ID   EGLX_ASPFN              Reviewed;         667 AA.
AC   B8N7S7;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=Probable endo-1,3(4)-beta-glucanase AFLA_105200;
DE            EC=3.2.1.6;
DE   AltName: Full=Mixed-linked glucanase AFLA_105200;
DE   Flags: Precursor;
GN   ORFNames=AFLA_105200;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ963475; EED53146.1; -; Genomic_DNA.
DR   RefSeq; XP_002376392.1; XM_002376351.1.
DR   AlphaFoldDB; B8N7S7; -.
DR   SMR; B8N7S7; -.
DR   EnsemblFungi; EED53146; EED53146; AFLA_105200.
DR   VEuPathDB; FungiDB:AFLA_006449; -.
DR   eggNOG; ENOG502QUM3; Eukaryota.
DR   HOGENOM; CLU_016972_4_0_1; -.
DR   OMA; FYMGVDY; -.
DR   OrthoDB; 1932445at2759; -.
DR   Proteomes; UP000001875; 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   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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..644
FT                   /note="Probable endo-1,3(4)-beta-glucanase AFLA_105200"
FT                   /id="PRO_0000395086"
FT   PROPEP          645..667
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395087"
FT   DOMAIN          25..288
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          354..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..500
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        144
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        149
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   LIPID           644
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        63
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   667 AA;  68433 MW;  6FA9DBFF4C651501 CRC64;
     MSSSSFVWTV GSIALSSLIT PTIADGSGSR YQLTEAWQGE KFLDHFKFFS GSDPTNGFVT
     YANQSYAESS GLIEVTESGS FYMGVDYKTK LSPNGPGRDS VRIESKEYYD EGLYIIDLQH
     MPGSVCGTWP AFWSVGPNWP YDGEIDIIEG VNKHEANEIV LHTSGSCSLS SENDMSGTMS
     SSECGESSGT IGCVVKGQTG TSGAPFNEKN GGVYAMEWTS SFVKIWYFAR SEIPQSITEG
     NPDTTAFGTP MAHLQGTCDF GERFKSQKFI LDTTFCGDWA GGVFGDSGCP VSDPSNPIQS
     CVNYVAENPA AFKEAYWEIN YIKLFQTGTG HSTASIASQA ETATAVVSKT VDSVPSVTST
     PILETTAPAP ETVSAEAPAT SSAVPEPANP QTSVAGAETT AAPAPSPETT AAPASPSSDD
     SEGADAVSET TIYVTETTTI CGASTQKGTI QTIGGGETEV SPASSTVESA ATPAAPTPTS
     QEPVASLPGT TVNDGTPVPT DVSPETPAEE TAGESGAPTP SAEQPEKPQP AATSIETGIV
     PPPVSNPAPT EQGTPEGASP VDATESRHVP DEPAPTSAAP IRSPSPSSWT ISSSSRVALS
     SSFASTTSSA SRTTSATKEA TAPTETDSGA STGTNPESPV FTAGASKSVG ISGLAGIVCG
     IAMAMLA
//