RecName: Full=Endogenous retrovirus group K member 9 Pro protein; AltName: Full=HERV-K(C6) Pro protein; AltName: Full=HERV-K109 Pro protein; AltName: Full=HERV-K_6q14.1 provirus ancestral Pro protein; AltName: Full=Protease; AltName: Full=Proteinase; Short=PR
HIV_retropepsin_like and G-patch domain-containing protein( domain architecture ID 10442237)
HIV_retropepsin_like and G-patch domain-containing protein
List of domain hits
Name | Accession | Description | Interval | E-value | |||
RVP | pfam00077 | Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ... |
6-105 | 6.80e-42 | |||
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026). : Pssm-ID: 425454 Cd Length: 101 Bit Score: 135.19 E-value: 6.80e-42
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G-patch | pfam01585 | G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ... |
111-155 | 2.70e-14 | |||
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines. : Pssm-ID: 396249 [Multi-domain] Cd Length: 45 Bit Score: 62.91 E-value: 2.70e-14
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Name | Accession | Description | Interval | E-value | |||
RVP | pfam00077 | Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ... |
6-105 | 6.80e-42 | |||
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026). Pssm-ID: 425454 Cd Length: 101 Bit Score: 135.19 E-value: 6.80e-42
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HIV_retropepsin_like | cd05482 | Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ... |
12-98 | 2.60e-32 | |||
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, 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: 133149 Cd Length: 87 Bit Score: 110.05 E-value: 2.60e-32
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G-patch | pfam01585 | G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ... |
111-155 | 2.70e-14 | |||
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines. Pssm-ID: 396249 [Multi-domain] Cd Length: 45 Bit Score: 62.91 E-value: 2.70e-14
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G_patch | smart00443 | glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ... |
111-154 | 9.00e-12 | |||
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins. Pssm-ID: 197727 [Multi-domain] Cd Length: 47 Bit Score: 56.40 E-value: 9.00e-12
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Name | Accession | Description | Interval | E-value | |||
RVP | pfam00077 | Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, ... |
6-105 | 6.80e-42 | |||
Retroviral aspartyl protease; Single domain aspartyl proteases from retroviruses, retrotransposons, and badnaviruses (plant dsDNA viruses). These proteases are generally part of a larger polyprotein; usually pol, more rarely gag. Retroviral proteases appear to be homologous to a single domain of the two-domain eukaryotic aspartyl proteases such as pepsins, cathepsins, and renins (pfam00026). Pssm-ID: 425454 Cd Length: 101 Bit Score: 135.19 E-value: 6.80e-42
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HIV_retropepsin_like | cd05482 | Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family ... |
12-98 | 2.60e-32 | |||
Retropepsins, pepsin-like aspartate proteases; This is a subfamily of retropepsins. The family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, 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: 133149 Cd Length: 87 Bit Score: 110.05 E-value: 2.60e-32
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G-patch | pfam01585 | G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in ... |
111-155 | 2.70e-14 | |||
G-patch domain; This domain is found in a number of RNA binding proteins, and is also found in proteins that contain RNA binding domains. This suggests that this domain may have an RNA binding function. This domain has seven highly conserved glycines. Pssm-ID: 396249 [Multi-domain] Cd Length: 45 Bit Score: 62.91 E-value: 2.70e-14
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G_patch | smart00443 | glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in ... |
111-154 | 9.00e-12 | |||
glycine rich nucleic binding domain; A predicted glycine rich nucleic binding domain found in the splicing factor 45, SON DNA binding protein and D-type Retrovirus- polyproteins. Pssm-ID: 197727 [Multi-domain] Cd Length: 47 Bit Score: 56.40 E-value: 9.00e-12
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RP_RTVL_H_like | cd06095 | Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family ... |
16-98 | 2.14e-05 | |||
Retropepsin of the RTVL_H family of human endogenous retrovirus-like elements; This family includes aspartate proteases from retroelements with LTR (long terminal repeats) including the RTVL_H family of human endogenous retrovirus-like elements. While fungal and mammalian pepsins are bilobal proteins with structurally related N- and C-termini, 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: 133159 Cd Length: 86 Bit Score: 40.78 E-value: 2.14e-05
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Blast search parameters | ||||
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