ID A0A3A3A010_9EURO Unreviewed; 751 AA.
AC A0A3A3A010;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Alpha-N-acetylglucosaminidase {ECO:0000313|EMBL:RJE22651.1};
GN ORFNames=PHISCL_04995 {ECO:0000313|EMBL:RJE22651.1};
OS Aspergillus sclerotialis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Polypaecilum.
OX NCBI_TaxID=2070753 {ECO:0000313|EMBL:RJE22651.1, ECO:0000313|Proteomes:UP000266188};
RN [1] {ECO:0000313|Proteomes:UP000266188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 366.77 {ECO:0000313|Proteomes:UP000266188};
RA Tafer H., Lopandic K.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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:RJE22651.1}.
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DR EMBL; MVGC01000157; RJE22651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A3A010; -.
DR STRING; 2070753.A0A3A3A010; -.
DR Proteomes; UP000266188; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.120.670; N-acetyl-b-d-glucoasminidase; 1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR029018; Hex-like_dom2.
DR InterPro; IPR007781; NAGLU.
DR InterPro; IPR024732; NAGLU_C.
DR InterPro; IPR024240; NAGLU_N.
DR InterPro; IPR024733; NAGLU_tim-barrel.
DR PANTHER; PTHR12872; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR12872:SF1; ALPHA-N-ACETYLGLUCOSAMINIDASE; 1.
DR Pfam; PF05089; NAGLU; 1.
DR Pfam; PF12972; NAGLU_C; 1.
DR Pfam; PF12971; NAGLU_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000266188};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..751
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017432494"
FT DOMAIN 26..113
FT /note="Alpha-N-acetylglucosaminidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12971"
FT DOMAIN 128..464
FT /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT /evidence="ECO:0000259|Pfam:PF05089"
FT DOMAIN 472..731
FT /note="Alpha-N-acetylglucosaminidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12972"
SQ SEQUENCE 751 AA; 86054 MW; 2C592EFC1E7A2CD3 CRC64;
MRFLSALFVF LFAILAWSAQ AHSTEGITRL LERRLPNHVD NFTFSLTDPA RPSDDWVNDE
YTVSTSSDGK IHIEGNSLSG ILQGLHRYLA DIVHVDIWWY IGNRLDVAPA ELPSISEPMK
GTSAIPWRYQ LNTVTFSYVA AFWQWEDWEL ELDWMAMRGV NLPLAWVGYE KILIEVLRET
GFTDEDIHDF LSGPAYLAWN RFGNIQGSWS GDLPFDWIDS QFELQKKILA RMIELGMTPV
LPSFTGFVPR SVSSVLPDAE VVNASNWADV DPEYTGVSFL QPFDPYFARM QKSFLKKQLD
AYGNITHFYT LDQYNEMTPS SGDLDFLRKV SKQTMESLKA VDPDATWFMQ GWLFYAAQDF
WSDDRIEAYL SAGEKFHDML ILDLHAESYP VWSRTKSFFG KAWIWCQVHG LGGNMNFYGD
LVNITHGPTE ALASSPGLVG VGNANEGQSD EIMFNVLLDQ GWSKTPLDTK RYFRNFVTAR
YSGGRASKRE IPECVYRAWD ILRTTAYSTP NWVNNYIGMT PQPLTGLSPS LDLKEELLYN
QSEIVEAWNL LLEGDLFGDP AYRFDLVQFT RQVLENAFVL TLPKLQSKYK NGAPVSEFMP
IGHKLLLIVQ SMDTVLETEK SLRLSEWISK ARSWGGNDKK LADYFEYNAR DQVTLWVAGQ
SKMLNDYAQK SWGGLVSGYY YPRWSIFINY LKDTPASNYN QTELRDKLFV FESKWVRETS
DSQNRAAESQ KDLKDVLKDL KKNLGDIFDS N
//
