BTGC_ASPFC
ID BTGC_ASPFC Reviewed; 688 AA.
AC B0Y429;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 57.
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=AFUB_056310;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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; DS499597; EDP51620.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y429; -.
DR SMR; B0Y429; -.
DR EnsemblFungi; EDP51620; EDP51620; AFUB_056310.
DR VEuPathDB; FungiDB:AFUB_056310; -.
DR HOGENOM; CLU_011476_0_1_1; -.
DR Proteomes; UP000001699; 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 Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..688
FT /note="Probable glucan endo-1,3-beta-glucosidase btgC"
FT /id="PRO_0000395122"
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..688
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Polar residues"
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..363
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 688 AA; 72692 MW; D7B4BE06E954BF51 CRC64;
MSGPNRTYSF GEGDDGLAHP SSRTHAMHSQ YDDVSPISDG ARMNPMNGQG MDHGLASVLE
DGRQGWGRSP EPSPSLLTGS SATPGMDNLG PGAVGGGISG IALSVANSHD RLSGVEALMG
TDGQEANIPA ERGLSTTGSD NPYVPEPPEY RYSYGSNIAL GAAAAPAGQL TPGQSVSHLS
STNPSQRNLY DIPYQDVGGL NAGPYQRHSA YSSNDLPVDI NPDEIVDDGD DGFVPAPNSG
SGARKSQAIP AAAGGAAAGG VLGNLGGLFG GKSAADTSYG PVPGAGLEAG EKGRWVKPKP
GGGNKKRGWI VGAILAFIII GAIVGGAVGG TIGHRGNEEP SSASSASSSS TQTATEDTSV
NGDLDKNSAE IKALMNNKNL HKVFPGIDYT PWGVQYPLCL KYPPSQNNVT RDMAVLTQLT
NNVRLYGTDC NQTEMVLHAI DKLEIKDMKI WLGVWIDSNE TTSRRQIDQL YKIIDDAKDI
SIFNGAIVGN EALYRAGSDK TSAQTTLINY MQEVKDHFKK KNIDLPVATS DLGDNWDATL
VQAADVVMAN VHPFFGGIPV DQAAAWTWRF WQDHNVALTK GTNKKQIISE VGWPSGGGND
CGQGANCPND TAGAVAGVDE LNKFMEDWVC QALDNGTDYF WFEAFDEPWK IVYNTGKENW
EDKWGLMDSA RNLKPGLKIP DCGGKTAT
