NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21040362|ref|NP_620477|]
View 

beta-secretase 2 isoform B preproprotein [Homo sapiens]

Protein Classification

pepsin/retropepsin-like aspartic protease family protein( domain architecture ID 27721)

pepsin/retropepsin-like aspartic protease family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
pepsin_retropepsin_like super family cl11403
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
89-393 0e+00

Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular and retroviral pepsin-like aspartate proteases. The cellular pepsin and pepsin-like enzymes are twice as long as their retroviral counterparts. The cellular pepsin-like aspartic proteases are found in mammals, plants, fungi and bacteria. These well known and extensively characterized enzymes include pepsins, chymosin, rennin, cathepsins, and fungal aspartic proteases. Several have long been known to be medically (rennin, cathepsin D and E, pepsin) or commercially (chymosin) important. The eukaryotic pepsin-like proteases contain two domains possessing similar topological features. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except in the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The eukaryotic pepsin-like proteases have two active site ASP residues with each N- and C-terminal lobe contributing one residue. While the fungal and mammalian pepsins are bilobal proteins, retropepsins function as dimers and the monomer resembles structure of the N- or C-terminal domains of eukaryotic enzyme. The active site motif (Asp-Thr/Ser-Gly-Ser) is conserved between the retroviral and eukaryotic proteases and between the N-and C-terminal of eukaryotic pepsin-like proteases. The retropepsin-like family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements; as well as eukaryotic DNA-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. Retropepsin 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. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A) and A2 (retropepsin family).


The actual alignment was detected with superfamily member cd05473:

Pssm-ID: 472175 [Multi-domain]  Cd Length: 364  Bit Score: 597.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  89 GRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKG 168
Cdd:cd05473   1 GQGYYIEMLIGTPPQKLNILVDTGSSNFAVAAAPHPFIHTYFHRELSSTYRDLGKGVTVPYTQGSWEGELGTDLVSIPKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 169 FNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAG--SGTNG 246
Cdd:cd05473  81 PNVTFRANIAAITESENFFLNGSNWEGILGLAYAELARPDSSVEPFFDSLVKQTGIPDVFSLQMCGAGLPVNGsaSGTVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 247 GSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARA 326
Cdd:cd05473 161 GSMVIGGIDPSLYKGDIWYTPIREEWYYEVIILKLEVGGQSLNLDCKEYNYDKAIVDSGTTNLRLPVKVFNAAVDAIKAA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21040362 327 SLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQK-LQ-------VLQCLKFpGLSQ 393
Cdd:cd05473 241 SLIEDFPDGFWLGSQLACWQKGTTPWEIFPKISIYLRDENSSQSFRITILPQLyLRpvedhgtQLDCYKF-AISQ 314
 
Name Accession Description Interval E-value
beta_secretase_like cd05473
Beta-secretase, aspartic-acid protease important in the pathogenesis of Alzheimer's disease; ...
89-393 0e+00

Beta-secretase, aspartic-acid protease important in the pathogenesis of Alzheimer's disease; Beta-secretase also called BACE (beta-site of APP cleaving enzyme) or memapsin-2. Beta-secretase is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths in peripheral nerve cells. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. Beta-secretase is a member of pepsin family of aspartic proteases. Same as other aspartic proteases, beta-secretase is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The enzymes specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133140 [Multi-domain]  Cd Length: 364  Bit Score: 597.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  89 GRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKG 168
Cdd:cd05473   1 GQGYYIEMLIGTPPQKLNILVDTGSSNFAVAAAPHPFIHTYFHRELSSTYRDLGKGVTVPYTQGSWEGELGTDLVSIPKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 169 FNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAG--SGTNG 246
Cdd:cd05473  81 PNVTFRANIAAITESENFFLNGSNWEGILGLAYAELARPDSSVEPFFDSLVKQTGIPDVFSLQMCGAGLPVNGsaSGTVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 247 GSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARA 326
Cdd:cd05473 161 GSMVIGGIDPSLYKGDIWYTPIREEWYYEVIILKLEVGGQSLNLDCKEYNYDKAIVDSGTTNLRLPVKVFNAAVDAIKAA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21040362 327 SLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQK-LQ-------VLQCLKFpGLSQ 393
Cdd:cd05473 241 SLIEDFPDGFWLGSQLACWQKGTTPWEIFPKISIYLRDENSSQSFRITILPQLyLRpvedhgtQLDCYKF-AISQ 314
Asp pfam00026
Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and ...
91-323 7.07e-38

Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and renins. Two-domain structure, probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (pfam00077), which are much smaller and appear to be homologous to a single domain of the eukaryotic asp proteases.


