hyaluronidase HylP [Streptococcus pyogenes]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Hyaluronidase_1 super family | cl06307 | Hyaluronidase protein (HylP); This family consists of several phage associated hyaluronidase ... |
65-337 | 0e+00 | |||||
Hyaluronidase protein (HylP); This family consists of several phage associated hyaluronidase proteins (EC:3.2.1.35) which seem to be specific to Streptococcus pyogenes and Streptococcus pyogenes bacteriophages. The substrate of hyaluronidase is hyaluronic acid, a sugar polymer composed of alternating N-acetylglucosamine and glucuronic acid residues. Hyaluronic acid is found in the ground substance of human connective tissue and the vitreous of the eye and also is the sole component of the capsule of group A streptococci. The capsule has been shown to be an important virulence factor of this organizm by virtue of its ability to resist phagocytosis. Production by S. pyogenes of both a hyaluronic acid capsule and hyaluronidase enzymatic activity capable of destroying the capsule is an interesting, yet-unexplained, phenomenon. The actual alignment was detected with superfamily member pfam07212: Pssm-ID: 429352 Cd Length: 273 Bit Score: 542.11 E-value: 0e+00
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| Mtd_N super family | cl47266 | Major tropism determinant N-terminal domain; This is the N-terminal domain of major tropism ... |
9-45 | 8.18e-06 | |||||
Major tropism determinant N-terminal domain; This is the N-terminal domain of major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein. Mtd-N forms a three-fold symmetric beta-prism. This resembles the pseudo three-fold-symmetric beta-prisms of monocot lectins, but lacks residues in these lectins identified as binding carbohydrates. The beta-prism and beta-sandwich domains reinforce overall trimeric assembly and therefore may have indirect roles in stabilizing the backbone of the variable region. The actual alignment was detected with superfamily member pfam18454: Pssm-ID: 436514 [Multi-domain] Cd Length: 37 Bit Score: 42.07 E-value: 8.18e-06
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| Name | Accession | Description | Interval | E-value | |||||
| Hyaluronidase_1 | pfam07212 | Hyaluronidase protein (HylP); This family consists of several phage associated hyaluronidase ... |
65-337 | 0e+00 | |||||
Hyaluronidase protein (HylP); This family consists of several phage associated hyaluronidase proteins (EC:3.2.1.35) which seem to be specific to Streptococcus pyogenes and Streptococcus pyogenes bacteriophages. The substrate of hyaluronidase is hyaluronic acid, a sugar polymer composed of alternating N-acetylglucosamine and glucuronic acid residues. Hyaluronic acid is found in the ground substance of human connective tissue and the vitreous of the eye and also is the sole component of the capsule of group A streptococci. The capsule has been shown to be an important virulence factor of this organizm by virtue of its ability to resist phagocytosis. Production by S. pyogenes of both a hyaluronic acid capsule and hyaluronidase enzymatic activity capable of destroying the capsule is an interesting, yet-unexplained, phenomenon. Pssm-ID: 429352 Cd Length: 273 Bit Score: 542.11 E-value: 0e+00
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| Mtd_N | pfam18454 | Major tropism determinant N-terminal domain; This is the N-terminal domain of major tropism ... |
9-45 | 8.18e-06 | |||||
Major tropism determinant N-terminal domain; This is the N-terminal domain of major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein. Mtd-N forms a three-fold symmetric beta-prism. This resembles the pseudo three-fold-symmetric beta-prisms of monocot lectins, but lacks residues in these lectins identified as binding carbohydrates. The beta-prism and beta-sandwich domains reinforce overall trimeric assembly and therefore may have indirect roles in stabilizing the backbone of the variable region. Pssm-ID: 436514 [Multi-domain] Cd Length: 37 Bit Score: 42.07 E-value: 8.18e-06
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| Name | Accession | Description | Interval | E-value | |||||
| Hyaluronidase_1 | pfam07212 | Hyaluronidase protein (HylP); This family consists of several phage associated hyaluronidase ... |
65-337 | 0e+00 | |||||
Hyaluronidase protein (HylP); This family consists of several phage associated hyaluronidase proteins (EC:3.2.1.35) which seem to be specific to Streptococcus pyogenes and Streptococcus pyogenes bacteriophages. The substrate of hyaluronidase is hyaluronic acid, a sugar polymer composed of alternating N-acetylglucosamine and glucuronic acid residues. Hyaluronic acid is found in the ground substance of human connective tissue and the vitreous of the eye and also is the sole component of the capsule of group A streptococci. The capsule has been shown to be an important virulence factor of this organizm by virtue of its ability to resist phagocytosis. Production by S. pyogenes of both a hyaluronic acid capsule and hyaluronidase enzymatic activity capable of destroying the capsule is an interesting, yet-unexplained, phenomenon. Pssm-ID: 429352 Cd Length: 273 Bit Score: 542.11 E-value: 0e+00
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| Mtd_N | pfam18454 | Major tropism determinant N-terminal domain; This is the N-terminal domain of major tropism ... |
9-45 | 8.18e-06 | |||||
Major tropism determinant N-terminal domain; This is the N-terminal domain of major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein. Mtd-N forms a three-fold symmetric beta-prism. This resembles the pseudo three-fold-symmetric beta-prisms of monocot lectins, but lacks residues in these lectins identified as binding carbohydrates. The beta-prism and beta-sandwich domains reinforce overall trimeric assembly and therefore may have indirect roles in stabilizing the backbone of the variable region. Pssm-ID: 436514 [Multi-domain] Cd Length: 37 Bit Score: 42.07 E-value: 8.18e-06
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