BTGC_ASPTN
ID BTGC_ASPTN Reviewed; 655 AA.
AC Q0CI96;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 25-MAY-2022, entry version 59.
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=ATEG_06588;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SEQUENCE CAUTION:
CC Sequence=EAU33132.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAU33132.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CH476602; EAU33132.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001215766.1; XM_001215766.1.
DR AlphaFoldDB; Q0CI96; -.
DR SMR; Q0CI96; -.
DR STRING; 341663.Q0CI96; -.
DR EnsemblFungi; EAU33132; EAU33132; ATEG_06588.
DR GeneID; 4322381; -.
DR eggNOG; ENOG502QTKT; Eukaryota.
DR OrthoDB; 1163530at2759; -.
DR Proteomes; UP000007963; 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..655
FT /note="Probable glucan endo-1,3-beta-glucosidase btgC"
FT /id="PRO_0000395127"
FT TOPO_DOM 1..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..655
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 458
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 557
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 655 AA; 69420 MW; C2560B77C3B3CAC5 CRC64;
MSGDPRSFSF NQGDDHPIDS SQQPLHPTNT MADSYSDRNW GAPGGLDHTH SMRTQSTATP
GMDNLGPAAV GGGISGIALG VANSHDRQSG VDAFRDTDGG NFPAERGYNA PGSDNPYVPP
PPAAAYDSSD NLTARSGAYG SSAALAAAAS APAGASNTSR RSFVDSPYQG VGALDAGPYQ
RQSVYNNGDY PLVINPDEII DDGDDGFALP NSKSAGHKSR AVPAAAAGAA GGAAAGGLLG
GIFKSKAAAE GPSYGPVPGA GIEAAEKGQW AKPKPGTGSR KRGWIVGIIL AVVIVGAIVG
GAVGGTLGNR EKESPSSSET ASGDEKVNGD LGKDSDEIKS LMNNPNLHKV FPGMDYTPWG
TQYPLCQKYP PSQNNVTRDI AVLSQLTNTV RLYGTDCNQT EMVLHAIDRL ELTEMKLWLG
VWIDTNKTTC ERQLNQLYDV LDKTKDHSIF KGAIIGNEAL YRAGSSIAEA EKTLISYMTE
VRDHFKKNNI NIPIATSDLG DNWNAELVKA SDVVMANVHP FFAGVSVDLA ASWTWDFWNN
HNLVLTKGTD KKQIISEVGW PSGGGNDCGD GGNCPNDSAG SVAGIDEMNQ FMSDWVCQAL
DNGTDYFWFE AFDEPWKIVY NTKNENWEDK WGLMDPARNL KDGLKIPDCG GKTAT