Pssm-ID: 394983 [Multi-domain]  Cd Length: 313  Bit Score: 138.95  E-value: 7.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362    91 GYYLEMLIGTPPQKLQILVDTGSSNFAVagtPHSYIDTY--------FDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDL 162
Cdd:pfam00026   1 EYFGTISIGTPPQKFTVIFDTGSSDLWV---PSSYCTKSsackshgtFDPSSSSTYKLNGTTFSISYGDGSASGFLGQDT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   163 VTIPKGFNTSFLVNIATiFESENFFLPGiKWNGILGLAYATLAkpSSSLETFFDSLVTQANIP-NVFSMQMcgaglpvAG 241
Cdd:pfam00026  78 VTVGGLTITNQEFGLAT-KEPGSFFEYA-KFDGILGLGFPSIS--AVGATPVFDNLKSQGLIDsPAFSVYL-------NS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   242 SGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNldCREynADKAIVDSGTTLLRLPQKVFDAVVE 321
Cdd:pfam00026 147 PDAAGGEIIFGGVDPSKYTGSLTYVPVTSQGYWQITLDSVTVGGSTSA--CSS--GCQAILDTGTSLLYGPTSIVSKIAK 222

                  ..
gi 21040362   322 AV 323
Cdd:pfam00026 223 AV 224
PTZ00147 PTZ00147
plasmepsin-1; Provisional
92-321 2.05e-17

plasmepsin-1; Provisional


Pssm-ID: 140176 [Multi-domain]  Cd Length: 453  Bit Score: 83.38  E-value: 2.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   92 YYLEMLIGTPPQKLQILVDTGSSNFAVAG----TPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPk 167
Cdd:PTZ00147 140 SYGEAKLGDNGQKFNFIFDTGSANLWVPSikctTEGCETKNLYDSSKSKTYEKDGTKVEMNYVSGTVSGFFSKDLVTIG- 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  168 gfNTSFLVNIATIFESENF--FLPGIKWNGILGLAYATLAkpSSSLETFFDSLVTQANIPN-VFSMQmcgagLPVagSGT 244
Cdd:PTZ00147 219 --NLSVPYKFIEVTDTNGFepFYTESDFDGIFGLGWKDLS--IGSVDPYVVELKNQNKIEQaVFTFY-----LPP--EDK 287
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21040362  245 NGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEiLKLEIGgqslNLDCREYNadkAIVDSGTTLLRLPQKVFDAVVE 321
Cdd:PTZ00147 288 HKGYLTIGGIEERFYEGPLTYEKLNHDLYWQVD-LDVHFG----NVSSEKAN---VIVDSGTSVITVPTEFLNKFVE 356
 
Name Accession Description Interval E-value
beta_secretase_like cd05473
Beta-secretase, aspartic-acid protease important in the pathogenesis of Alzheimer's disease; ...
89-393 0e+00

