Peptidase M-like protein [Bacteroides thetaiotaomicron VPI-5482]
Protein Classification
BACON and ZnMc_pappalysin_like domain-containing protein( domain architecture ID 11606315)
BACON and ZnMc_pappalysin_like domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| metzin_BF0631 super family | cl26140 | zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family ... |
103-406 | 4.36e-119 | ||||||
zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family are zinc-dependent metalloproteinases, related to ulilysin and other members of the pappalysin family. Members occur as predicted lipoproteins and occur mostly in the genera Bacteriodes and Prevotella. [Protein fate, Degradation of proteins, peptides, and glycopeptides] The actual alignment was detected with superfamily member TIGR03952: Pssm-ID: 274876 Cd Length: 351 Bit Score: 351.01 E-value: 4.36e-119
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| BACON | cd14948 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
30-111 | 3.47e-19 | ||||||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. : Pssm-ID: 271342 [Multi-domain] Cd Length: 83 Bit Score: 81.54 E-value: 3.47e-19
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| Name | Accession | Description | Interval | E-value | ||||||
| metzin_BF0631 | TIGR03952 | zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family ... |
103-406 | 4.36e-119 | ||||||
zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family are zinc-dependent metalloproteinases, related to ulilysin and other members of the pappalysin family. Members occur as predicted lipoproteins and occur mostly in the genera Bacteriodes and Prevotella. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 274876 Cd Length: 351 Bit Score: 351.01 E-value: 4.36e-119
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| ZnMc_pappalysin_like | cd04275 | Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ... |
124-397 | 2.45e-67 | ||||||
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved. Pssm-ID: 239802 [Multi-domain] Cd Length: 225 Bit Score: 213.74 E-value: 2.45e-67
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| BACON | cd14948 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
30-111 | 3.47e-19 | ||||||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. Pssm-ID: 271342 [Multi-domain] Cd Length: 83 Bit Score: 81.54 E-value: 3.47e-19
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| Peptidase_M43 | pfam05572 | Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ... |
277-396 | 7.27e-09 | ||||||
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a metallo-protease belonging to Merops family M43. It cleaves insulin-like growth factor (IGF) binding protein-4 (IGFBP-4), causing a dramatic reduction in its affinity for IGF-I and -II. Through this mechanism, PAPP-A is a regulator of IGF bioactivity in several systems, including the human ovary and the cardiovascular system. Pssm-ID: 368506 Cd Length: 152 Bit Score: 54.54 E-value: 7.27e-09
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| BACON | pfam13004 | Putative binding domain, N-terminal; The BACON (Bacteroidetes-Associated Carbohydrate-binding ... |
55-112 | 1.02e-06 | ||||||
Putative binding domain, N-terminal; The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, PDB:3ZMR, has found no evidence for carbohydrate-binding for this domain. Pssm-ID: 432932 [Multi-domain] Cd Length: 61 Bit Score: 45.58 E-value: 1.02e-06
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| Name | Accession | Description | Interval | E-value | ||||||
| metzin_BF0631 | TIGR03952 | zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family ... |
103-406 | 4.36e-119 | ||||||
zinc-dependent metalloproteinase lipoprotein, BF0631 family; Members of this protein family are zinc-dependent metalloproteinases, related to ulilysin and other members of the pappalysin family. Members occur as predicted lipoproteins and occur mostly in the genera Bacteriodes and Prevotella. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 274876 Cd Length: 351 Bit Score: 351.01 E-value: 4.36e-119
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| ZnMc_pappalysin_like | cd04275 | Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma ... |
124-397 | 2.45e-67 | ||||||
Zinc-dependent metalloprotease, pappalysin_like subfamily. The pregnancy-associated plasma protein A (PAPP-A or pappalysin-1) cleaves insulin-like growth factor-binding proteins 4 and 5, thereby promoting cell growth by releasing bound growth factor. This model includes pappalysins and related metalloprotease domains from all three kingdoms of life. The three-dimensional structure of an archaeal representative, ulilysin, has been solved. Pssm-ID: 239802 [Multi-domain] Cd Length: 225 Bit Score: 213.74 E-value: 2.45e-67
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| BACON | cd14948 | Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The ... |
30-111 | 3.47e-19 | ||||||
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain; The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes. Pssm-ID: 271342 [Multi-domain] Cd Length: 83 Bit Score: 81.54 E-value: 3.47e-19
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| Peptidase_M43 | pfam05572 | Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a ... |
277-396 | 7.27e-09 | ||||||
Pregnancy-associated plasma protein-A; Pregnancy-associated plasma protein A (PAPP-A) is a metallo-protease belonging to Merops family M43. It cleaves insulin-like growth factor (IGF) binding protein-4 (IGFBP-4), causing a dramatic reduction in its affinity for IGF-I and -II. Through this mechanism, PAPP-A is a regulator of IGF bioactivity in several systems, including the human ovary and the cardiovascular system. Pssm-ID: 368506 Cd Length: 152 Bit Score: 54.54 E-value: 7.27e-09
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| BACON | pfam13004 | Putative binding domain, N-terminal; The BACON (Bacteroidetes-Associated Carbohydrate-binding ... |
55-112 | 1.02e-06 | ||||||
Putative binding domain, N-terminal; The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, PDB:3ZMR, has found no evidence for carbohydrate-binding for this domain. Pssm-ID: 432932 [Multi-domain] Cd Length: 61 Bit Score: 45.58 E-value: 1.02e-06
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| ZnMc_MMP_like | cd04268 | Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix ... |
254-361 | 2.02e-03 | ||||||
Zinc-dependent metalloprotease, MMP_like subfamily. This group contains matrix metalloproteinases (MMPs), serralysins, and the astacin_like family of proteases. Pssm-ID: 239796 [Multi-domain] Cd Length: 165 Bit Score: 38.63 E-value: 2.02e-03
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| ZnMc_MMP_like_2 | cd04276 | Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase ... |
277-313 | 3.00e-03 | ||||||
Zinc-dependent metalloprotease; MMP_like sub-family 2. A group of bacterial metalloproteinase domains similar to matrix metalloproteinases and astacin. Pssm-ID: 239803 Cd Length: 197 Bit Score: 38.85 E-value: 3.00e-03
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| ZnMc_serralysin_like | cd04277 | Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases ... |
274-353 | 3.34e-03 | ||||||
Zinc-dependent metalloprotease, serralysin_like subfamily. Serralysins and related proteases are important virulence factors in pathogenic bacteria. They may be secreted into the medium via a mechanism found in gram-negative bacteria, that does not require n-terminal signal sequences which are cleaved after the transmembrane translocation. A calcium-binding domain c-terminal to the metalloprotease domain, which contains multiple tandem repeats of a nine-residue motif including the pattern GGxGxD, and which forms a parallel beta roll may be involved in the translocation mechanism and/or substrate binding. Serralysin family members may have a broad spectrum of substrates each, including host immunoglobulins, complement proteins, cell matrix and cytoskeletal proteins, as well as antimicrobial peptides. Pssm-ID: 239804 [Multi-domain] Cd Length: 186 Bit Score: 38.55 E-value: 3.34e-03
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