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Database: UniProt
Entry: A0A2H3J9R3_WOLCO
LinkDB: A0A2H3J9R3_WOLCO
Original site: A0A2H3J9R3_WOLCO 
ID   A0A2H3J9R3_WOLCO        Unreviewed;       749 AA.
AC   A0A2H3J9R3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Glycoside hydrolase family 89 protein {ECO:0000313|EMBL:PCH34408.1};
GN   ORFNames=WOLCODRAFT_160854 {ECO:0000313|EMBL:PCH34408.1};
OS   Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phaeolaceae; Wolfiporia.
OX   NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH34408.1, ECO:0000313|Proteomes:UP000218811};
RN   [1] {ECO:0000313|EMBL:PCH34408.1, ECO:0000313|Proteomes:UP000218811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MD-104 {ECO:0000313|EMBL:PCH34408.1,
RC   ECO:0000313|Proteomes:UP000218811};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
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DR   EMBL; KB467831; PCH34408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3J9R3; -.
DR   STRING; 742152.A0A2H3J9R3; -.
DR   OMA; YGQPFVW; -.
DR   OrthoDB; 1112009at2759; -.
DR   Proteomes; UP000218811; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PCH34408.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218811};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..749
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013776515"
FT   DOMAIN          26..107
FT                   /note="Alpha-N-acetylglucosaminidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12971"
FT   DOMAIN          122..459
FT                   /note="Alpha-N-acetylglucosaminidase tim-barrel"
FT                   /evidence="ECO:0000259|Pfam:PF05089"
FT   DOMAIN          468..744
FT                   /note="Alpha-N-acetylglucosaminidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12972"
SQ   SEQUENCE   749 AA;  82959 MW;  1B49CAF1DE2E36DF CRC64;
     MQGNFLLLVG VLGALLVDAA TTSLDGIYSL VQRQIPQHQN SFTFALIEGD GDSFVISDTH
     GDSGGITIEC TTVSACARGL YTYVTRYGGV DIWWTGSRLN QLASPLPSVG EPVNGSAIVE
     YRYHFNTVTF DYTAAFWAFD QWSSELDWLA LRGVNLPLAW VGYEYILIEV FRDAGLTDAE
     IASFLSGSAF QAWNRFGNIQ GSWGGDLPTQ WVNDQFALNQ QIVARMVELG MTPVLPAFTG
     FVPRAMARVY PNASIVNGSQ WGGFPADLTD VSFLEPFDDL FATLQMSFIS KQQAAYGNAT
     HIYTLDQYNE NSPYSGDTAY LYNISLYTFD SMRAADPEAV WMMQGWLFFA DESFWTADRI
     AAYLGGVENN DDMIVLDLYS EAAPQWQRTN SYYGKQWIWC ELHDYGGNMG FEGNLPVLST
     DPLEALYSSG SSMKGMGLTM EGQEGNEIVY DFLLDQAWSP TSLDITSYVE AWVARRYPIS
     NLPSAAQTAW GILSTTVYSN SNSDTQATIK SIFELAPSTS GLVNLTGHHP TEIPYNTNTT
     IVPALTNLTL AATQNPTLLT VPEFAYDLVD VVRQLLANRF IDAYEALITE YDSSSATAAS
     VTSAGQPLLD ILTILDTLLW TNENFLLSTW IADARALAGS NATYADYLEY NARNQITLWG
     PDGEINDYAS KQWAGLVGTY YLDRWQTFIT YLADIKHNGT AYDNTAIQAQ LLDIGKEWDT
     QIWGQQAGES WDVVGDVMTV VNDIVQKWI
//
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