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Conserved domains on  [gi|2786866398|ref|WP_370030852|]
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retroviral-like aspartic protease family protein [Qipengyuania mesophila]

Protein Classification

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

EC:  3.4.23.-
Gene Ontology:  GO:0004190|GO:0006508
PubMed:  8439290|1851433

Graphical summary

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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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  33 RLTVPVTIGGnGPYRFLVDTGAQATVVSHDIAEDLALPRR--GQAMLVAMGSAQRVDMVEVDELSFADRSITRLLSPLLH 110
Cdd:cd05483     2 HFVVPVTING-QPVRFLLDTGASTTVISEELAERLGLPLTlgGKVTVQTANGRVRAARVRLDSLQIGGITLRNVPAVVLP 80
                          90
                  ....*....|....*.
gi 2786866398 111 AGNIGADGILGLDSLQ 126
Cdd:cd05483    81 GDALGVDGLLGMDFLR 96
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398 170 DATVDDIRISVIIDTGAQGSTGNRALLRKLRTRAQGEISATDVHGV--RVLSDLSYVRQLEIGGMTMGNVPIGFTDSPTF 247
Cdd:pfam13650   2 PVTINGKPVRFLVDTGASGTVISPSLAERLGLKVRGLAYTVRVSTAggRVSAARVRLDSLRLGGLTLENVPALVLDLGDL 81

                  ....*...
gi 2786866398 248 HA--LGLD 253
Cdd:pfam13650  82 IDglLGMD 89
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  33 RLTVPVTIGGnGPYRFLVDTGAQATVVSHDIAEDLALPRR--GQAMLVAMGSAQRVDMVEVDELSFADRSITRLLSPLLH 110
Cdd:cd05483     2 HFVVPVTING-QPVRFLLDTGASTTVISEELAERLGLPLTlgGKVTVQTANGRVRAARVRLDSLQIGGITLRNVPAVVLP 80
                          90
                  ....*....|....*.
gi 2786866398 111 AGNIGADGILGLDSLQ 126
Cdd:cd05483    81 GDALGVDGLLGMDFLR 96
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  36 VPVTIGGNgPYRFLVDTGAQATVVSHDIAEDLALPRRGQAMLVAMGSA---QRVDMVEVDELSFADRSITRLlsPLLHAG 112
Cdd:pfam13975   1 VDVTINGR-PVRFLVDTGASVTVISEALAERLGLDRLVDAYPVTVRTAngtVRAARVRLDSVKIGGIELRNV--PAVVLP 77
                          90
                  ....*....|....
gi 2786866398 113 NIGADGILGLDSLQ 126
Cdd:pfam13975  78 GDLDDVLLGMDFLK 91
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398 170 DATVDDIRISVIIDTGAQGSTGNRALLRKLRTRAQGEISATDVHGV--RVLSDLSYVRQLEIGGMTMGNVPIGFTDSPTF 247
Cdd:pfam13650   2 PVTINGKPVRFLVDTGASGTVISPSLAERLGLKVRGLAYTVRVSTAggRVSAARVRLDSLRLGGLTLENVPALVLDLGDL 81

                  ....*...
gi 2786866398 248 HA--LGLD 253
Cdd:pfam13650  82 IDglLGMD 89
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398   3 AAASAQGPPPVDEGAEGVVADHALDRDRYERLTVPVTIGGNgPYRFLVDTGAQATVVSHDIAEDLALPRRGQAMLVAMGS 82
Cdd:COG3577    11 GRGVRAQLNPGQAPVSTGGGEVVLKRDRDGHFVVEGTINGQ-PVRFLVDTGASTVVLSESDARRLGLDPEDLGRPVRVQT 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2786866398  83 AQ---RVDMVEVDELSFADRSITRlLSPLLHAGNIGADGILGLDSLQDLRVLIDF 134
Cdd:COG3577    90 ANgvvRAARVRLDSVRIGGITLRN-VRAVVLPGGELDDGLLGMSFLGRLDFEIDG 143
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398 166 MVITDATVDDIRISVIIDTGAQGSTGNRALLRKLR--TRAQGEISATDVHGvRVLSDLSYVRQLEIGGMTMGNVPIGFTD 243
Cdd:cd05483     2 HFVVPVTINGQPVRFLLDTGASTTVISEELAERLGlpLTLGGKVTVQTANG-RVRAARVRLDSLQIGGITLRNVPAVVLP 80

