EGLX_ASPFC
ID EGLX_ASPFC Reviewed; 652 AA.
AC B0XTU6;
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 endo-1,3(4)-beta-glucanase AFUB_029980;
DE EC=3.2.1.6;
DE AltName: Full=Mixed-linked glucanase AFUB_029980;
DE Flags: Precursor;
GN ORFNames=AFUB_029980;
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: Mixed-linked glucanase involved in the degradation of complex
CC natural cellulosic substrates. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans
CC when the glucose residue whose reducing group is involved in the
CC linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; DS499595; EDP54938.1; -; Genomic_DNA.
DR AlphaFoldDB; B0XTU6; -.
DR SMR; B0XTU6; -.
DR EnsemblFungi; EDP54938; EDP54938; AFUB_029980.
DR VEuPathDB; FungiDB:AFUB_029980; -.
DR HOGENOM; CLU_016972_4_0_1; -.
DR PhylomeDB; B0XTU6; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Cellulose degradation;
KW Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..630
FT /note="Probable endo-1,3(4)-beta-glucanase AFUB_029980"
FT /id="PRO_0000395084"
FT PROPEP 631..652
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395085"
FT DOMAIN 36..289
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT REGION 379..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 630
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 652 AA; 65993 MW; B2A3477AC381AB33 CRC64;
MAPSSLLLSV GSLITSSLVS ATALEARQSQ TYQLAESWQG ESFINDWNFF DGADPTNGYV
TYVNQSFAKQ SGLVKVTESG SFYMGVDYES TLNPNGAGRE SVRIESKNYY TEGLYVIDIE
HMPGSICGTW PAFWSVGKNW PNDGEIDIIE GVNLQKANKI VLHTSGSCDV SGSNDMTGTL
SSSECGEASG TVGCVVKGTN GSSGDPFNES GGGVYAMEWT DTFIKIWFFP RSQIPASLAS
GNPDTSSFGT PMAHLQGSCD FAERFKAQKL IIDTTFCGDW AGNVFAESTC PMSDPSSPMQ
SCVNYVAQNP AAFKEAYWEI NSIKIYQYGV SAASSAAVSQ ATASKVEGTR VSAQAANTAT
PTVPAPVETT TVPQPAQTNT VATSAADHAT PSSAETTTVP AATGAPSVSA TEGGDSELES
TSTVYVTSTT TICPVAESSS AAAAGGKEDA PSNGTSGAEV AATSVAAAAP AAATSGHPGA
DAIANSAAAT STDAQSESAT SRLTAGALSE IPTAPPEPVS QAVSTGSFDD SDTAQGDSEE
QGSIASASVA PSTIPVPASS SAAALGGSSI ASSFASSRLI PRPTGSSTAA SATAIATWSP
TAGESASGTA KESATLTTPS EVFFTPGLSN GANRMSVGLS GLIGVMFIAA LA
