ID   W2SX78_NECAM            Unreviewed;       474 AA.
AC   W2SX78;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN   ORFNames=NECAME_13181 {ECO:0000313|EMBL:ETN74143.1};
OS   Necator americanus (Human hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae; Bunostominae;
OC   Necator.
OX   NCBI_TaxID=51031 {ECO:0000313|EMBL:ETN74143.1, ECO:0000313|Proteomes:UP000053676};
RN   [1] {ECO:0000313|Proteomes:UP000053676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24441737; DOI=10.1038/ng.2875;
RA   Tang Y.T., Gao X., Rosa B.A., Abubucker S., Hallsworth-Pepin K., Martin J.,
RA   Tyagi R., Heizer E., Zhang X., Bhonagiri-Palsikar V., Minx P., Warren W.C.,
RA   Wang Q., Zhan B., Hotez P.J., Sternberg P.W., Dougall A., Gaze S.T.,
RA   Mulvenna J., Sotillo J., Ranganathan S., Rabelo E.M., Wilson R.K.,
RA   Felgner P.L., Bethony J., Hawdon J.M., Gasser R.B., Loukas A., Mitreva M.;
RT   "Genome of the human hookworm Necator americanus.";
RL   Nat. Genet. 46:261-269(2014).
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}.
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DR   EMBL; KI660385; ETN74143.1; -; Genomic_DNA.
DR   RefSeq; XP_013296370.1; XM_013440916.1.
DR   AlphaFoldDB; W2SX78; -.
DR   STRING; 51031.W2SX78; -.
DR   EnsemblMetazoa; NECAME_13181; NECAME_13181; NECAME_13181.
DR   GeneID; 25353209; -.
DR   KEGG; nai:NECAME_13181; -.
DR   CTD; 25353209; -.
DR   OMA; KEFSCQC; -.
DR   OrthoDB; 2883747at2759; -.
DR   Proteomes; UP000053676; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053676}.
FT   DOMAIN          332..343
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS00022"
SQ   SEQUENCE   474 AA;  53784 MW;  F238F7229007781F CRC64;
     MTQMDSFPVY WNVPSKVCHS RKIDIPLQEF GIIHNRGHEF QGDQIVIFYE YNFGYFPYYI
     DYDADQPVNG GLPQNCPLDK HLALVSKQIR EAIPREDFNG IAVIDFEEWR PLYQLNWGKK
     AVYKAESLRL VREQFPSISG KSAEALAKKE FNTAAKKIFL STIGLARQLR PYARWGFYGF
     PYCNYDAGNS ESDMLCNEKF RKYNDEMSFI FEASSALFPS IYLSLKGTSA QNYRYIQAIM
     VESARIAALQ NPILDVYPYT KFEYNPYQSL DSFYAKKDVC NSLKQAADLG ARGIVLWSSS
     KNMKQRCEGL AKYVQDMLGP CTFRMQPSNY VCRCDPLFTG NNCLRRKHFK WIYNIGPKTS
     TNSSNIAKGN RRSGRRKKLK KIRFIKVSGD AGKETEDGRP ASAEAIVVAV ATPASRNTDE
     IGPSLATMKS TTLSGMSTNV KFANPFIATH TPPDVTTPDA VFRLTPPPLD FRLV
//