Beta-secretase, aspartic-acid protease important in the pathogenesis of Alzheimer's disease; Beta-secretase also called BACE (beta-site of APP cleaving enzyme) or memapsin-2. Beta-secretase is an aspartic-acid protease important in the pathogenesis of Alzheimer's disease, and in the formation of myelin sheaths in peripheral nerve cells. It cleaves amyloid precursor protein (APP) to reveal the N-terminus of the beta-amyloid peptides. The beta-amyloid peptides are the major components of the amyloid plaques formed in the brain of patients with Alzheimer's disease (AD). Since BACE mediates one of the cleavages responsible for generation of AD, it is regarded as a potential target for pharmacological intervention in AD. Beta-secretase is a member of pepsin family of aspartic proteases. Same as other aspartic proteases, beta-secretase is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The enzymes specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133140 [Multi-domain]  Cd Length: 364  Bit Score: 597.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  89 GRGYYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPKG 168
Cdd:cd05473   1 GQGYYIEMLIGTPPQKLNILVDTGSSNFAVAAAPHPFIHTYFHRELSSTYRDLGKGVTVPYTQGSWEGELGTDLVSIPKG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 169 FNTSFLVNIATIFESENFFLPGIKWNGILGLAYATLAKPSSSLETFFDSLVTQANIPNVFSMQMCGAGLPVAG--SGTNG 246
Cdd:cd05473  81 PNVTFRANIAAITESENFFLNGSNWEGILGLAYAELARPDSSVEPFFDSLVKQTGIPDVFSLQMCGAGLPVNGsaSGTVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 247 GSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQKVFDAVVEAVARA 326
Cdd:cd05473 161 GSMVIGGIDPSLYKGDIWYTPIREEWYYEVIILKLEVGGQSLNLDCKEYNYDKAIVDSGTTNLRLPVKVFNAAVDAIKAA 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21040362 327 SLIPEFSDGFWTGSQLACWTNSETPWSYFPKISIYLRDENSSRSFRITILPQK-LQ-------VLQCLKFpGLSQ 393
Cdd:cd05473 241 SLIEDFPDGFWLGSQLACWQKGTTPWEIFPKISIYLRDENSSQSFRITILPQLyLRpvedhgtQLDCYKF-AISQ 314
pepsin_like cd05471
Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH; ...
92-362 1.33e-50

Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH; Pepsin-like aspartic proteases are found in mammals, plants, fungi and bacteria. These well known and extensively characterized enzymes include pepsins, chymosin, renin, cathepsins, and fungal aspartic proteases. Several have long been known to be medically (renin, cathepsin D and E, pepsin) or commercially (chymosin) important. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Aspartate residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. Most members of the pepsin family specifically cleave bonds in peptides that are at least six residues in length, with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap.The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133138 [Multi-domain]  Cd Length: 283  Bit Score: 171.45  E-value: 1.33e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGTP------HSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTI 165
Cdd:cd05471   1 YYGEITIGTPPQKFSVIFDTGSSLLWVPSSNctscscQKHPRFKYDSSKSSTYKDTGCTFSITYGDGSVTGGLGTDTVTI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 166 PKGFNTSFLVNIATifeSENFFLPGIKWNGILGLAYATLAKPSSSleTFFDSLVTQANIP-NVFSMQmcgagLPVAGSGT 244
Cdd:cd05471  81 GGLTIPNQTFGCAT---SESGDFSSSGFDGILGLGFPSLSVDGVP--SFFDQLKSQGLISsPVFSFY-----LGRDGDGG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 245 NGGSLVLGGIEPSLYKGDIWYTPI--KEEWYYQIEILKLEIGGQSLNLDCREYNadkAIVDSGTTLLRLPQKVFDAVVEA 322
Cdd:cd05471 151 NGGELTFGGIDPSKYTGDLTYTPVvsNGPGYWQVPLDGISVGGKSVISSSGGGG---AIVDSGTSLIYLPSSVYDAILKA 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 21040362 323 VARAslipefsdgfwTGSQLACWTNSETPWSYFPKISIYL 362
Cdd:cd05471 228 LGAA-----------VSSSDGGYGVDCSPCDTLPDITFTF 256
Asp pfam00026
Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and ...
91-323 7.07e-38

Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and renins. Two-domain structure, probably arising from ancestral duplication. This family does not include the retroviral nor retrotransposon proteases (pfam00077), which are much smaller and appear to be homologous to a single domain of the eukaryotic asp proteases.


