retroviral-like aspartic protease family protein [Qipengyuania mesophila]
retroviral-like aspartic protease family protein( domain architecture ID 10144586)
aspartic protease belonging to the retropepsin-like protease family contains an active site aspartate occurring within a motif (Asp-Thr/Ser-Gly); belongs to the MEROPS peptidase family A2 (retropepsin family, clan AA), subfamily A2A
List of domain hits
Name | Accession | Description | Interval | E-value | |||
retropepsin_like_bacteria | cd05483 | Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ... |
33-126 | 1.05e-12 | |||
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A. : Pssm-ID: 133150 Cd Length: 96 Bit Score: 63.03 E-value: 1.05e-12
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Asp_protease_2 | pfam13650 | Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ... |
170-253 | 1.89e-06 | |||
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix. : Pssm-ID: 433378 Cd Length: 90 Bit Score: 45.35 E-value: 1.89e-06
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Name | Accession | Description | Interval | E-value | |||
retropepsin_like_bacteria | cd05483 | Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ... |
33-126 | 1.05e-12 | |||
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A. Pssm-ID: 133150 Cd Length: 96 Bit Score: 63.03 E-value: 1.05e-12
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gag-asp_proteas | pfam13975 | gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ... |
36-126 | 2.06e-10 | |||
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins. Pssm-ID: 464060 Cd Length: 92 Bit Score: 56.43 E-value: 2.06e-10
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Asp_protease_2 | pfam13650 | Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ... |
170-253 | 1.89e-06 | |||
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix. Pssm-ID: 433378 Cd Length: 90 Bit Score: 45.35 E-value: 1.89e-06
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COG3577 | COG3577 | Predicted aspartyl protease [General function prediction only]; |
3-134 | 1.98e-06 | |||
Predicted aspartyl protease [General function prediction only]; Pssm-ID: 442797 Cd Length: 152 Bit Score: 46.86 E-value: 1.98e-06
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retropepsin_like_bacteria | cd05483 | Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ... |
166-252 | 9.49e-05 | |||
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A. Pssm-ID: 133150 Cd Length: 96 Bit Score: 40.69 E-value: 9.49e-05
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COG3577 | COG3577 | Predicted aspartyl protease [General function prediction only]; |
128-245 | 1.50e-03 | |||
Predicted aspartyl protease [General function prediction only]; Pssm-ID: 442797 Cd Length: 152 Bit Score: 38.39 E-value: 1.50e-03
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Name | Accession | Description | Interval | E-value | |||
retropepsin_like_bacteria | cd05483 | Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ... |
33-126 | 1.05e-12 | |||
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A. Pssm-ID: 133150 Cd Length: 96 Bit Score: 63.03 E-value: 1.05e-12
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gag-asp_proteas | pfam13975 | gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ... |
36-126 | 2.06e-10 | |||
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins. Pssm-ID: 464060 Cd Length: 92 Bit Score: 56.43 E-value: 2.06e-10
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Asp_protease_2 | pfam13650 | Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ... |
36-123 | 4.65e-09 | |||
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix. Pssm-ID: 433378 Cd Length: 90 Bit Score: 52.67 E-value: 4.65e-09
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Asp_protease_2 | pfam13650 | Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to ... |
170-253 | 1.89e-06 | |||
Aspartyl protease; This family consists of predicted aspartic proteases, typically from 180 to 230 amino acids in length, in MEROPS clan AA. This model describes the well-conserved 121-residue C-terminal region. The poorly conserved, variable length N-terminal region usually contains a predicted transmembrane helix. Pssm-ID: 433378 Cd Length: 90 Bit Score: 45.35 E-value: 1.89e-06
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COG3577 | COG3577 | Predicted aspartyl protease [General function prediction only]; |
3-134 | 1.98e-06 | |||
Predicted aspartyl protease [General function prediction only]; Pssm-ID: 442797 Cd Length: 152 Bit Score: 46.86 E-value: 1.98e-06
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RP_DDI | cd05479 | RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the ... |
30-141 | 1.21e-05 | |||
RP_DDI; retropepsin-like domain of DNA damage inducible protein; The family represents the retropepsin-like domain of DNA damage inducible protein. DNA damage inducible protein has a retropepsin-like domain and an amino-terminal ubiquitin-like domain and/or a UBA (ubiquitin-associated) domain. This CD represents the retropepsin-like domain of DDI. Pssm-ID: 133146 Cd Length: 124 Bit Score: 43.70 E-value: 1.21e-05
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retropepsin_like_bacteria | cd05483 | Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria ... |
166-252 | 9.49e-05 | |||
Bacterial aspartate proteases, retropepsin-like protease family; This family of bacteria aspartate proteases is a subfamily of retropepsin-like protease family, which includes enzymes from retrovirus and retrotransposons. While fungal and mammalian pepsin-like aspartate proteases are bilobal proteins with structurally related N- and C-termini, this family of bacteria aspartate proteases is half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate proteases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A. Pssm-ID: 133150 Cd Length: 96 Bit Score: 40.69 E-value: 9.49e-05
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retropepsin_like | cd00303 | Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate ... |
36-126 | 1.89e-04 | |||
Retropepsins; pepsin-like aspartate proteases; The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements, as well as eukaryotic dna-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. While fungal and mammalian pepsins are bilobal proteins with structurally related N and C-terminals, retropepsins are half as long as their fungal and mammalian counterparts. The monomers are structurally related to one lobe of the pepsin molecule and retropepsins function as homodimers. The active site aspartate occurs within a motif (Asp-Thr/Ser-Gly), as it does in pepsin. Retroviral aspartyl protease is synthesized as part of the POL polyprotein that contains an aspartyl protease, a reverse transcriptase, RNase H, and an integrase. The POL polyprotein undergoes specific enzymatic cleavage to yield the mature proteins. In aspartate peptidases, Asp residues are ligands of an activated water molecule in all examples where catalytic residues have been identified. This group of aspartate peptidases is classified by MEROPS as the peptidase family A2 (retropepsin family, clan AA), subfamily A2A. Pssm-ID: 133136 Cd Length: 92 Bit Score: 39.63 E-value: 1.89e-04
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COG3577 | COG3577 | Predicted aspartyl protease [General function prediction only]; |
128-245 | 1.50e-03 | |||
Predicted aspartyl protease [General function prediction only]; Pssm-ID: 442797 Cd Length: 152 Bit Score: 38.39 E-value: 1.50e-03
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Asp_protease | pfam09668 | Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to ... |
34-133 | 1.58e-03 | |||
Aspartyl protease; This family of eukaryotic aspartyl proteases have a fold similar to retroviral proteases which implies they function proteolytically during regulated protein turnover. Pssm-ID: 312981 Cd Length: 124 Bit Score: 37.72 E-value: 1.58e-03
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gag-asp_proteas | pfam13975 | gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is ... |
169-253 | 5.59e-03 | |||
gag-polyprotein putative aspartyl protease; This family of putative aspartyl proteases is found pre-dominantly in retroviral proteins. Pssm-ID: 464060 Cd Length: 92 Bit Score: 35.63 E-value: 5.59e-03
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Blast search parameters | ||||
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