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Database: UniProt
Entry: B8N0I3_ASPFN
LinkDB: B8N0I3_ASPFN
Original site: B8N0I3_ASPFN 
ID   B8N0I3_ASPFN            Unreviewed;       813 AA.
AC   B8N0I3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Glycosyl hydrolase, putative {ECO:0000313|EMBL:EED55155.1};
GN   ORFNames=AFLA_024260 {ECO:0000313|EMBL:EED55155.1};
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 {ECO:0000313|EMBL:EED55155.1, ECO:0000313|Proteomes:UP000001875};
RN   [1] {ECO:0000313|EMBL:EED55155.1, ECO:0000313|Proteomes:UP000001875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC   SRRC 167 {ECO:0000313|Proteomes:UP000001875};
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; EQ963473; EED55155.1; -; Genomic_DNA.
DR   RefSeq; XP_002373937.1; XM_002373896.1.
DR   AlphaFoldDB; B8N0I3; -.
DR   STRING; 332952.B8N0I3; -.
DR   EnsemblFungi; EED55155; EED55155; AFLA_024260.
DR   VEuPathDB; FungiDB:AFLA_000268; -.
DR   eggNOG; KOG2230; Eukaryota.
DR   HOGENOM; CLU_005015_2_4_1; -.
DR   OMA; AWPNLHW; -.
DR   UniPathway; UPA00280; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052761; F:exo-1,4-beta-D-glucosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR043534; EBDG/EBM.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR041351; Ig_GlcNase.
DR   InterPro; IPR041447; Mannosidase_ig.
DR   PANTHER; PTHR43536; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR   PANTHER; PTHR43536:SF1; MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   Pfam; PF18368; Ig_GlcNase; 1.
DR   Pfam; PF17786; Mannosidase_ig; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EED55155.1}.
FT   DOMAIN          33..137
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          158..258
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          608..690
FT                   /note="Mannosidase Ig/CBM-like"
FT                   /evidence="ECO:0000259|Pfam:PF17786"
FT   DOMAIN          702..805
FT                   /note="Exo-beta-D-glucosaminidase Ig-fold"
FT                   /evidence="ECO:0000259|Pfam:PF18368"
SQ   SEQUENCE   813 AA;  92037 MW;  DBCD0DC1A3E8DF2E CRC64;
     MAGLIQNHVY NDTHLFYSNN LATVDQTIFR APWLYREELR LLAPPKGQHM FLITHGITSK
     ADIYFNGKQI ASNATQQGSY GGHRYDITPF VRTGKNVLLI QAHPTNYLRD FAQGFVDWNP
     YPPDNGTGVW RDVELKQTGP VSMSSPRILT DFIGVHTENV TATIKVDIKN HEDRIANGVV
     HGTVQAQDKG SQTVAFSKQF KLEPYKNATV SIDVVLKNPK IWWPATWGKQ PLYTVKAKTT
     VGQNEISDIA PPTQFGIRHV TSKLNSYNDT EFSVNGYPFH VRGGGYSPDM FLRFDLEHLR
     NIFRYMLDMG LNTVRLEGKQ EHPELYDLAD RMGLMVMSGW ECCDKWEGWK YNNEANGVKW
     TEKDYPIAET TMLHEAEMMQ AHPSMLAFLI GSDFWPDEKA TNVYVNALNR MDWPNPIIAS
     ASKRGYPKLL GPSGMKMDGP YDWVPPNYWY HDKLGAAFGF GSEQGPGVGT PELGSLQQFM
     SAQELESLWM KPEQPQWHMA KNDSPFADRS LYNEGLFARY GPPTGLEDYL RKSQMSDYEG
     TRAEFEAFAI RQNASRPATG VVYWMLNGAW PSLHWQLFDY YLRPAGSYFG TKVGARLEHV
     AYDYEAHTVH IINHSLKNFG KRNVTVDLID LNGTSMHHES IATYTTPTSS KQVATVPEIN
     KIKDVGFLRL TLKDSVKGTT ISRNVYWLPP NTESLDWDNS TFYTTPVTKY TDLTALNKMP
     AANVSTSMKM TVSKHGSTFG EVTLENKSDV PAFFMHLTVS DENGHELAPV YWSDNYVTLF
     PREKLILTVE FQGRKWAATL SGANVEKRGI GRS
//
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