Pssm-ID: 394983 [Multi-domain]  Cd Length: 313  Bit Score: 138.95  E-value: 7.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362    91 GYYLEMLIGTPPQKLQILVDTGSSNFAVagtPHSYIDTY--------FDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDL 162
Cdd:pfam00026   1 EYFGTISIGTPPQKFTVIFDTGSSDLWV---PSSYCTKSsackshgtFDPSSSSTYKLNGTTFSISYGDGSASGFLGQDT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   163 VTIPKGFNTSFLVNIATiFESENFFLPGiKWNGILGLAYATLAkpSSSLETFFDSLVTQANIP-NVFSMQMcgaglpvAG 241
Cdd:pfam00026  78 VTVGGLTITNQEFGLAT-KEPGSFFEYA-KFDGILGLGFPSIS--AVGATPVFDNLKSQGLIDsPAFSVYL-------NS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   242 SGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNldCREynADKAIVDSGTTLLRLPQKVFDAVVE 321
Cdd:pfam00026 147 PDAAGGEIIFGGVDPSKYTGSLTYVPVTSQGYWQITLDSVTVGGSTSA--CSS--GCQAILDTGTSLLYGPTSIVSKIAK 222

                  ..
gi 21040362   322 AV 323
Cdd:pfam00026 223 AV 224
gastricsin cd05477
Gastricsins, asparate proteases produced in gastric mucosa; Gastricsin is also called ...
92-323 2.51e-34

Gastricsins, asparate proteases produced in gastric mucosa; Gastricsin is also called pepsinogen C. Gastricsins are produced in gastric mucosa of mammals. It is synthesized by the chief cells in the stomach as an inactive zymogen. It is self-converted to a mature enzyme under acidic conditions. Human gastricsin is distributed throughout all parts of the stomach. Gastricsin is synthesized as an inactive progastricsin that has an approximately 40 residue prosequence. It is self-converting to a mature enzyme being triggered by a drop in pH from neutrality to acidic conditions. Like other aspartic proteases, gastricsin are characterized by two catalytic aspartic residues at the active site, and display optimal activity at acidic pH. Mature enzyme has a pseudo-2-fold symmetry that passes through the active site between the catalytic aspartate residues. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic aspartate residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. Although the three-dimensional structures of the two lobes are very similar, the amino acid sequences are more divergent, except for the conserved catalytic site motif. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133144 [Multi-domain]  Cd Length: 318  Bit Score: 129.62  E-value: 2.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGT----PHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPK 167
Cdd:cd05477   4 YYGEISIGTPPQNFLVLFDTGSSNLWVPSVlcqsQACTNHTKFNPSQSSTYSTNGETFSLQYGSGSLTGIFGYDTVTVQG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 168 GFNTSFLVNIATIFESENFFLPgiKWNGILGLAYATLAKPSSSleTFFDSLVTQANIP-NVFSMQMCGAglpvagSGTNG 246
Cdd:cd05477  84 IIITNQEFGLSETEPGTNFVYA--QFDGILGLAYPSISAGGAT--TVMQGMMQQNLLQaPIFSFYLSGQ------QGQQG 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21040362 247 GSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLdCREynADKAIVDSGTTLLRLPQKVFDAVVEAV 323
Cdd:cd05477 154 GELVFGGVDNNLYTGQIYWTPVTSETYWQIGIQGFQINGQATGW-CSQ--GCQAIVDTGTSLLTAPQQVMSTLMQSI 227
pepsin_A cd05478
Pepsin A, aspartic protease produced in gastric mucosa of mammals; Pepsin, a well-known ...
92-313 1.10e-31

Pepsin A, aspartic protease produced in gastric mucosa of mammals; Pepsin, a well-known aspartic protease, is produced by the human gastric mucosa in seven different zymogen isoforms, subdivided into two types: pepsinogen A and pepsinogen C. The prosequence of the zymogens are self cleaved under acidic pH. The mature enzymes are called pepsin A and pepsin C, correspondingly. The well researched porcine pepsin is also in this pepsin A family. Pepsins play an integral role in the digestion process of vertebrates. Pepsins are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. More recently evolved enzymes have similar three-dimensional structures, however their amino acid sequences are more divergent except for the conserved catalytic site motif. Pepsins specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133145 [Multi-domain]  Cd Length: 317  Bit Score: 122.17  E-value: 1.10e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVagtPHSYIDT-------YFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVT 164
Cdd:cd05478  11 YYGTISIGTPPQDFTVIFDTGSSNLWV---PSVYCSSqacsnhnRFNPRQSSTYQSTGQPLSIQYGTGSMTGILGYDTVQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 165 IPKGFNTSFLVNIAtifESE-NFFLPGIKWNGILGLAYATLAkpSSSLETFFDSLVTQANIP-NVFSMQMcgaglpvAGS 242
Cdd:cd05478  88 VGGISDTNQIFGLS---ETEpGSFFYYAPFDGILGLAYPSIA--SSGATPVFDNMMSQGLVSqDLFSVYL-------SSN 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21040362 243 GTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNldCREynADKAIVDSGTTLLRLPQ 313
Cdd:cd05478 156 GQQGSVVTFGGIDPSYYTGSLNWVPVTAETYWQITVDSVTINGQVVA--CSG--GCQAIVDTGTSLLVGPS 222
Cathepsin_D2 cd05490
Cathepsin_D2, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase of ...
92-329 8.79e-31

