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Database: UniProt
Entry: A0A2V1C599_9HELO
LinkDB: A0A2V1C599_9HELO
Original site: A0A2V1C599_9HELO 
ID   A0A2V1C599_9HELO        Unreviewed;       755 AA.
AC   A0A2V1C599;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glycoside hydrolase family 89 protein {ECO:0000313|EMBL:PVH80836.1};
GN   ORFNames=DL98DRAFT_531858 {ECO:0000313|EMBL:PVH80836.1};
OS   Cadophora sp. DSE1049.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiales incertae sedis; Cadophora.
OX   NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH80836.1, ECO:0000313|Proteomes:UP000244409};
RN   [1] {ECO:0000313|EMBL:PVH80836.1, ECO:0000313|Proteomes:UP000244409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE1049 {ECO:0000313|EMBL:PVH80836.1,
RC   ECO:0000313|Proteomes:UP000244409};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(2018).
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DR   EMBL; KZ804143; PVH80836.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V1C599; -.
DR   STRING; 1485229.A0A2V1C599; -.
DR   Proteomes; UP000244409; 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; 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.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PVH80836.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244409};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..755
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015885323"
FT   DOMAIN          24..109
FT                   /note="Alpha-N-acetylglucosaminidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12971"
FT   DOMAIN          124..460
FT                   /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF05089"
FT   DOMAIN          469..733
FT                   /note="Alpha-N-acetylglucosaminidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12972"
SQ   SEQUENCE   755 AA;  85234 MW;  20EBEECD2EB8F11C CRC64;
     MLLSRCFVWL TRTVGALSAL STKGIEDLVR RRLPAHVDDL EFRLLDGGTS TVGNDVYSVS
     SLDDGRILVE GNTLSALSSG LHRYLTDAMH VDIWWFIGSR LDVGPETLPM LDVSMNGSSI
     IPWRYHFNTV TFSYTTAFWT WEDWELELDW LALRGVNLPL AWVGYEKILV EVYRELGMTD
     TEILSFFSGP AYQSWNRFGN IQGSWNSELP MAWIDGQSEL QKNITRRMVE LGMTPVLPCF
     TGFVPAAIRR VLPNAMVVNG SNWGGLPVEY TNVTFLQPLD PVFSMIQKSF ISEQTAMYGN
     ITHIYTLDQY NENNPESGDL EYLRSVSHNT WQSLKAADPN AVWMMQGWLF FALSSFWTEE
     RIEAYLGGVE SDEDMLIIDI FSESAPQWQR TNSYFGKPWI WCQLHNFGGN MGLYGQVENV
     TVNPIEALAA SSSLVGFGLT MEAQEGNEIM YDLLLDQAWS ESPINTESYF HNWVTRRYSG
     TGDIPAEVYT AWDMMRTTVY NNTNSSIVAV TKSIFELSPN ISNMVHLQGP DGPHSTITAY
     NPATLTSAWN LLFDASKSNP KLWDNPAYQY DMTDITRQVF SNAFIDIYTS LINVYTSANS
     TNATLSSIGT NLTAQLRTLD SVLSTNSAFS LATYLSEARS SSENATLQSF FLKDLRNQIT
     LWGPNGELND YASKSWGGLV NSYYVPRWEI FIEYLRAVPF QRYNETELKS ELRDFERGWV
     NGRGNETTMQ RAQVAAGLSD VLEQAAGRWN GVFGK
//
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