ID   A0A2M9JWJ7_9ACTN        Unreviewed;       794 AA.
AC   A0A2M9JWJ7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Hyaluronidase {ECO:0000313|EMBL:PJN11229.1};
GN   ORFNames=CG723_09815 {ECO:0000313|EMBL:PJN11229.1};
OS   Streptomyces sp. CB01635.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN11229.1, ECO:0000313|Proteomes:UP000232157};
RN   [1] {ECO:0000313|Proteomes:UP000232157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA   Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA   Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA   Shen B.;
RT   "Discovery of the Leinamycin Family of Natural Products by Mining
RT   Actinobacterial Genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN11229.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NNBL01000003; PJN11229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9JWJ7; -.
DR   OrthoDB; 9760892at2; -.
DR   Proteomes; UP000232157; Unassembled WGS sequence.
DR   GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IEA:UniProt.
DR   GO; GO:0042806; F:fucose binding; 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   GO; GO:0010185; P:regulation of cellular defense response; IEA:UniProt.
DR   GO; GO:0001868; P:regulation of complement activation, lectin pathway; 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; IPR006585; FTP1.
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; 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   SMART; SM00607; FTP; 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.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000232157};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..794
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039134933"
FT   DOMAIN          646..792
FT                   /note="Fucolectin tachylectin-4 pentraxin-1"
FT                   /evidence="ECO:0000259|SMART:SM00607"
SQ   SEQUENCE   794 AA;  85890 MW;  53BE2C83ABC36376 CRC64;
     MTARRALHAC SVATLLVAAS AAAVPPVSAH APDHRLPVVS PTPQHMTRAG ADVALPSRAE
     LVVGDTTDKP ARDLLTATLR AHGVRHVDVR TKASGHAPLT VLLGPATRPD VAKALRGTDV
     PTQDEGYAVR VAGRTVALGG TDATGQFYAA QTFGQLVTKG KIAGASVSDF PSMRLRGSIE
     GFYGPPWTEA ERLDQMDFLG EVKSNTYVYA PKDDPYHRDK WREPYPADKL AQLGTLVDRA
     RTNHVRFTFA VSPGGSVCYS DPADVKALTA KLQALYDLGV RSFSVPLDDI SYTKWNCDAD
     QQKFGAPGRG PAAKAQVGLL NTVQQDFIAT HDGANPLQMV PTEYGDLTDT AYKQEIRGNL
     DKNIEVMWTG TDVVPREITN DQAQKASELF GRKVFVWDNY PVNDFGRTSG RLLLAPYDKR
     EPGLSEHLSG LVSNPMNQEA ASKLAVFTMS DFSWNDRGYD RTRSARQSAL HLAGGDARVA
     DAVQTFVDLN HMAPTFGAEP WQPQSPILSA QLEKFWKAYA SDPTAAIRAF TPTAANIGRI
     PAVLRAGVPD QQFLHDAGPW LDSTALWGKA LGHGLAALKA IDAHDADRAA GERAAMEKAA
     DAASHITIDP AEHHQPGPVK IADPFLGDFV SQVQDLHDAS KGLEPLRQLA LNKDTKQSSD
     YASDGEFPYS AAKAADGDRF NFSTTSGKEA QPWWQVDLGS VADLERVDVY NRSDCCADRT
     KDYYVLVSDE PFTGTLADQL TKPGVWSHHE TAQAGGPTAI PVTAHGHYVR VWLASEKPVE
     LNMAEVEVYG RARS
//