RecName: Full=Tricorn protease homolog
List of domain hits
Name | Accession | Description | Interval | E-value | |||||||||||||||
COG4946 | COG4946 | Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
63-1068 | 0e+00 | |||||||||||||||
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown]; : Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 670.21 E-value: 0e+00
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Name | Accession | Description | Interval | E-value | |||||||||||||||
COG4946 | COG4946 | Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
63-1068 | 0e+00 | |||||||||||||||
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown]; Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 670.21 E-value: 0e+00
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Peptidase_S41_TRI | cd07562 | Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ... |
696-1066 | 1.21e-92 | |||||||||||||||
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 peptidase family and named for its tricorn-like shape, exists only in some archaea and eubacteria. It has been shown to act as a carboxypeptidase, involved in the degradation of proteasomal products to preferentially yield di- and tripeptides, with subsequent and final degradations to free amino acid residues by tricorn interacting factors, F1, F2 and F3. Tricorn is a hexameric D3-symmetric protease of 720kD, and can self-associate further into a giant icosahedral capsid structure containing twenty copies of the complex. Each tricorn peptidase monomer consists of five structural domains: a six-bladed beta-propeller and a seven-bladed beta-propeller that limit access to the active site, the two domains (C1 and C2) that carry the active site residues, and a PDZ-like domain (proposed to be important for substrate recognition) between the C1 and C2 domains. The active site tetrad residues are distributed between the C1 and C2 domains, with serine and histidine on C1 and serine and glutamate on C2. Pssm-ID: 143478 [Multi-domain] Cd Length: 266 Bit Score: 296.42 E-value: 1.21e-92
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TSPc | smart00245 | tail specific protease; tail specific protease |
853-1043 | 6.46e-40 | |||||||||||||||
tail specific protease; tail specific protease Pssm-ID: 214582 Cd Length: 192 Bit Score: 146.25 E-value: 6.46e-40
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Tricorn_PDZ | pfam14685 | Tricorn protease PDZ domain; This domain is the PDZ domain of tricorn protease. |
773-858 | 1.69e-32 | |||||||||||||||
Tricorn protease PDZ domain; This domain is the PDZ domain of tricorn protease. Pssm-ID: 405386 [Multi-domain] Cd Length: 88 Bit Score: 121.15 E-value: 1.69e-32
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Name | Accession | Description | Interval | E-value | |||||||||||||||
COG4946 | COG4946 | Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
63-1068 | 0e+00 | |||||||||||||||
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown]; Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 670.21 E-value: 0e+00
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Peptidase_S41_TRI | cd07562 | Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 ... |
696-1066 | 1.21e-92 | |||||||||||||||
Tricorn protease; serine protease family S41; The tricorn protease (TRI), a member of the S41 peptidase family and named for its tricorn-like shape, exists only in some archaea and eubacteria. It has been shown to act as a carboxypeptidase, involved in the degradation of proteasomal products to preferentially yield di- and tripeptides, with subsequent and final degradations to free amino acid residues by tricorn interacting factors, F1, F2 and F3. Tricorn is a hexameric D3-symmetric protease of 720kD, and can self-associate further into a giant icosahedral capsid structure containing twenty copies of the complex. Each tricorn peptidase monomer consists of five structural domains: a six-bladed beta-propeller and a seven-bladed beta-propeller that limit access to the active site, the two domains (C1 and C2) that carry the active site residues, and a PDZ-like domain (proposed to be important for substrate recognition) between the C1 and C2 domains. The active site tetrad residues are distributed between the C1 and C2 domains, with serine and histidine on C1 and serine and glutamate on C2. Pssm-ID: 143478 [Multi-domain] Cd Length: 266 Bit Score: 296.42 E-value: 1.21e-92
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CtpA | COG0793 | C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
699-1063 | 5.98e-55 | |||||||||||||||
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440556 [Multi-domain] Cd Length: 341 Bit Score: 194.70 E-value: 5.98e-55
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TSPc | smart00245 | tail specific protease; tail specific protease |
853-1043 | 6.46e-40 | |||||||||||||||
tail specific protease; tail specific protease Pssm-ID: 214582 Cd Length: 192 Bit Score: 146.25 E-value: 6.46e-40
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Tricorn_PDZ | pfam14685 | Tricorn protease PDZ domain; This domain is the PDZ domain of tricorn protease. |
773-858 | 1.69e-32 | |||||||||||||||
Tricorn protease PDZ domain; This domain is the PDZ domain of tricorn protease. Pssm-ID: 405386 [Multi-domain] Cd Length: 88 Bit Score: 121.15 E-value: 1.69e-32
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cpPDZ_Tricorn-protease | cd10828 | circularly permuted PDZ domain of Tricorn protease, and related proteins; permuted PDZ (PSD-95 ... |
772-860 | 4.75e-32 | |||||||||||||||
circularly permuted PDZ domain of Tricorn protease, and related proteins; permuted PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Tricorn protease, and related domains. The tricorn protease can degrade oligopeptides (which may have been generated by the proteasome) and channel the products to F1, F2 and F3 proteases which, in turn, catalyze the terminal degradation step yielding free amino acids. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. The tricorn family PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus. Pssm-ID: 467628 [Multi-domain] Cd Length: 93 Bit Score: 120.12 E-value: 4.75e-32
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Peptidase_S41 | pfam03572 | Peptidase family S41; |
887-1042 | 3.24e-30 | |||||||||||||||
Peptidase family S41; Pssm-ID: 460977 Cd Length: 165 Bit Score: 117.32 E-value: 3.24e-30
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Peptidase_S41 | cd06567 | C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing ... |
888-1043 | 6.89e-27 | |||||||||||||||
