ID   EGLX_NEOFI              Reviewed;         651 AA.
AC   A1DHY9;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Probable endo-1,3(4)-beta-glucanase NFIA_089530;
DE            EC=3.2.1.6;
DE   AltName: Full=Mixed-linked glucanase NFIA_089530;
DE   Flags: Precursor;
GN   ORFNames=NFIA_089530;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
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; DS027696; EAW18996.1; -; Genomic_DNA.
DR   RefSeq; XP_001260893.1; XM_001260892.1.
DR   AlphaFoldDB; A1DHY9; -.
DR   SMR; A1DHY9; -.
DR   STRING; 36630.CADNFIAP00007826; -.
DR   EnsemblFungi; EAW18996; EAW18996; NFIA_089530.
DR   GeneID; 4587451; -.
DR   KEGG; nfi:NFIA_089530; -.
DR   VEuPathDB; FungiDB:NFIA_089530; -.
DR   eggNOG; ENOG502QUM3; Eukaryota.
DR   HOGENOM; CLU_016972_4_0_1; -.
DR   OMA; ILNINFC; -.
DR   OrthoDB; 754530at2759; -.
DR   Proteomes; UP000006702; 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..629
FT                   /note="Probable endo-1,3(4)-beta-glucanase NFIA_089530"
FT                   /id="PRO_0000395095"
FT   PROPEP          630..651
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395096"
FT   DOMAIN          36..289
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          364..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..404
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..557
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           629
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"
SQ   SEQUENCE   651 AA;  66035 MW;  0DD6CA7D45C885A8 CRC64;
     MAPSSLFLSV GSLIASSLVS ATALEARQSQ TYQLAESWQG ESFINDWNFF DRADPTNGYV
     TYVNQSFAEQ SGLVKVTQSG SFYMGVDYES TLNPNGPGRE SVRIETKNYY TEGLYVIDIE
     HMPGSICGTW PAFWSVGKDW PNDGEIDIIE GVNLQKANKI VLHTSGSCDV SGSNDMTGTL
     SSSECGEASG TVGCVVKGTN GSSGDPFNEA GGGVYAMEWT DTFIKIWFFP RSQIPASLSS
     GNPDTSSFGT PMAHLQGSCD FAERFKAQKF IIDTTFCGDW AGNVFAESTC PMSDPSSPMQ
     SCVNYVAQNP AAFKEAYWEI NSIKVYQYGV SAASSAAVSQ ATASKVEGTL VSVQAANTAT
     PTVPVPAETT AVPQPAQTNT VATSAADYAT QSSAETTTVP AATGAPSVSA AEGGDSELES
     TSTVYVTSTT TICPVAESSS AAAAGGKKDA PFNGVSGAEV AATSVAAAPA AATSEHPGAD
     AIANSAAATS TVAKSEGVAS QLTAGALSEI PTAPPEPVSQ AVSTGSFDDS DTAQGDSEEH
     GSIASASAAP STIPVPASSS AAALGGSSIA SSFASSRLVP RPTGSSTAAS VTAIATWSPT
     AGERASGTAK GSATLTAPSE VVFTPGLSNG ANRMSVGLSG LIGVMFIAAL A