lipoprotein aminopeptidase LpqL [Mycobacterium tuberculosis variant africanum MAL010102]
Protein Classification
M28 family metallopeptidase( domain architecture ID 10133824)
M28 family metallopeptidase contains aminopeptidases as well as carboxypeptidases that have co-catalytic zinc ions; contains a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||
| M28_SGAP_like | cd03876 | M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ... |
51-482 | 2.11e-137 | |||||||
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures. : Pssm-ID: 349873 [Multi-domain] Cd Length: 289 Bit Score: 397.82 E-value: 2.11e-137
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| PA_SaNapH_like | cd04816 | PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ... |
124-243 | 4.01e-44 | |||||||
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. : Pssm-ID: 240120 [Multi-domain] Cd Length: 122 Bit Score: 151.32 E-value: 4.01e-44
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| Name | Accession | Description | Interval | E-value | |||||||
| M28_SGAP_like | cd03876 | M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ... |
51-482 | 2.11e-137 | |||||||
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures. Pssm-ID: 349873 [Multi-domain] Cd Length: 289 Bit Score: 397.82 E-value: 2.11e-137
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| Peptidase_M28 | pfam04389 | Peptidase family M28; |
252-473 | 5.02e-57 | |||||||
Peptidase family M28; Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 187.88 E-value: 5.02e-57
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| Iap | COG2234 | Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
206-479 | 5.20e-51 | |||||||
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism]; Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 174.55 E-value: 5.20e-51
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| PA_SaNapH_like | cd04816 | PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ... |
124-243 | 4.01e-44 | |||||||
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 240120 [Multi-domain] Cd Length: 122 Bit Score: 151.32 E-value: 4.01e-44
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
69-241 | 1.10e-15 | |||||||
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes. Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 80.47 E-value: 1.10e-15
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| PA | pfam02225 | PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ... |
141-230 | 4.83e-13 | |||||||
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors. Pssm-ID: 460499 [Multi-domain] Cd Length: 91 Bit Score: 64.84 E-value: 4.83e-13
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| PRK10199 | PRK10199 | alkaline phosphatase isozyme conversion aminopeptidase; Provisional |
240-460 | 1.96e-07 | |||||||
alkaline phosphatase isozyme conversion aminopeptidase; Provisional Pssm-ID: 182299 [Multi-domain] Cd Length: 346 Bit Score: 52.82 E-value: 1.96e-07
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| T9SSA_dep_M36 | NF038113 | T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ... |
136-242 | 8.12e-06 | |||||||
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131). Pssm-ID: 468356 [Multi-domain] Cd Length: 868 Bit Score: 48.50 E-value: 8.12e-06
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| Name | Accession | Description | Interval | E-value | |||||||
| M28_SGAP_like | cd03876 | M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family ... |
51-482 | 2.11e-137 | |||||||
M28 Zn-peptidase Streptomyces griseus aminopeptidase and similar proteins; Peptidase family M28; Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30 kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures. Pssm-ID: 349873 [Multi-domain] Cd Length: 289 Bit Score: 397.82 E-value: 2.11e-137
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| Peptidase_M28 | pfam04389 | Peptidase family M28; |
252-473 | 5.02e-57 | |||||||
Peptidase family M28; Pssm-ID: 461288 [Multi-domain] Cd Length: 192 Bit Score: 187.88 E-value: 5.02e-57
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| Iap | COG2234 | Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein ... |
206-479 | 5.20e-51 | |||||||
Zn-dependent amino- or carboxypeptidase, M28 family [Posttranslational modification, protein turnover, chaperones, Amino acid transport and metabolism]; Pssm-ID: 441835 [Multi-domain] Cd Length: 257 Bit Score: 174.55 E-value: 5.20e-51
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| PA_SaNapH_like | cd04816 | PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ... |
124-243 | 4.01e-44 | |||||||
PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 240120 [Multi-domain] Cd Length: 122 Bit Score: 151.32 E-value: 4.01e-44
