ID A0A016WJU1_9BILA Unreviewed; 300 AA.
AC A0A016WJU1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN Name=Acey_s0637.g946 {ECO:0000313|EMBL:EYC39881.1};
GN ORFNames=Y032_0637g946 {ECO:0000313|EMBL:EYC39881.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC39881.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC Evidence={ECO:0000256|RuleBase:RU610713};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|RuleBase:RU610713}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:EYC39881.1}.
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DR EMBL; JARK01000237; EYC39881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WJU1; -.
DR STRING; 53326.A0A016WJU1; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR PANTHER; PTHR11769; HYALURONIDASE; 1.
DR PANTHER; PTHR11769:SF35; HYALURONIDASE; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycosidase {ECO:0000256|RuleBase:RU610713};
KW Hydrolase {ECO:0000256|RuleBase:RU610713};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT DOMAIN 231..273
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 263..272
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 300 AA; 34243 MW; 640216455EC86F3C CRC64;
MLQANTPKNC VIQRNSIVKV FRNQSIALAR INNIGIHNES EIESIAEKDF NDAARNFFVK
TIQMGRELRP HALWGFYGFP YCNYNAGQNG EYECSKPYRD WNDRMMFIFN ESSALYPSIY
LGFNATSDQR FRYVQAILRE ARRVANKFTP PLPIYAYSKI EYNPLKEIAD FYDTRDLCST
IKQPADLGID GIIFWSSSNN MTLRCPYIKD NMEKVIGPKV RTIISQQDAC GKIRCRSNGK
CVLPTNTTCQ DFNMNTNLYK CECNEGFSGE DCSVQNTDGV AVAPQRSGRS ATLKRVIHLS
//