ID A0A2S4XU31_9ACTN Unreviewed; 681 AA.
AC A0A2S4XU31;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Hyaluronidase {ECO:0000313|EMBL:POX40048.1};
GN ORFNames=C3486_15450 {ECO:0000313|EMBL:POX40048.1};
OS Streptomyces sp. Ru73.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080748 {ECO:0000313|EMBL:POX40048.1, ECO:0000313|Proteomes:UP000236956};
RN [1] {ECO:0000313|EMBL:POX40048.1, ECO:0000313|Proteomes:UP000236956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru73 {ECO:0000313|EMBL:POX40048.1,
RC ECO:0000313|Proteomes:UP000236956};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) 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:POX40048.1}.
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DR EMBL; PQSQ01000029; POX40048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4XU31; -.
DR OrthoDB; 9760892at2; -.
DR Proteomes; UP000236956; Unassembled WGS sequence.
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; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.58.460; Hyaluronidase post-catalytic domain-like; 1.
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; 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; 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:UP000236956}.
FT DOMAIN 71..207
FT /note="Beta-hexosaminidase bacterial type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02838"
FT DOMAIN 214..525
FT /note="Beta-N-acetylglucosaminidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF07555"
FT DOMAIN 546..635
FT /note="NagJ-like helical"
FT /evidence="ECO:0000259|Pfam:PF21774"
FT REGION 9..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 73348 MW; 623D2CB206F0D322 CRC64;
MSEACQRFRH RLRPALGRPR SRSSPHPGGH VTALARPLTG SLAVLLAAAT LGAAPPDGTR
PEPAAERQLP VISPTPQHMS RVADDVRLGG RAEVVVGKDT DAAARQLLTR TLRAHGVRDI
DVTTRAGHHA PLTLLLGPAG RADIAAALRG TDVPDHAEGY ALRVAGRRSG QATVALGGTD
AAGQYYAVQT LRGLITKGRI AGAAVSDHPN MPLRGTIEGF YGSPWTNEER LDQMDFLGDV
KANTYVYAPK DDPYHREKWR DPYPADKLDQ LGRLVKRATA HHVRFTFAVS PGNSICYSDP
ADTKALTAKL QSMYDLGVRS FSVPLDDISY TKWNCAGDEK KFGAPGRGPA AEAQVGLLNT
VQRDFIATHD GTHPLQMVPT EYGDLTDTAY KQKLRSTLDK GIEVMWTGTE VVPSGITNDQ
ASKAAELFGR KVFVWDNYPV NDYGQTAGRL LLAPYDKREA GLSDHLSGIV SNPMNQEAAS
KLAVFTIADF AWNDRGYDVR RSARQSALHL AGGDPRVADA VQTFVDLNHL APTFGPTPWQ
PQSPVLSARL AAFWKAYDTD PKAALKQLRP TVDGIAEAPA VLRAGVPDKL FLHDADRWLD
ATALWGSAMR HGLATLTAVQ NDDSARAAKE RAAMDADAIA AGKITSDPAE TRPHGPVKIG
DPFIGDFLAK VREIQDAATE G
//