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| M28 | cd02690 | M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also ... |
251-473 | 2.82e-34 | |||||||
M28 Zn-peptidases include aminopeptidases and carboxypeptidases; Peptidase M28 family (also called aminopeptidase Y family) contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Plasma glutamate carboxypeptidase (PGCP) and glutamate carboxypeptidase II (NAALADase) hydrolyze dipeptides. Several members of the M28 peptidase family have PA domain inserts which may participate in substrate binding and/or in promoting conformational changes, which influence the stability and accessibility of the site to substrate. These include prostate-specific membrane antigen (PSMA), yeast aminopeptidase S (SGAP), human transferrin receptors (TfR1 and TfR2), plasma glutamate carboxypeptidase (PGCP) and several predicted aminopeptidases where relatively little is known about them. Also included in the M28 family are glutaminyl cyclases (QC), which are involved in N-terminal glutamine cyclization of many endocrine peptides. Nicastrin and nicalin belong to this family but lack the amino-acid conservation required for catalytically active aminopeptidases. Pssm-ID: 349868 [Multi-domain] Cd Length: 202 Bit Score: 127.84 E-value: 2.82e-34
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| M28_like_PA | cd05661 | M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called ... |
246-469 | 8.12e-30 | |||||||
M28 Zn-peptidase containing a PA domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Pssm-ID: 349911 [Multi-domain] Cd Length: 262 Bit Score: 117.29 E-value: 8.12e-30
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| M28_like | cd03877 | M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family ... |
250-458 | 7.10e-23 | |||||||
M28 Zn-peptidase, many containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Some proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution. Pssm-ID: 349874 [Multi-domain] Cd Length: 206 Bit Score: 96.16 E-value: 7.10e-23
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| PA_ScAPY_like | cd02130 | PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ... |
118-230 | 1.69e-19 | |||||||
PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae aminopeptidase Y (ScAPY). This group contains various PA domain-containing proteins similar to the S. cerevisiae APY, including Trichophyton rubrum leucine aminopeptidase 1(LAP1). Proteins in this group belong to the peptidase M28 family. ScAPY hydrolyzes amino acid-4-methylcoumaryl-7-amides (MCAs). ScAPY more rapidly hydrolyzes dipeptidyl-MCAs. Hydrolysis of amino acid-MCAs or dipeptides is stimulated by Co2+ while the hydrolysis of dipeptidyl-MCAs, tripeptides, and longer peptides is inhibited by Co2+. ScAPY is vacuolar and is activated by proteolytic processing. LAP1 is a secreted leucine aminopeptidase. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239045 [Multi-domain] Cd Length: 122 Bit Score: 84.23 E-value: 1.69e-19
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| M28_like_PA_PDZ_associated | cd05663 | M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ ... |
224-423 | 4.51e-19 | |||||||
M28 Zn-peptidase containing a protease-associated (PA) domain insert and associated with a PDZ domain; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins, many of which contain a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Proteins in this subfamily are also associated with the PDZ domain, a widespread protein module that has been recruited to serve multiple functions during the course of evolution. Pssm-ID: 349913 [Multi-domain] Cd Length: 266 Bit Score: 87.12 E-value: 4.51e-19
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| M28_Pgcp_like | cd03883 | M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate ... |
73-328 | 4.59e-18 | |||||||
M28 Zn-Peptidase Plasma glutamate carboxypeptidase; Peptidase M28 family; Plasma glutamate carboxypeptidase (PGCP; blood plasma glutamate carboxypeptidase; EC 3.4.17.21) subfamily. PGCP is a 56kDa glutamate carboxypeptidase that is mainly produced in mammalian placenta and kidney, the majority of which is thought to be secreted into the bloodstream. Similar proteins are also found in other species, including bacteria. These proteins contain protease-associated (PA) domain inserts between the first and second strands of the central beta sheet in the protease-like domain. The PA domains may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. The exact physiological substrates of PGCP are unknown, although this enzyme may play an important role in the hydrolysis of circulating peptides. Its closest homolog encodes an important brain glutamate carboxypeptidase II (NAALADase) identical to the prostate-specific membrane antigen (PSMA), which serves as a marker for prostatic cancer metastasis. Hypermethylation of PGCP gene has been associated with human bronchial epithelial (HBE) cell immortalization and lung cancer. PGCP also provides an attractive target for serological analysis in hepatitis C virus (HCV)-induced hepatocellular carcinoma (HCC) patients. Pssm-ID: 349879 [Multi-domain] Cd Length: 425 Bit Score: 86.21 E-value: 4.59e-18