Cathepsin_D2, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase of the lysosomal compartment where it functions in protein catabolism. It is a member of the pepsin family of proteinases. This enzyme is distinguished from other members of the pepsin family by two features that are characteristic of lysosomal hydrolases. First, mature Cathepsin D is found predominantly in a two-chain form due to a posttranslational cleavage event. Second, it contains phosphorylated, N-linked oligosaccharides that target the enzyme to lysosomes via mannose-6-phosphate receptors. Cathepsin D preferentially attacks peptide bonds flanked by bulky hydrophobic amino acids and its pH optimum is between pH 2.8 and 4.0. Two active site aspartic acid residues are essential for the catalytic activity of aspartic proteinases. Like other aspartic proteinases, Cathepsin D is a bilobed molecule; the two evolutionary related lobes are mostly made up of beta-sheets and flank a deep active site cleft. Each of the two related lobes contributes one active site aspartic acid residue and contains a single carbohydrate group. Cathepsin D is an essential enzyme. Mice deficient for proteinase cathepsin D, generated by gene targeting, develop normally during the first 2 weeks, stop thriving in the third week and die in a state of anorexia in the fourth week. The mice develop atrophy of ileal mucosa followed by other degradation of intestinal organs. In these knockout mice, lysosomal proteolysis was normal. These results suggest that vital functions of cathepsin D are exerted by limited proteolysis of proteins regulating cell growth and/or tissue homeostasis, while its contribution to bulk proteolysis in lysosomes appears to be non-critical. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133157 [Multi-domain]  Cd Length: 325  Bit Score: 119.90  E-value: 8.79e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDT------YFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTI 165
Cdd:cd05490   7 YYGEIGIGTPPQTFTVVFDTGSSNLWVPSVHCSLLDIacwlhhKYNSSKSSTYVKNGTEFAIQYGSGSLSGYLSQDTVSI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 166 PKgfntsflVNIATIFESENFFLPGI-----KWNGILGLAYATLAkpSSSLETFFDSLVTQANIP-NVFSMQmcgagLPV 239
Cdd:cd05490  87 GG-------LQVEGQLFGEAVKQPGItfiaaKFDGILGMAYPRIS--VDGVTPVFDNIMAQKLVEqNVFSFY-----LNR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 240 AGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQsLNLdCREynADKAIVDSGTTLLRLPQKVFDAV 319
Cdd:cd05490 153 DPDAQPGGELMLGGTDPKYYTGDLHYVNVTRKAYWQIHMDQVDVGSG-LTL-CKG--GCEAIVDTGTSLITGPVEEVRAL 228
                       250
                ....*....|
gi 21040362 320 VEAVARASLI 329
Cdd:cd05490 229 QKAIGAVPLI 238
Proteinase_A_fungi cd05488
Fungal Proteinase A , aspartic proteinase superfamily; Fungal Proteinase A, a proteolytic ...
92-315 2.62e-29