C-terminal processing peptidase family S41; Peptidase family S41 (C-terminal processing peptidase or CTPase family) contains very different subfamilies; it includes photosystem II D1 C-terminal processing protease (CTPase), interphotoreceptor retinoid-binding protein IRBP and tricorn protease (TRI). CTPase and TRI both contain the PDZ domain while IRBP, although being very similar to the tail-specific protease domain, lacks the PDZ insertion domain and hydrolytic activity. These serine proteases have distinctly different active sites: in CTPase, the active site consists of a serine/lysine catalytic dyad while in tricorn core protease, it is a tetrad (serine, histidine, serine, glutamate). CPases with different substrate specificities in different species include processing of D1 protein of the photosystem II reaction center in higher plants and cleavage of a peptide of 11 residues from the precursor form of penicillin-binding protein; and others such as tricorn protease (TRI) act as a carboxypeptidase, involved in the degradation of proteasomal products. CTPase homolog IRBP, secreted by photoreceptors into the interphotoreceptor matrix, having arisen in the early evolution of the vertebrate eye, promotes the release of all-trans retinol from photoreceptors and facilitates its delivery to the retinal pigment epithelium. Pssm-ID: 143475 [Multi-domain] Cd Length: 224 Bit Score: 109.69 E-value: 6.89e-27
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Tricorn_C1 | pfam14684 | Tricorn protease C1 domain; This domain is the C1 core domain of tricorn protease. This is a ... |
694-762 | 1.29e-25 | |||||||||||||||
Tricorn protease C1 domain; This domain is the C1 core domain of tricorn protease. This is a mixed alpha-beta domain. Pssm-ID: 434126 [Multi-domain] Cd Length: 70 Bit Score: 100.72 E-value: 1.29e-25
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Peptidase_S41_IRBP | cd07563 | Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor ... |
820-1064 | 1.64e-11 | |||||||||||||||
Interphotoreceptor retinoid-binding protein; serine protease family S41; Interphotoreceptor retinoid-binding protein (IRBP) is a homolog of the S41 protease, C-terminal processing peptidase (CTPase) family. It is thought to facilitate the compartmentalization of the visual cycle that requires poorly soluble and potentially toxic retinoids to cross the aqueous subretinal space between the photoreceptors and the retinal pigment epithelium (RPE). IRBP is secreted by photoreceptors into the interphotoreceptor matrix (IPM) where it is rapidly turned over by a combination of RPE and photoreceptor endocytosis. It is the most abundant soluble protein component of the IPM, consisting of homologous modules, each repeat structure arising through the duplication (as in teleost IRBP) or quadruplication (in tetrapods) of an ancient gene, arisen in the early evolution of the vertebrate eye. IRBP has been shown to promote the release of all-trans retinol from photoreceptors and facilitates its delivery to the RPE. Conversely, IRBP can promote the release of 11-cis-retinal from the RPE, prevent its isomerization in the subretinal space, and transfer it to photoreceptors. In vivo evidence implicates IRBP as a retinoid transporter in the visual cycle, suggesting a critical role for IRBP in cone function essential for human vision. IRBP is a dominant autoimmune antigen in the eye; IRBP proteolysis analysis has proven a useful biomarker for autoimmune uveitis (AU) disorders, a major cause of blindness. This family also includes a chlamydia-secreted protein, designated chlamydia protease-like activity factor (CPAF), known to degrade host proteins, enabling Chlamydia to evade host defenses and replicate. Pssm-ID: 143479 [Multi-domain] Cd Length: 250 Bit Score: 65.78 E-value: 1.64e-11
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TolB | COG0823 | Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
82-287 | 2.15e-09 | |||||||||||||||
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 57.37 E-value: 2.15e-09
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TolB | COG0823 | Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
409-527 | 1.07e-08 | |||||||||||||||
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 55.45 E-value: 1.07e-08
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TolB | COG0823 | Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
68-143 | 3.17e-07 | |||||||||||||||
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 51.21 E-value: 3.17e-07
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TolB | COG0823 | Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
230-322 | 9.79e-07 | |||||||||||||||
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 49.67 E-value: 9.79e-07
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TolB | COG0823 | Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
434-526 | 2.29e-06 | |||||||||||||||
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 48.51 E-value: 2.29e-06
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TolB | COG0823 | Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
63-145 | 5.09e-06 | |||||||||||||||
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 47.74 E-value: 5.09e-06
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TolB | COG0823 | Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
258-395 | 1.99e-05 | |||||||||||||||
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 45.82 E-value: 1.99e-05
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TolB | COG0823 | Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
495-530 | 3.59e-04 | |||||||||||||||
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport]; Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 42.35 E-value: 3.59e-04
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PD40 | pfam07676 | WD40-like Beta Propeller Repeat; This family appears to be related to the pfam00400 repeat. ... |
498-522 | 1.28e-03 | |||||||||||||||
WD40-like Beta Propeller Repeat; This family appears to be related to the pfam00400 repeat. This repeat corresponds to the RIVW repeat identified in cell surface proteins [Adindla et al. Comparative and Functional Genomics 2004; 5:2-16]. Pssm-ID: 429587 [Multi-domain] Cd Length: 37 Bit Score: 37.50 E-value: 1.28e-03
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Sortilin-Vps10 | pfam15902 | Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, ... |
226-278 | 4.17e-03 | |||||||||||||||
Sortilin, neurotensin receptor 3,; Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1. Pssm-ID: 464929 [Multi-domain] Cd Length: 444 Bit Score: 41.03 E-value: 4.17e-03
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Blast search parameters | ||||
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