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| M28_like_PA | cd05660 | M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 ... |
239-474 | 1.44e-16 | |||||||
M28 Zn-peptidase containing a protease-associated (PA) domain insert; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate. Pssm-ID: 349910 [Multi-domain] Cd Length: 290 Bit Score: 80.10 E-value: 1.44e-16
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
69-241 | 1.10e-15 | |||||||
myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal MYXO-CTERM domain (see TIGR03901), suggesting processing and surface-anchoring by the still-unknown putative transpeptidase, myxosortase. Members of this family include MXAN_3564 (mepA), part of the effector cargo of outer membrane vesicles that the species produces in large numbers during predation on other microbes. Pssm-ID: 468355 [Multi-domain] Cd Length: 1597 Bit Score: 80.47 E-value: 1.10e-15
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| M28_like | cd05662 | M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized ... |
245-458 | 1.51e-15 | |||||||
M28 Zn-Peptidases; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins that do not contain a protease-associated (PA) domain. Pssm-ID: 349912 [Multi-domain] Cd Length: 268 Bit Score: 76.74 E-value: 1.51e-15
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| PA | cd00538 | PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ... |
131-243 | 1.30e-13 | |||||||
PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2. Pssm-ID: 238300 [Multi-domain] Cd Length: 126 Bit Score: 67.54 E-value: 1.30e-13
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| PA | pfam02225 | PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ... |
141-230 | 4.83e-13 | |||||||
PA domain; The PA (Protease associated) domain is found as an insert domain in diverse proteases. The PA domain is also found in a plant vacuolar sorting receptor Swiss:O22925 and members of the RZF family Swiss:O43567. It has been suggested that this domain forms a lid-like structure that covers the active site in active proteases, and is involved in protein recognition in vacuolar sorting receptors. Pssm-ID: 460499 [Multi-domain] Cd Length: 91 Bit Score: 64.84 E-value: 4.83e-13
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| M28_like | cd08015 | M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ... |
252-457 | 1.13e-12 | |||||||
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Pssm-ID: 349937 [Multi-domain] Cd Length: 218 Bit Score: 67.23 E-value: 1.13e-12
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| M28_like | cd05640 | M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ... |
250-473 | 1.19e-12 | |||||||
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Pssm-ID: 349893 [Multi-domain] Cd Length: 281 Bit Score: 68.24 E-value: 1.19e-12
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| PA_C5a_like | cd02133 | PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ... |
157-245 | 2.31e-12 | |||||||
PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a peptidase. This group contains various PA domain-containing proteins similar to S. pyogenes C5a, including, i) Vpr, a minor extracellular serine protease from Bacillus subtilis, ii) a large molecular mass collagenolytic protease from Geobacillus collagenovorans MO-1, and iii) PrtS, a cell envelope protease from Streptococcus thermophilus CNRZ 385. Proteins in this group belong to the peptidase S8 family. C5a peptidase is a cell surface serine protease which specifically inactivates C5a [a chemotactic peptide, which attracts polymorphonuclear leukocytes (PMNs)], by cleaving it to release a 7-residue carboxy-terminal fragment which contains the PMN binding site. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239048 [Multi-domain] Cd Length: 143 Bit Score: 64.62 E-value: 2.31e-12
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| PA_subtilisin_1 | cd04818 | PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ... |
130-241 | 8.22e-11 | |||||||
PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup. Pssm-ID: 240122 [Multi-domain] Cd Length: 118 Bit Score: 59.26 E-value: 8.22e-11
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| PA_C_RZF_like | cd02123 | PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA ... |
136-231 | 3.31e-10 | |||||||
PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239038 [Multi-domain] Cd Length: 153 Bit Score: 58.51 E-value: 3.31e-10
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| M28_AAP | cd03879 | M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; ... |
232-346 | 5.35e-10 | |||||||
M28 Zn-peptidase Aeromonas (Vibrio) proteolytica aminopeptidase; Peptidase family M28; Aeromonas (Vibrio) proteolytica aminopeptidase (AAP; leucine aminopeptidase from Vibrio proteolyticus; Bacterial leucyl aminopeptidase; E.C. 3.4.11.10) subfamily. AAP is a small (32kDa), heat stable leucine aminopeptidase and is active as a monomer. Similar forms of the enzyme have been isolated from Escherichia coli and Staphylococcus thermophilus. Leucine aminopeptidases, in general, play important roles in many biological processes such as protein catabolism, hormone degradation, regulation of migration and cell proliferation, as well as HIV infection and proliferation. AAP is a broad-specificity enzyme, utilizing two zinc(II) ions in its active site to remove N-terminal amino acids, with preference for large hydrophobic amino acids in the P1 position of the substrate, Leu being the most efficiently cleaved. It can accommodate all residues, except Pro, Asp and Glu in the P1' position. Pssm-ID: 349875 [Multi-domain] Cd Length: 286 Bit Score: 60.33 E-value: 5.35e-10
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| M28_Fxna_like | cd03875 | M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic ... |
248-329 | 9.46e-10 | |||||||
M28 Zn-peptidase Endoplasmic reticulum metallopeptidase 1; Peptidase family M28; Endoplasmic reticulum metallopeptidase 1 (ERMP1; Felix-ina, FXNA or Fxna peptidase; KIAA1815) subfamily. ERMP1 is a multi-pass membrane protein located in the endoplasmic reticulum membrane. In humans, Fxna may play a crucial role in processing proteins required for the organization of somatic cells and oocytes into discrete follicular structures, although which proteins are hydrolyzed has not yet been determined. Another member of this subfamily is the 24-kDa vacuolar protein (VP24) which is probably involved in the formation of intravacuolar pigmented globules (cyanoplasts) in highly anthocyanin-containing vacuoles; however, the biological function of the C-terminal region which includes the putative transmembrane metallopeptidase domain is unknown. Pssm-ID: 349872 [Multi-domain] Cd Length: 307 Bit Score: 59.91 E-value: 9.46e-10
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| PA_VSR | cd02125 | PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ... |
145-231 | 4.24e-09 | |||||||
PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This group includes various PA domain-containing VSRs such as garden pea BP-80, pumpkin PV72, and various Arabidopsis VSRs including AtVSR1. In contrast to most eukaryotes, which only have one or two VSRs, plants have several. This may in part be a reflection of having a more complex vacuolar system with both lytic vacuoles and storage vacuoles. The lytic vacuole is thought to be equivalent to the mammalian lysosome and the yeast vacuole. Pea BP-80 is a type 1 transmembrane protein, involved in the targeting of proteins to the lytic vacuole; it has been suggested that this protein also mediates targeting to the storage vacuole. PV72 and AtVSR1 may mediate transport of seed storage proteins to protein storage vacuoles. The significance of the PA domain to VSRs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239040 [Multi-domain] Cd Length: 127 Bit Score: 54.79 E-value: 4.24e-09
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| M20_18_42 | cd18669 | M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family ... |
252-406 | 4.88e-09 | |||||||
M20, M18 and M42 Zn-peptidases include aminopeptidases and carboxypeptidases; This family corresponds to the MEROPS MH clan families M18, M20, and M42. The peptidase M20 family contains exopeptidases, including carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase, dipeptidases such as bacterial dipeptidase, peptidase V (PepV), a eukaryotic, non-specific dipeptidase, and two Xaa-His dipeptidases (carnosinases). This family also includes the bacterial aminopeptidase peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. These peptidases generally hydrolyze the late products of protein degradation so as to complete the conversion of proteins to free amino acids. Glutamate carboxypeptidase hydrolyzes folate analogs such as methotrexate, and therefore can be used to treat methotrexate toxicity. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 (aspartyl aminopeptidase, DAP) family cleaves only unblocked N-terminal acidic amino-acid residues and is highly selective for hydrolyzing aspartate or glutamate residues. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). Pssm-ID: 349948 [Multi-domain] Cd Length: 198 Bit Score: 56.29 E-value: 4.88e-09
