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   13-SEP-2023, entry version 61.
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   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
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=CBS 144.89 / FGSC A1163 / CEA10;
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
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   CDD; cd02181; GH16_fungal_Lam16A_glucanase; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   PANTHER; PTHR10963:SF58; ENDO-1,3(4)-BETA-GLUCANASE XGEA; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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
//