ID   BTGC_ASPFN              Reviewed;         685 AA.
AC   B8NTP7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   03-MAY-2023, entry version 63.
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=AFLA_099780;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963484; EED46314.1; -; Genomic_DNA.
DR   RefSeq; XP_002383850.1; XM_002383809.1.
DR   AlphaFoldDB; B8NTP7; -.
DR   SMR; B8NTP7; -.
DR   STRING; 332952.B8NTP7; -.
DR   GlyCosmos; B8NTP7; 4 sites, No reported glycans.
DR   VEuPathDB; FungiDB:AFLA_010218; -.
DR   eggNOG; ENOG502QTKT; Eukaryota.
DR   OrthoDB; 675117at2759; -.
DR   Proteomes; UP000001875; 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   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN           1..685
FT                   /note="Probable glucan endo-1,3-beta-glucosidase btgC"
FT                   /id="PRO_0000395123"
FT   TOPO_DOM        1..312
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..685
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..92
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        488
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        587
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   CARBOHYD        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        632
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   685 AA;  72800 MW;  CBCDFB8987DF725B CRC64;
     MSGPHRSFSF NQGDDGAGDA GDVSPIRSQE GHFMNSPPRH NDVSPVSARS QAMGSSPSSG
     FLSAHEHGDR GWGQNSGHTQ AMRTNSTTPG MDNLGPAAVG GGISGIALGV ANSHNRQSGI
     DAFRDTDGRN LPAERGYNTT GSDNPYVPTP PGGGSHGSAE NLRPRDSYGS NVALGAAAAP
     AGQLTPGGSN PSQRSLFDSP YQGVGAMDAG PYQRQSAYSA AGDYPLVINP DEIADDGDDG
     FTPVPNGKSA SSNARAIPAA AAGGAAGGGL FGLFKSKKAD NPSYGPVPGA GLEAGEKSRW
     VKPTPGGGSR KRGWIVGLAL AFIVVGAIVG GAVGGTLGNR ENEAPDTTKS ASSDTESNGD
     LNKDSSEIKD LMNNPDLHKV FPGMDYTPWG VQYPLCLKYP PSQNNVTRDV AVLSQLTNTV
     RLYGTDCNQT EMVLHAIDRL ELKDMKVWLG VWIDSNDTTN DRQIKQLYKV LDDTKDISIF
     KGAIVGNEAL YRAGNDIASA KKKLISYMDD VRNHFKEKNY DLPIATSDLG DNWKEDLVTA
     TDLVMSNVHP FFAGVTAKEA AGWTWNFWNQ NDVPLTKGTN KKQVISEVGW PSGGGNDCGS
     NNKCTDDTSG SVAGIDEMNQ FMSDWICQAL ENGTDYFWFE AFDEPWKVQY NTKDENWEDK
     WGLMDAARKL KPGLKIPDCG GKTAA
//