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| PA_GO-like | cd02132 | PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ... |
144-232 | 8.11e-09 | |||||||
PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239047 [Multi-domain] Cd Length: 139 Bit Score: 53.97 E-value: 8.11e-09
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| PA_hSPPL_like | cd02129 | PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ... |
152-220 | 2.70e-08 | |||||||
PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239044 [Multi-domain] Cd Length: 120 Bit Score: 52.01 E-value: 2.70e-08
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| PRK10199 | PRK10199 | alkaline phosphatase isozyme conversion aminopeptidase; Provisional |
240-460 | 1.96e-07 | |||||||
alkaline phosphatase isozyme conversion aminopeptidase; Provisional Pssm-ID: 182299 [Multi-domain] Cd Length: 346 Bit Score: 52.82 E-value: 1.96e-07
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| Peptidase_M20 | pfam01546 | Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging ... |
269-336 | 3.99e-07 | |||||||
Peptidase family M20/M25/M40; This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. Pssm-ID: 460247 [Multi-domain] Cd Length: 315 Bit Score: 51.96 E-value: 3.99e-07
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| M28_PSMA_like | cd08022 | M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific ... |
241-350 | 6.55e-07 | |||||||
M28 Zn-peptidase prostate-specific membrane antigen; Peptidase M28 family; prostate-specific membrane antigen (PSMA, also called glutamate carboxypeptidase II or GCP-II)-like subfamily. PSMA is a homodimeric type II transmembrane protein containing three distinct domains: protease-like, apical or protease-associated (PA) and helical domains. The protease-like domain is a large extracellular portion (ectodomain). PSMA is over-expressed predominantly in prostate cancer (PCa) as well as in the neovasculature of most solid tumors, but not in the vasculature of the normal tissues. PSMA is considered a biomarker for PCa and possibly for use as an imaging and therapeutic target. The extracellular domain of PSMA possesses two unique enzymatic functions: N-acetylated, alpha-linked acidic dipeptidase (NAALADase) which cleaves terminal glutamate from the neurodipeptide N-acetyl-aspartyl-glutamate (NAAG), and folate hydrolase (FOLH) which cleaves the terminal glutamates from gamma-linked polyglutamates (carboxypeptidase). A mutation in this gene may be associated with impaired intestinal absorption of dietary folates, resulting in low blood folate levels and consequent hyperhomocysteinemia. Expression of this protein in the brain may be involved in a number of pathological conditions associated with glutamate excitotoxicity. Inhibition of GCP-II has been shown to be effective in preclinical models of neurological disorders associated with excessive activation of glutamatergic systems. This gene likely arose from a duplication event of a nearby chromosomal region. Alternative splicing gives rise to multiple transcript variants. Pssm-ID: 349942 [Multi-domain] Cd Length: 287 Bit Score: 51.08 E-value: 6.55e-07
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| Zinc_peptidase_like | cd03873 | Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and ... |
252-355 | 1.56e-06 | |||||||
Zinc peptidases M18, M20, M28, and M42; Zinc peptidases play vital roles in metabolic and signaling pathways throughout all kingdoms of life. This hierarchy contains zinc peptidases that correspond to the MH clan in the MEROPS database, which contains 4 families (M18, M20, M28, M42). The peptidase M20 family includes carboxypeptidases such as the glutamate carboxypeptidase from Pseudomonas, the thermostable carboxypeptidase Ss1 of broad specificity from archaea and yeast Gly-X carboxypeptidase. The dipeptidases include bacterial dipeptidase, peptidase V (PepV), a non-specific eukaryotic dipeptidase, and two Xaa-His dipeptidases (carnosinases). There is also the bacterial aminopeptidase, peptidase T (PepT) that acts only on tripeptide substrates and has therefore been termed a tripeptidase. Peptidase family M28 contains aminopeptidases and carboxypeptidases, and has co-catalytic zinc ions. However, several enzymes in this family utilize other first row transition metal ions such as cobalt and manganese. Each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. The aminopeptidases in this family are also called bacterial leucyl aminopeptidases, but are able to release a variety of N-terminal amino acids. IAP aminopeptidase and aminopeptidase Y preferentially release basic amino acids while glutamate carboxypeptidase II preferentially releases C-terminal glutamates. Glutamate carboxypeptidase II and plasma glutamate carboxypeptidase hydrolyze dipeptides. Peptidase families M18 and M42 contain metallo-aminopeptidases. M18 is widely distributed in bacteria and eukaryotes. However, only yeast aminopeptidase I and mammalian aspartyl aminopeptidase have been characterized in detail. Some M42 (also known as glutamyl aminopeptidase) enzymes exhibit aminopeptidase specificity while others also have acylaminoacyl-peptidase activity (i.e. hydrolysis of acylated N-terminal residues). Pssm-ID: 349870 [Multi-domain] Cd Length: 200 Bit Score: 48.96 E-value: 1.56e-06