Fungal Proteinase A , aspartic proteinase superfamily; Fungal Proteinase A, a proteolytic enzyme distributed among a variety of organisms, is a member of the aspartic proteinase superfamily. In Saccharomyces cerevisiae, targeted to the vacuole as a zymogen, activation of proteinases A at acidic pH can occur by two different pathways: a one-step process to release mature proteinase A, involving the intervention of proteinase B, or a step-wise pathway via the auto-activation product known as pseudo-proteinase A. Once active, S. cerevisiae proteinase A is essential to the activities of other yeast vacuolar hydrolases, including proteinase B and carboxypeptidase Y. The mature enzyme is bilobal, with each lobe providing one of the two catalytically essential aspartic acid residues in the active site. The crystal structure of free proteinase A shows that flap loop is atypically pointing directly into the S(1) pocket of the enzyme. Proteinase A preferentially hydrolyzes hydrophobic residues such as Phe, Leu or Glu at the P1 position and Phe, Ile, Leu or Ala at P1'. Moreover, the enzyme is inhibited by IA3, a natural and highly specific inhibitor produced by S. cerevisiae. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133155 [Multi-domain]  Cd Length: 320  Bit Score: 116.00  E-value: 2.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDTY----FDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIpk 167
Cdd:cd05488  11 YFTDITLGTPPQKFKVILDTGSSNLWVPSVKCGSIACFlhskYDSSASSTYKANGTEFKIQYGSGSLEGFVSQDTLSI-- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 168 gfnTSFLVNIATIFE--SEnfflPGI-----KWNGILGLAYATLAKPSssLETFFDSLVTQANI-PNVFSMQMcgaglpv 239
Cdd:cd05488  89 ---GDLTIKKQDFAEatSE----PGLafafgKFDGILGLAYDTISVNK--IVPPFYNMINQGLLdEPVFSFYL------- 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21040362 240 AGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLDcreynADKAIVDSGTTLLRLPQKV 315
Cdd:cd05488 153 GSSEEDGGEATFGGIDESRFTGKITWLPVRRKAYWEVELEKIGLGDEELELE-----NTGAAIDTGTSLIALPSDL 223
Cathepsin_D_like cd05485
Cathepsin_D_like, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase ...
92-329 4.57e-26

Cathepsin_D_like, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase of the lysosomal compartment where it functions in protein catabolism. It is a member of the pepsin family of proteinases. This enzyme is distinguished from other members of the pepsin family by two features that are characteristic of lysosomal hydrolases. First, mature Cathepsin D is found predominantly in a two-chain form due to a posttranslational cleavage event. Second, it contains phosphorylated, N-linked oligosaccharides that target the enzyme to lysosomes via mannose-6-phosphate receptors. Cathepsin D preferentially attacks peptide bonds flanked by bulky hydrophobic amino acids and its pH optimum is between pH 2.8 and 4.0. Two active site aspartic acid residues are essential for the catalytic activity of aspartic proteinases. Like other aspartic proteinases, Cathepsin D is a bilobed molecule; the two evolutionary related lobes are mostly made up of beta-sheets and flank a deep active site cleft. Each of the two related lobes contributes one active site aspartic acid residue and contains a single carbohydrate group. Cathepsin D is an essential enzyme. Mice deficient for proteinase cathepsin D, generated by gene targeting, develop normally during the first 2 weeks, stop thriving in the third week and die in a state of anorexia in the fourth week. The mice develop atrophy of ileal mucosa followed by other degradation of intestinal organs. In these knockout mice, lysosomal proteolysis was normal. These results suggest that vital functions of cathepsin D are exerted by limited proteolysis of proteins regulating cell growth and/or tissue homeostasis, while its contribution to bulk proteolysis in lysosomes appears to be non-critical. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133152 [Multi-domain]  Cd Length: 329  Bit Score: 107.24  E-value: 4.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYID------TYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTI 165
Cdd:cd05485  12 YYGVITIGTPPQSFKVVFDTGSSNLWVPSKKCSWTNiacllhNKYDSTKSSTYKKNGTEFAIQYGSGSLSGFLSTDTVSV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 166 pkgfnTSFLVNIATIFESENffLPGI-----KWNGILGLAYATLAkpSSSLETFFDSLVTQANIPN-VFSMQmcgagLPV 239
Cdd:cd05485  92 -----GGVSVKGQTFAEAIN--EPGLtfvaaKFDGILGMGYSSIS--VDGVVPVFYNMVNQKLVDApVFSFY-----LNR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 240 AGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLnldCReyNADKAIVDSGTTLLRLPQKVFDAV 319
Cdd:cd05485 158 DPSAKEGGELILGGSDPKHYTGNFTYLPVTRKGYWQFKMDSVSVGEGEF---CS--GGCQAIADTGTSLIAGPVDEIEKL 232
                       250
                ....*....|
gi 21040362 320 VEAVARASLI 329
Cdd:cd05485 233 NNAIGAKPII 242
renin_like cd05487
Renin stimulates production of angiotensin and thus affects blood pressure; Renin, also known ...
92-323 4.29e-25

