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Database: UniProt
Entry: A0A1R1SJD1_9ACTN
LinkDB: A0A1R1SJD1_9ACTN
Original site: A0A1R1SJD1_9ACTN 
ID   A0A1R1SJD1_9ACTN        Unreviewed;      1004 AA.
AC   A0A1R1SJD1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Putative hyaluronidase {ECO:0000313|EMBL:OMI38384.1};
GN   ORFNames=SPAR_16282 {ECO:0000313|EMBL:OMI38384.1};
OS   Streptomyces sparsogenes DSM 40356.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI38384.1, ECO:0000313|Proteomes:UP000186168};
RN   [1] {ECO:0000313|EMBL:OMI38384.1, ECO:0000313|Proteomes:UP000186168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI38384.1,
RC   ECO:0000313|Proteomes:UP000186168};
RA   Coyne S., Seebeck F.P.;
RT   "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL   Submitted (MAY-2013) 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:OMI38384.1}.
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DR   EMBL; ASQP01000235; OMI38384.1; -; Genomic_DNA.
DR   RefSeq; WP_065959405.1; NZ_ASQP01000235.1.
DR   AlphaFoldDB; A0A1R1SJD1; -.
DR   STRING; 67365.GCA_001704635_04659; -.
DR   Proteomes; UP000186168; 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; 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:UP000186168};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1004
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5010359006"
FT   DOMAIN          864..1001
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          14..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          865..906
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1004 AA;  106219 MW;  8892C5E0DCD6F5B8 CRC64;
     MAAAVIGGLL GAAPGAAAAP GAPTAPGASA TDRESDGGLP PVWPRPQSLR AQGAGVSVGR
     EVTLVADAAS DPYALDALRA LLHDAGARVV NEATEPTPKG MPLADGLVVR VGGRGAERAL
     RALDAPERGD LPSGGYRLAT GQVSGKPTVA LSGVGPDGLF HAVQTLRRLM VRPDGGTGTF
     PGVAVRDWPA AAVRGTTEGF YGRPWSHRDR LAHLDFMGRT KQNRYLYAPG DDPYRQARWR
     DPYPAERREQ FRELADRARR NHVTLAWAVS PGQELCFSSA DDLKALLRKV DAMWALGVRA
     FQLQFQDVSY SEWHCGADAD TFGSGPEAAA KAQARVAGAV AAHLAARHPG AAPLSLLPTE
     YYQDGDTDFR RALAERLDPD VEVAWTGVGV VPKTITGAEL AGARAVFGHA LVTMDNYPVN
     DYAQDRVFLG PYEGRDPAVA GRSAALLANA MEQPVASRVA LFTAADFAWN PRGYRPQESW
     RAAVDDLAGP DPRTRAALRA LAGNDASSVL GGEESAYLRP LIEAFWTALS GETGKPGQTG
     KPGAGGERLD RAADRLRSAF RTMRDAPDRL SATLGEELGP WLDQLGRYGD AGVRAVDMLT
     AQARGDGAAG WRGRTAVQEL WEKIAESRVT VGKGVLAPFL KQALARADAW VGLDGADRAS
     LRTSKDLRAA ADGDATTSVT ADDPVTVRFD RARPLTAVSA LTGRAAASPG TVEAHVPGTG
     WRRLGAVSGS GWTQLAGRGL RADALRLTWA AGATPPAMHE ITPWFADSPA AELRLSREAV
     DVEAGGRAAV VEARVTARRP EDVHDELTVH APRGVRVTAD EAVTAPRGGT ATARIELSVP
     AGTRTGTFTV PVRFGSQERV LTVRAVPPTG GPDLARADGA TATSSGDETP DFPASAAIDG
     DPATRWSSPA EDEAWLRLEL ARPARVGRLD LHWQDAYASR YRVQVSADGR TWRTAATVSD
     GRGGHETVRM DAPGTRFIRV EGVERATRFG YSLWSVSAYG VTED
//
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