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| PA_PoS1_like | cd02124 | PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ... |
116-199 | 1.95e-06 | |||||||
PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239039 Cd Length: 129 Bit Score: 46.94 E-value: 1.95e-06
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| PA_1 | cd04813 | PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ... |
154-223 | 3.35e-06 | |||||||
PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. Proteins in this subgroup contain a RING-finger (Really Interesting New Gene) domain C-terminal to this PA domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup. Pssm-ID: 240117 [Multi-domain] Cd Length: 117 Bit Score: 46.23 E-value: 3.35e-06
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| PA_subtilisin_like | cd02120 | PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ... |
116-231 | 3.97e-06 | |||||||
PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This group contains various PA domain-containing subtilisin-like proteases including melon cucumisin, Arabidopsis thaliana Ara12, a nodule specific serine protease from Alnus glutinosa ag12, members of the tomato P69 family, and tomato LeSBT2. These proteins belong to the peptidase S8 family. Cucumisin from the juice of melon fruits is a thermostable serine peptidase, with a broad substrate specificity for oligopeptides and proteins. A. thaliana Ara12 is a thermostable, extracellular serine protease, found chiefly in silique tissue and stem tissue. Ara12 is stimulated by Ca2+ ions. A. glutinosa ag12 is expressed at high levels in the nodules, and at low levels in the shoot tips; it is implicated in both symbiotic and non-symbiotic processes in plant development. The tomato P69 protease family is comprised of various protein isoforms of approximately 69KDa. These isoforms accumulate extracellularly. Some of the P69 genes are tightly regulated in a tissue specific fashion, and by environmental and developmental signals. For example: infection with avirulent bacteria activates transcription of the genes for the P69 B and C isoforms, the P69 E transcript was detected only in roots, and the P69F transcript only in hydathodes. The Tomato LeSBT2 subtilase transcript was not detected in flowers and roots, but was present in cotyledons and leaves. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239035 [Multi-domain] Cd Length: 126 Bit Score: 46.25 E-value: 3.97e-06
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| M28_like | cd05643 | M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), ... |
279-499 | 5.71e-06 | |||||||
M28 Zn-peptidase-like; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion. Pssm-ID: 349895 [Multi-domain] Cd Length: 290 Bit Score: 48.17 E-value: 5.71e-06
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| T9SSA_dep_M36 | NF038113 | T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ... |
136-242 | 8.12e-06 | |||||||
T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family metallopeptidase domain, like fungalysin (see PF02128), and a C-terminal T9SS type A sorting domain (see TIGR04131). Pssm-ID: 468356 [Multi-domain] Cd Length: 868 Bit Score: 48.50 E-value: 8.12e-06
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| PepD2 | COG2195 | Di- or tripeptidase [Amino acid transport and metabolism]; |
252-345 | 1.02e-05 | |||||||
Di- or tripeptidase [Amino acid transport and metabolism]; Pssm-ID: 441798 [Multi-domain] Cd Length: 364 Bit Score: 47.74 E-value: 1.02e-05
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| PA_EDEM3_like | cd02126 | PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ... |
165-220 | 3.54e-05 | |||||||
PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239041 [Multi-domain] Cd Length: 126 Bit Score: 43.50 E-value: 3.54e-05
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| M28_Nicastrin | cd03881 | M28 Zn-peptidase nicastrin, a main component of gamma-secretase complex; Peptidase M28 family, ... |
247-331 | 3.73e-05 | |||||||
