ID   EGLX_ASPCL              Reviewed;         639 AA.
AC   A1C7B5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Probable endo-1,3(4)-beta-glucanase ACLA_073210;
DE            EC=3.2.1.6;
DE   AltName: Full=Mixed-linked glucanase ACLA_073210;
DE   Flags: Precursor;
GN   ORFNames=ACLA_073210;
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: 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; DS027045; EAW14286.1; -; Genomic_DNA.
DR   RefSeq; XP_001275712.1; XM_001275711.1.
DR   AlphaFoldDB; A1C7B5; -.
DR   SMR; A1C7B5; -.
DR   PRIDE; A1C7B5; -.
DR   EnsemblFungi; EAW14286; EAW14286; ACLA_073210.
DR   GeneID; 4708021; -.
DR   KEGG; act:ACLA_073210; -.
DR   VEuPathDB; FungiDB:ACLA_073210; -.
DR   eggNOG; ENOG502QUM3; Eukaryota.
DR   HOGENOM; CLU_016972_4_0_1; -.
DR   OMA; CANFAAG; -.
DR   OrthoDB; 754530at2759; -.
DR   Proteomes; UP000006701; 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; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..617
FT                   /note="Probable endo-1,3(4)-beta-glucanase ACLA_073210"
FT                   /id="PRO_0000395082"
FT   PROPEP          618..639
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395083"
FT   DOMAIN          26..290
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          337..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        146
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        151
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   LIPID           617
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   639 AA;  65108 MW;  5CF35BA52DF084C0 CRC64;
     MAPSSLLLSV GSLIASSLAS ATSLQIREQS QSYQLTESWQ GESFINDWNF FDRGDPTNGY
     VTYVNQSVAE SSGLVKVTQS GSFYMGVDYE SKLNPDGPGR ESVRIESKKY YTQGLYVVDI
     AHMPGSICGT WPAFWSVGAN WPHDGEIDII EGVNKHDANE IVLHTSGSCD VAGSHDMTGS
     LTSGECGDAS GTIGCVVKGT QGSAGDPFNA QGGGVYAIEW TDSFLKIWFF PRNSIPASIT
     AGKPDSSAFG TPMAHLQGTC DFAERFKEQK FILDTTFCGD WAGNVFGESG CPLSDASSPM
     RSCVDYVAQN PAAFKEAYWE INSIKIYQLG AAPAPATVAS PNTASEVHSA SELAPATQTE
     KPTVPTAAET TVVPPASQTS TVAEETPIAP LATAATVTAV NPAPPATQPT AEPATAVTVT
     DGGDSFRTIF LTSTTTICPE AQSSSSAAAH GGNKNAPVGA VPGQPSGADA VGNPNPSTTT
     EAVAETETSQ PELTAGGISE LPKSAPAPTA SQPTSEFKPS DVPDVPKPSP EAEHPAPPAA
     AGSSIINTPS SSAIFGSSTA VGTFTSLARV SRPTGGATFV PTIATATGSP TVGEDGSSGS
     ATASATLTAP TGILFTAGAR KLSVGLSGLV GALAVAALA