                  ....*....
gi 2786866398 244 SPTFHALGL 252
Cdd:cd05483    81 GDALGVDGL 89
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398 128 LRVLIDFREERMRVADAASLGGNSGYEIIVRARRKlGQMVItDATVDDIRISVIIDTGAQGSTGNRALLRKLRTRAQGEI 207
Cdd:COG3577     5 LGLFFGGRGVRAQLNPGQAPVSTGGGEVVLKRDRD-GHFVV-EGTINGQPVRFLVDTGASTVVLSESDARRLGLDPEDLG 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2786866398 208 SATDVHGV--RVLSDLSYVRQLEIGGMTMGNVPIGFTDSP 245
Cdd:COG3577    83 RPVRVQTAngVVRAARVRLDSVRIGGITLRNVRAVVLPGG 122
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  33 RLTVPVTIGGnGPYRFLVDTGAQATVVSHDIAEDLALPRR--GQAMLVAMGSAQRVDMVEVDELSFADRSITRLLSPLLH 110
Cdd:cd05483     2 HFVVPVTING-QPVRFLLDTGASTTVISEELAERLGLPLTlgGKVTVQTANGRVRAARVRLDSLQIGGITLRNVPAVVLP 80
                          90
                  ....*....|....*.
gi 2786866398 111 AGNIGADGILGLDSLQ 126
Cdd:cd05483    81 GDALGVDGLLGMDFLR 96
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  36 VPVTIGGNgPYRFLVDTGAQATVVSHDIAEDLALPRRGQAMLVAMGSA---QRVDMVEVDELSFADRSITRLlsPLLHAG 112
Cdd:pfam13975   1 VDVTINGR-PVRFLVDTGASVTVISEALAERLGLDRLVDAYPVTVRTAngtVRAARVRLDSVKIGGIELRNV--PAVVLP 77
                          90
                  ....*....|....
gi 2786866398 113 NIGADGILGLDSLQ 126
Cdd:pfam13975  78 GDLDDVLLGMDFLK 91
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  36 VPVTIGGNgPYRFLVDTGAQATVVSHDIAEDLALPRRGQAMLVAMGSA---QRVDMVEVDELSFADRSITRlLSPLLHAG 112
Cdd:pfam13650   1 VPVTINGK-PVRFLVDTGASGTVISPSLAERLGLKVRGLAYTVRVSTAggrVSAARVRLDSLRLGGLTLEN-VPALVLDL 78
                          90
                  ....*....|.
gi 2786866398 113 NIGADGILGLD 123
Cdd:pfam13650  79 GDLIDGLLGMD 89
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398 170 DATVDDIRISVIIDTGAQGSTGNRALLRKLRTRAQGEISATDVHGV--RVLSDLSYVRQLEIGGMTMGNVPIGFTDSPTF 247
Cdd:pfam13650   2 PVTINGKPVRFLVDTGASGTVISPSLAERLGLKVRGLAYTVRVSTAggRVSAARVRLDSLRLGGLTLENVPALVLDLGDL 81

