 675117at2759; -.
DR   Proteomes; UP000000560; Chromosome III.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR   GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
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   2: Evidence at transcript level;
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..649
FT                   /note="Glucan endo-1,3-beta-glucosidase btgC"
FT                   /id="PRO_0000395128"
FT   TOPO_DOM        1..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..649
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        452
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        551
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        369
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        596
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   649 AA;  68963 MW;  8476F1DF5B3F1D93 CRC64;
     MGDRSEQYGD IPPISSQHRM HGYGNNGEPA AMPGDGQQNW GSGPGIAHTH SMRTASTATP
     GMDNLGPSAV GGGISGIALG VANTHDRQSG IDAFRDADAT LGYIPAERGY HTTGADNPYV
     PSPPSVGPGP DESSEGLRSH ETFGSSAALS AAGAPAGNWT PPSGSRHSFL DGSYQGVASG
     PYQRHSAYSS QDYPADINPD DILDDGDDGF AAAPSNKPNA AGGAATGGAA GGLLGEFFGA
     KKAADASYDP VPGAGLPSVE KYAKPRPSGA SRKRGWIIGG ILAFIVIGAI VGGAVGGTLG
     NRRSETASES SEVSADDDTE TNGDLDKNSD EIKSLMAMEG LHKVFPGMDY TPWGVQHPEC
     DKWPPSQNNV TRDMAVLSRL TNTVRLYGTD CNQTEMVLHA IDRLELTDMK LWLGVWIDTN
     TTTNERQLSQ LYDILDKRSD HSVFKGAIIG NEALYRAGST KEEARKNIID YMRQVRKHFN
     DHNIDIKVAT SDLGDNWDET LADATDVVMS NVHPFFGGVE VSKAAGWTWS FWNSHNAPLT
     QGTNKGNIIA EVGWPSGGGN DCGDGANCKD DTSGAVAGVK QMNQFMADWV CPALENGTDY
     FWFEAFDEPW KVKFNKGDEQ WEDKWGLMDP GRNLKPGIEI PDCGGKTAA
//