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Database: UniProt
Entry: A0A0F7NDQ4_9ACTN
LinkDB: A0A0F7NDQ4_9ACTN
Original site: A0A0F7NDQ4_9ACTN 
ID   A0A0F7NDQ4_9ACTN        Unreviewed;       902 AA.
AC   A0A0F7NDQ4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Beta-N-acetylhexosaminidase {ECO:0000313|EMBL:AKH85523.1};
GN   ORFNames=AA958_28465 {ECO:0000313|EMBL:AKH85523.1};
OS   Streptomyces sp. CNQ-509.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH85523.1, ECO:0000313|Proteomes:UP000034283};
RN   [1] {ECO:0000313|EMBL:AKH85523.1, ECO:0000313|Proteomes:UP000034283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH85523.1,
RC   ECO:0000313|Proteomes:UP000034283};
RA   Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA   Kalinowski J., Heide L., Kaysser L.;
RT   "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT   of Meroterpenoid Chemistry.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP011492; AKH85523.1; -; Genomic_DNA.
DR   RefSeq; WP_047018757.1; NZ_CP011492.1.
DR   AlphaFoldDB; A0A0F7NDQ4; -.
DR   STRING; 444103.AA958_28465; -.
DR   KEGG; strc:AA958_28465; -.
DR   PATRIC; fig|444103.5.peg.5998; -.
DR   OrthoDB; 9760892at2; -.
DR   Proteomes; UP000034283; Chromosome.
DR   GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   InterPro; IPR049019; NagJ-like_helical.
DR   InterPro; IPR011496; O-GlcNAcase_cat.
DR   PANTHER; PTHR13170; O-GLCNACASE; 1.
DR   PANTHER; PTHR13170:SF16; PROTEIN O-GLCNACASE; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   Pfam; PF07555; NAGidase; 1.
DR   Pfam; PF21774; NagJ_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF140657; Hyaluronidase post-catalytic domain-like; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..902
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039091784"
FT   DOMAIN          642..779
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          24..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..38
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   902 AA;  94565 MW;  B7B5DA25CDE2F943 CRC64;
     MPVPRPAVVG AVLLALGLSP LAAPPAAGAP PPPARAGDIS PTPRSVEARA DGVTVTRTVT
     LVTGPEPDGP ALAVAEKALR DAGAEDVRRT ATAPDEGRGL TVYLGGPDAN PASAAALGAL
     GVEGPAGLPA DGYVLAAGTA EPAGGTPGGD GIVLAGADAS GTYYAAQSLR QLLPHRDSPG
     TRVAGTAVRD WPGTGWRGAI EGFYGVPWSH ASRLDQLSFY GEHKMNIYVY SPKDDPYLRE
     RWREPYPADE LARIAELVER ARANHVEFTY ALSPGLSVCY SSDADVQALN DKFQTLWDIG
     VRTFAVPLDD ISYTDWNCAA DEERFGTGGG AAGAAQAHLL NRVNREFVRT HDGAEPLQMV
     PTEYYDTTPS PYKKALAEQL DEDVLVEWTG IGVVAPVMTV AQARDAREVF GHPILTWDNY
     PVNDYAQQRL LLGPFNGREK GLPGELAGIT ANPMNQAAAS KLALYTVADF AWNDAAYDAR
     ESWAGALAEL AGGDRHTTAA LRAFADASYG SALNPGQAPE LSAAIAAYWD RGGEDALDDA
     LAALEAAPGV LRDRLPDRAF VEESGPWLDA TRDWGTATRT ALRMVEAARD GDGDRAWRLR
     QRLPELVDQA TSHIYTGLGG REVKVVVGEG VLDAFVADAA AAHDRSLGLP PRPKGATNLG
     TYQGNTVDRM TDGDDSTFFW SDGAPRAGSW VSVDLHGERE IGEVGLAMAK SGSPNDYLQQ
     GVLEYSADGE TWQELATFSG TPDVEATAPE GTKARYVRAR STAAQGNWLV VREFTVAGGG
     PATTAGGPPA AEGSSLAAAA DGDTASVYRA ARAPQAGESL DIRFAEPRAA KSLIVLRPQD
     APNAGATVQI RNEPDGPWRT AGTLAGAYTE LRVPGGAVAE VRLRWSGGGA VPQITDVGVA
     GS
//
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