BTGC_ASPCL
ID BTGC_ASPCL Reviewed; 695 AA.
AC A1CAI0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, 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=ACLA_011750;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027049; EAW12748.1; -; Genomic_DNA.
DR RefSeq; XP_001274174.1; XM_001274173.1.
DR AlphaFoldDB; A1CAI0; -.
DR SMR; A1CAI0; -.
DR STRING; 344612.A1CAI0; -.
DR EnsemblFungi; EAW12748; EAW12748; ACLA_011750.
DR GeneID; 4706510; -.
DR KEGG; act:ACLA_011750; -.
DR VEuPathDB; FungiDB:ACLA_011750; -.
DR eggNOG; ENOG502QTKT; Eukaryota.
DR HOGENOM; CLU_011476_0_1_1; -.
DR OMA; PLNTQYP; -.
DR OrthoDB; 1163530at2759; -.
DR Proteomes; UP000006701; 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..695
FT /note="Probable glucan endo-1,3-beta-glucosidase btgC"
FT /id="PRO_0000395121"
FT TOPO_DOM 1..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 318..338
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..695
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 498
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT ACT_SITE 597
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O22317"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 695 AA; 74031 MW; FD2BC27323310650 CRC64;
MSGPHRTFSF EQRGDGEAHS SFMDHAMHPQ YDDVSPISNM SSSPGHMNET HHGLASVPED
NHQGWGQARG PSPSNRTGFT ATPEMDNLGP ASVGGGISGI ALGVANSHDR LSGVEARRGT
DGQEANIPAE RGYNTTGSDN PYIPAPPDMG GYGSSETLHP RQSYGSNVAL GAAAGPAGQL
TPGHSATHLG TSNSSQRNLY DAPYQSAGGL SAGPYQRHSA YSSNDLPLDI NPEEIADDGD
DGFAPAGNSR SSARRSQAVP AAAGGAAAGG VLGGIGGLFN NRNPAETSYD PVPGAGLEAG
EKSQWVKPKP STGSRKRGWI IGAILAVIII GAIVGGAVGG TIGHKDSGDS ASGSSASTQS
ASGDTDTNGD LDKNSAEIKA LMNNKDLHKV FPGMDYTPWG VQYPLCLKYP PSQNNVTRDM
AVLAQLTNNV RLYGTDCNQT EMVLHAIDKL DLKDMKVWLG VWIDTNETTS RRQIDQLYKI
VDDAKDISIF NGAIVGNEAL FRAGDNKITA QATLTKYMQE VRDHFKKHDI KMPIATSDLG
DNWNAELVQI ADVVMSNVHP FFGGIPVDQA AAWTWRFWQD HDVILTQGTD KRQVISEVGW
PSGGGNDCGK GANCPDDTSG AVAGIDELNK FMEDWVCQAL DNGTDYFWFE AFDEPWKIEF
NTKNENWEDK WGLMDPARKL KSGLKIPDCG GKTAA
