ER degradation-enhancing alpha-mannosidase-like protein 3 isoform X4 [Rattus norvegicus]
Protein Classification
glycoside hydrolase family 47 protein( domain architecture ID 10479226)
glycoside hydrolase family 47 protein such as ER class I alpha1,2-mannosidase, which is a critical enzyme in the maturation of N-linked oligosaccharides and ER-associated degradation
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| Glyco_hydro_47 | pfam01532 | Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ... |
60-499 | 6.25e-154 | ||||||||
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2). : Pssm-ID: 460241 Cd Length: 453 Bit Score: 460.87 E-value: 6.25e-154
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| PA_EDEM3_like | cd02126 | PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ... |
647-772 | 6.17e-78 | ||||||||
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: 249.20 E-value: 6.17e-78
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| Name | Accession | Description | Interval | E-value | ||||||||
| Glyco_hydro_47 | pfam01532 | Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ... |
60-499 | 6.25e-154 | ||||||||
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2). Pssm-ID: 460241 Cd Length: 453 Bit Score: 460.87 E-value: 6.25e-154
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| PA_EDEM3_like | cd02126 | PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ... |
647-772 | 6.17e-78 | ||||||||
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: 249.20 E-value: 6.17e-78
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| PTZ00470 | PTZ00470 | glycoside hydrolase family 47 protein; Provisional |
55-499 | 3.09e-77 | ||||||||
glycoside hydrolase family 47 protein; Provisional Pssm-ID: 240427 Cd Length: 522 Bit Score: 261.58 E-value: 3.09e-77
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| T9SSA_dep_M36 | NF038113 | T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ... |
650-774 | 1.03e-15 | ||||||||
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: 82.01 E-value: 1.03e-15
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| PA | pfam02225 | PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ... |
665-758 | 1.33e-14 | ||||||||
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: 69.85 E-value: 1.33e-14
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
645-748 | 9.26e-14 | ||||||||
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: 75.85 E-value: 9.26e-14
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| LanM-like | cd04792 | Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ... |
237-329 | 6.34e-04 | ||||||||
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB. Pssm-ID: 271200 [Multi-domain] Cd Length: 836 Bit Score: 43.46 E-value: 6.34e-04
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| Name | Accession | Description | Interval | E-value | ||||||||
| Glyco_hydro_47 | pfam01532 | Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ... |
60-499 | 6.25e-154 | ||||||||
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2). Pssm-ID: 460241 Cd Length: 453 Bit Score: 460.87 E-value: 6.25e-154
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| PA_EDEM3_like | cd02126 | PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This ... |
647-772 | 6.17e-78 | ||||||||
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: 249.20 E-value: 6.17e-78
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| PTZ00470 | PTZ00470 | glycoside hydrolase family 47 protein; Provisional |
55-499 | 3.09e-77 | ||||||||
glycoside hydrolase family 47 protein; Provisional Pssm-ID: 240427 Cd Length: 522 Bit Score: 261.58 E-value: 3.09e-77
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| PA | cd00538 | PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction ... |
645-772 | 1.95e-22 | ||||||||
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: 93.73 E-value: 1.95e-22
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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 ... |
650-775 | 3.52e-22 | ||||||||
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: 93.94 E-value: 3.52e-22
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| PA_subtilisin_1 | cd04818 | PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. ... |
649-772 | 3.89e-19 | ||||||||
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: 83.92 E-value: 3.89e-19
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| PA_hPAP21_like | cd02127 | PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted ... |
672-773 | 2.86e-17 | ||||||||
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: 78.57 E-value: 2.86e-17
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| PA_GO-like | cd02132 | PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on ... |
646-772 | 2.05e-16 | ||||||||
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: 76.69 E-value: 2.05e-16
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| T9SSA_dep_M36 | NF038113 | T9SS-dependent M36 family metallopeptidase; Members of this family have an M36 family ... |
650-774 | 1.03e-15 | ||||||||
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: 82.01 E-value: 1.03e-15
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| PA | pfam02225 | PA domain; The PA (Protease associated) domain is found as an insert domain in diverse ... |
665-758 | 1.33e-14 | ||||||||
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: 69.85 E-value: 1.33e-14
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| myxo_dep_M36 | NF038112 | myxosortase-dependent M36 family metallopeptidase; Members of this bacterial protein family ... |
645-748 | 9.26e-14 | ||||||||
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: 75.85 E-value: 9.26e-14
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| PA_C5a_like | cd02133 | PA_C5a_like: Protease-associated domain containing proteins like Streptococcus pyogenes C5a ... |
685-770 | 1.09e-11 | ||||||||
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: 63.46 E-value: 1.09e-11
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| PA_1 | cd04813 | PA_1: Protease-associated (PA) domain subgroup 1. A subgroup of PA-domain containing proteins. ... |
669-762 | 1.85e-10 | ||||||||
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: 58.94 E-value: 1.85e-10
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| PA_ScAPY_like | cd02130 | PA_ScAPY_like: Protease-associated domain containing proteins like Saccharomyces cerevisiae ... |
675-727 | 4.01e-09 | ||||||||
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: 55.34 E-value: 4.01e-09
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| PA_GRAIL_like | cd02122 | PA _GRAIL_like: Protease-associated (PA) domain GRAIL-like. This group includes PA domain ... |
653-738 | 4.95e-08 | ||||||||
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: 52.69 E-value: 4.95e-08
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| PA_VSR | cd02125 | PA_VSR: Protease-associated (PA) domain-containing plant vacuolar sorting receptor (VSR). This ... |
658-772 | 1.10e-06 | ||||||||
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: 48.63 E-value: 1.10e-06
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| PA_hSPPL_like | cd02129 | PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like ... |
682-750 | 1.65e-05 | ||||||||
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: 45.07 E-value: 1.65e-05
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| PA_PoS1_like | cd02124 | PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA ... |
669-770 | 9.82e-05 | ||||||||
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: 43.09 E-value: 9.82e-05
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| PA_subtilisin_like | cd02120 | PA_subtilisin_like: Protease-associated domain containing subtilisin-like proteases. This ... |
667-764 | 1.02e-04 | ||||||||
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: 42.79 E-value: 1.02e-04
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| PA_SaNapH_like | cd04816 | PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus ... |
685-770 | 4.20e-04 | ||||||||
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: 41.16 E-value: 4.20e-04
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| LanM-like | cd04792 | Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ... |
237-329 | 6.34e-04 | ||||||||
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB. Pssm-ID: 271200 [Multi-domain] Cd Length: 836 Bit Score: 43.46 E-value: 6.34e-04
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