M28 Zn-peptidase nicastrin, a main component of gamma-secretase complex; Peptidase M28 family, nicastrin subfamily. Nicastrin is a main component of the gamma-secretase complex, which also contains presenilin, Pen-2 and Aph-1. Its extracellular domain sequence resembles aminopeptidases, but certain catalytic residues are not conserved. It is mainly localized to the endoplasmic reticulum and Golgi. It is highly glycosylated (Mr 120 kDa) and is essential for substrate recognition of the N-terminus of gamma-secretase substrates derived from APP and Notch. Nicastrin facilitates substrate cleavage by the catalytic presenilin subunit in the gamma-secretase complex. One conserved glutamate is especially important, probably because this residue forms an ion pair with the amino terminus of the substrate. This substrate-binding domain is often called the DAP domain (named after DYIGS, the amino acid stretch that modulates amyloid precursor protein (APP) processing, and Peptidase homologous region). The sequence of the substrate N-terminus is apparently not critical for the interaction, but a free amino group is. Thus, nicastrin can be considered a kind of gatekeeper for the gamma-secretase complex: type I membrane proteins that have not shed their ectodomains cannot interact properly with nicastrin and do not gain access to the active site. Dysfunction of gamma-secretase is thought to cause Alzheimer's disease, with most mutations derived from Alzheimer's disease mapping to the catalytic subunit presenilin 1 (PS1). Pssm-ID: 349877 [Multi-domain] Cd Length: 519 Bit Score: 46.26 E-value: 3.73e-05
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| M20_bAS | cd03884 | M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine ... |
252-336 | 9.53e-05 | |||||||
M20 Peptidase beta-alanine synthase, an amidohydrolase; Peptidase M20 family, beta-alanine synthase (bAS; N-carbamoyl-beta-alanine amidohydrolase and beta-ureidopropionase; EC 3.5.1.6) subfamily. bAS is an amidohydrolase and is the final enzyme in the pyrimidine catabolic pathway, which is involved in the regulation of the cellular pyrimidine pool. bAS catalyzes the irreversible hydrolysis of the N-carbamylated beta-amino acids to beta-alanine or aminoisobutyrate with the release of carbon dioxide and ammonia. Also included in this subfamily is allantoate amidohydrolase (allantoate deiminase), which catalyzes the conversion of allantoate to (S)-ureidoglycolate, one of the crucial alternate steps in purine metabolism. It is possible that these two enzymes arose from the same ancestral peptidase that evolved into two structurally related enzymes with distinct catalytic properties and biochemical roles within the cell. Downstream enzyme (S)-ureidoglycolate amidohydrolase (UAH) is homologous in structure and sequence with AAH and catalyzes the conversion of (S)-ureidoglycolate into glyoxylate, releasing two molecules of ammonia as by-products. Yeast requires beta-alanine as a precursor of pantothenate and coenzyme A biosynthesis, but generates it mostly via degradation of spermine. Disorders in pyrimidine degradation and beta-alanine metabolism caused by beta-ureidopropionase deficiency (UPB1 gene) in humans are normally associated with neurological disorders. Pssm-ID: 349880 [Multi-domain] Cd Length: 398 Bit Score: 44.82 E-value: 9.53e-05
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| M28_like | cd08656 | M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase ... |
249-319 | 1.21e-04 | |||||||
M28 Zn-peptidase; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Pssm-ID: 349943 [Multi-domain] Cd Length: 287 Bit Score: 44.05 E-value: 1.21e-04
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| PA_hPAP21_like | cd02127 | PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ... |
142-199 | 1.41e-04 | |||||||
PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted glycoprotein hPAP21 (human protease-associated domain-containing protein, 21kDa). This group contains various PA domain-containing proteins similar to hPAP21. Complex N-glycosylation may be required for the secretion of hPAP21. The significance of the PA domain to hPAP21 has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239042 [Multi-domain] Cd Length: 118 Bit Score: 41.59 E-value: 1.41e-04
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| PA_VapT_like | cd04817 | PA_VapT_like: Protease-associated domain containing proteins like VapT from Vibrio ... |
165-238 | 2.30e-04 | |||||||