                  ....*...
gi 2786866398 248 HA--LGLD 253
Cdd:pfam13650  82 IDglLGMD 89
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398   3 AAASAQGPPPVDEGAEGVVADHALDRDRYERLTVPVTIGGNgPYRFLVDTGAQATVVSHDIAEDLALPRRGQAMLVAMGS 82
Cdd:COG3577    11 GRGVRAQLNPGQAPVSTGGGEVVLKRDRDGHFVVEGTINGQ-PVRFLVDTGASTVVLSESDARRLGLDPEDLGRPVRVQT 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2786866398  83 AQ---RVDMVEVDELSFADRSITRlLSPLLHAGNIGADGILGLDSLQDLRVLIDF 134
Cdd:COG3577    90 ANgvvRAARVRLDSVRIGGITLRN-VRAVVLPGGELDDGLLGMSFLGRLDFEIDG 143
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  30 RYERLTVPVTIGGNgPYRFLVDTGAQATVVSHDIAEDLALPR----RGQAMLVAMGSAQ---RVDMVEVD-ELSFADRSI 101
Cdd:cd05479    13 KVPMLYINVEINGV-PVKAFVDSGAQMTIMSKACAEKCGLMRlidkRFQGIAKGVGTQKilgRIHLAQVKiGNLFLPCSF 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2786866398 102 TRLlspllhaGNIGADGILGLDSLQDLRVLIDFREERMRV 141
Cdd:cd05479    92 TVL-------EDDDVDFLIGLDMLKRHQCVIDLKENVLRI 124
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398 166 MVITDATVDDIRISVIIDTGAQGSTGNRALLRKLR--TRAQGEISATDVHGvRVLSDLSYVRQLEIGGMTMGNVPIGFTD 243
Cdd:cd05483     2 HFVVPVTINGQPVRFLLDTGASTTVISEELAERLGlpLTLGGKVTVQTANG-RVRAARVRLDSLQIGGITLRNVPAVVLP 80

                  ....*....
gi 2786866398 244 SPTFHALGL 252
Cdd:cd05483    81 GDALGVDGL 89
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  36 VPVTIGGNgPYRFLVDTGAQATVVSHDIAEDLALPRR----GQAMLVAMGSAQRVDMVEVD-ELSFADRSITR--LLSPL 108
Cdd:cd00303     1 LKGKINGV-PVRALVDSGASVNFISESLAKKLGLPPRllptPLKVKGANGSSVKTLGVILPvTIGIGGKTFTVdfYVLDL 79
                          90
                  ....*....|....*...
gi 2786866398 109 LHagnigADGILGLDSLQ 126
Cdd:cd00303    80 LS-----YDVILGRPWLE 92
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398 128 LRVLIDFREERMRVADAASLGGNSGYEIIVRARRKlGQMVItDATVDDIRISVIIDTGAQGSTGNRALLRKLRTRAQGEI 207
Cdd:COG3577     5 LGLFFGGRGVRAQLNPGQAPVSTGGGEVVLKRDRD-GHFVV-EGTINGQPVRFLVDTGASTVVLSESDARRLGLDPEDLG 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2786866398 208 SATDVHGV--RVLSDLSYVRQLEIGGMTMGNVPIGFTDSP 245
Cdd:COG3577    83 RPVRVQTAngVVRAARVRLDSVRIGGITLRNVRAVVLPGG 122
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398  34 LTVPVTIGGNgPYRFLVDTGAQATVVSHDIAEDLALPR----RGQAMLVAMGSAQRVDMVEVDELSFADRSITRLLSPLl 109
Cdd:pfam09668  25 LYINCEINGV-PVKAFVDSGAQTSIMSPRCAERCGIMRlvdtRFAGIAKGVGTARILGRIHMADVKIGGLFLPCSFSVI- 102
                          90       100
                  ....*....|....*....|....
gi 2786866398 110 haGNIGADGILGLDSLQDLRVLID 133
Cdd:pfam09668 103 --EGQDMDLLLGLDMLKRHQCCID 124
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2786866398 169 TDATVDDIRISVIIDTGAQGSTGNRALLRKL---RTRAQGEISATDVHGvRVLSDLSYVRQLEIGGMTMGNVPIGFTDSP 245
Cdd:pfam13975   1 VDVTINGRPVRFLVDTGASVTVISEALAERLgldRLVDAYPVTVRTANG-TVRAARVRLDSVKIGGIELRNVPAVVLPGD 79

                  ....*....
gi 2786866398 246 TFHA-LGLD 253
Cdd:pfam13975  80 LDDVlLGMD 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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