ID A0A100I3X0_ASPNG Unreviewed; 429 AA.
AC A0A100I3X0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Endo-1,3(4)-beta-glucanase {ECO:0000313|EMBL:GAQ33625.1};
GN ORFNames=ABL_00263 {ECO:0000313|EMBL:GAQ33625.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ33625.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609};
CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane
CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ33625.1}.
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DR EMBL; BCMY01000001; GAQ33625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100I3X0; -.
DR SMR; A0A100I3X0; -.
DR VEuPathDB; FungiDB:An01g04560; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1131906; -.
DR VEuPathDB; FungiDB:ATCC64974_19610; -.
DR VEuPathDB; FungiDB:M747DRAFT_263997; -.
DR OMA; NGPNWPE; -.
DR Proteomes; UP000068243; 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:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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:SF24; GLYCOSIDASE C21B10.07-RELATED; 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 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00022622};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00022622}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007087128"
FT DOMAIN 17..282
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 316..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..379
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 45847 MW; 7CAE8DC57FB591F6 CRC64;
MRRTATLLSA LGLTAQLSSA AYTLQDDYSG DSFFDGFTFF TGADPTNGFV DYVDEATAQS
NGYISTSGDA PVYMGVDHTN IAGSSGRQSV RISSDATYNH GLFILDLGHM PGGVCGTWPA
FWLVGADWPN NGEIDIIEGV NQQSGNDMTL HTSDGCSVSS SADFTGSMTT SNCYVSAAGQ
SNNAGCGITD PDGTSYGTAF NANNGGVFAT EWTSDAISIW FFERGSIPDD IDSGNPDPDS
WGSPVARFQG DCDIDAHFDS LQIIFDTTFC GDWAGNVWGS GSCASVASSC SDYVANNPEA
FAEAYWIINS LKVYQDDGDD DDTVAGVVDY GDDEDDDDND NSDDDDSDDD DDSDDDDDDS
DSDDDSDDDD DDNDDDDDDE SRPWRGGGGG RNRHGPKLYA STSTSSFPSP SFMRKAKWER
RNPMAGMIF
//
