BTGC_NEOFI
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 25-MAY-2022, entry version 70.
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 / NRRL 181
RC / 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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; PLNTQYP; -.
DR OrthoDB; 1163530at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
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: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 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..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