PA_VapT_like: Protease-associated domain containing proteins like VapT from Vibrio metschnikovii strain RH530. This group contains various PA domain-containing proteins similar to V. metschnikovii VapT, including the serine alkaline protease SapSh from the psychotroph Shewanella strain Ac10 and the Apa1 protease from the psychrotroph Pseudoalteromonas Sp. As-11. VapT is a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease showing high activity over a broad pH range and temperature. SapSh has a high level of protease activity at low temperatures. Apa1 is also cold-adapted. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 240121 Cd Length: 139 Bit Score: 41.32 E-value: 2.30e-04
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| PRK09290 | PRK09290 | allantoate amidohydrolase; Reviewed |
259-335 | 1.58e-03 | |||||||
allantoate amidohydrolase; Reviewed Pssm-ID: 236456 [Multi-domain] Cd Length: 413 Bit Score: 40.91 E-value: 1.58e-03
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| ArgE | COG0624 | Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino ... |
252-330 | 2.59e-03 | |||||||
Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase [Amino acid transport and metabolism]; Acetylornithine deacetylase/Succinyl-diaminopimelate desuccinylase or related deacylase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440389 [Multi-domain] Cd Length: 388 Bit Score: 40.25 E-value: 2.59e-03
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| PA_2 | cd04819 | PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. ... |
116-230 | 2.66e-03 | |||||||
PA_2: Protease-associated (PA) domain subgroup 2. A subgroup of PA-domain containing proteins. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins in this group contain a C-terminal RING-finger domain. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases: such as hSPPL2a and 2b, ii) various E3 ubiquitin ligases similar to human GRAIL (gene related to anergy in lymphocytes) protein, iii) various proteins containing a RING finger motif such as Arabidopsis ReMembR-H2 protein, iv) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), v) various plant vacuolar sorting receptors such as Pisum sativum BP-80, vi) prostate-specific membrane antigen (PSMA), vii) yeast aminopeptidase Y viii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, ix) various subtilisin-like proteases such as Cucumisin from the juice of melon fruits, and x) human TfR (transferrin receptor) 1 and human TfR2. The proteins listed above belong to other subgroups; relatively little is known about proteins in this subgroup. Pssm-ID: 240123 [Multi-domain] Cd Length: 127 Bit Score: 38.14 E-value: 2.66e-03
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| PRK12890 | PRK12890 | allantoate amidohydrolase; Reviewed |
259-336 | 3.51e-03 | |||||||
allantoate amidohydrolase; Reviewed Pssm-ID: 237248 [Multi-domain] Cd Length: 414 Bit Score: 39.89 E-value: 3.51e-03
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| PA_GRAIL_like | cd02122 | PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ... |
140-199 | 3.92e-03 | |||||||
PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain containing E3 (ubiquitin ligases) similar to human GRAIL (gene related to anergy in lymphocytes) protein. Proteins in this group contain a C3H2C3 RING finger. E3 ubiquitin ligase is part of an enzymic cascade, the end result of which is the ubiquitination of proteins. In this cascade, E1 activates the ubiquitin, the activated ubiquitin is carried by E2, and E3 recognizes the acceptor protein as well as catalyzes the transfer of the activated ubiquitin from E2 to this acceptor. GRAIL, a transmembrane protein localized in the endosomes, controls the development of T cell clonal anergy, and may ubiquitinate membrane-associated targets for T cell activation. GRAIL1 is associated with, and regulated by, two isoforms of otubain 1 (the ubiquitin-specific protease). Additional E3s belonging to this group include human (h)Goliath and Xenopus GREUL1 (Goliath Related E3 Ubiquitin Ligase 1). hGoliath and GRAIL both have the property of self-ubiquitination. hGoliath is expressed in leukocytes; its expression and localization is not modified in leukemia. GREUL1 may play a role in the generation of anterior ectoderm. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Pssm-ID: 239037 [Multi-domain] Cd Length: 138 Bit Score: 37.66 E-value: 3.92e-03
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| M28_like | cd05642 | M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called ... |
236-349 | 3.92e-03 | |||||||
M28 Zn-peptidase-like; uncharacterized subfamily; Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. Pssm-ID: 349894 [Multi-domain] Cd Length: 347 Bit Score: 39.40 E-value: 3.92e-03
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| PRK12893 | PRK12893 | Zn-dependent hydrolase; |
252-338 | 7.65e-03 | |||||||
Zn-dependent hydrolase; Pssm-ID: 237250 [Multi-domain] Cd Length: 412 Bit Score: 38.71 E-value: 7.65e-03
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