Renin stimulates production of angiotensin and thus affects blood pressure; Renin, also known as angiotensinogenase, is a circulating enzyme that participates in the renin-angiotensin system that mediates extracellular volume, arterial vasoconstriction, and consequently mean arterial blood pressure. The enzyme is secreted by the kidneys from specialized juxtaglomerular cells in response to decreases in glomerular filtration rate (a consequence of low blood volume), diminished filtered sodium chloride and sympathetic nervous system innervation. The enzyme circulates in the blood stream and hydrolyzes angiotensinogen secreted from the liver into the peptide angiotensin I. Angiotensin I is further cleaved in the lungs by endothelial bound angiotensin converting enzyme (ACE) into angiotensin II, the final active peptide. Renin is a member of the aspartic protease family. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Aspartate residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133154 [Multi-domain]  Cd Length: 326  Bit Score: 104.47  E-value: 4.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYIDT------YFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTI 165
Cdd:cd05487   9 YYGEIGIGTPPQTFKVVFDTGSSNLWVPSSKCSPLYTacvthnLYDASDSSTYKENGTEFTIHYASGTVKGFLSQDIVTV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 166 PKgfntsflVNIATIFeSENFFLPGI-----KWNGILGLAYATLAkpSSSLETFFDSLVTQANIP-NVFSMQMCGaglpv 239
Cdd:cd05487  89 GG-------IPVTQMF-GEVTALPAIpfmlaKFDGVLGMGYPKQA--IGGVTPVFDNIMSQGVLKeDVFSVYYSR----- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 240 AGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGgqSLNLDCREYNAdkAIVDSGTTLLRLPQKVFDAV 319
Cdd:cd05487 154 DSSHSLGGEIVLGGSDPQHYQGDFHYINTSKTGFWQIQMKGVSVG--SSTLLCEDGCT--AVVDTGASFISGPTSSISKL 229

                ....
gi 21040362 320 VEAV 323
Cdd:cd05487 230 MEAL 233
Cathespin_E cd05486
Cathepsin E, non-lysosomal aspartic protease; Cathepsin E is an intracellular, non-lysosomal ...
92-314 4.46e-24

Cathepsin E, non-lysosomal aspartic protease; Cathepsin E is an intracellular, non-lysosomal aspartic protease expressed in a variety of cells and tissues. The protease has proposed physiological roles in antigen presentation by the MHC class II system, in the biogenesis of the vasoconstrictor peptide endothelin, and in neurodegeneration associated with brain ischemia and aging. Cathepsin E is the only A1 aspartic protease that exists as a homodimer with a disulfide bridge linking the two monomers. Like many other aspartic proteases, it is synthesized as a zymogen which is catalytically inactive towards its natural substrates at neutral pH and which auto-activates in an acidic environment. The overall structure follows the general fold of aspartic proteases of the A1 family, it is composed of two structurally similar beta barrel lobes, each lobe contributing an aspartic acid residue to form a catalytic dyad that acts to cleave the substrate peptide bond. The catalytic Asp residues are contained in an Asp-Thr-Gly-Ser/thr motif in both N- and C-terminal lobes of the enzyme. The aspartic acid residues act together to allow a water molecule to attack the peptide bond. One aspartic acid residue (in its deprotonated form) activates the attacking water molecule, whereas the other aspartic acid residue (in its protonated form) polarizes the peptide carbonyl, increasing its susceptibility to attack. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133153 [Multi-domain]  Cd Length: 316  Bit Score: 101.11  E-value: 4.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAV--------AGTPHSYidtyFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLV 163
Cdd:cd05486   1 YFGQISIGTPPQNFTVIFDTGSSNLWVpsiyctsqACTKHNR----FQPSESSTYVSNGEAFSIQYGTGSLTGIIGIDQV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 164 TIpKG---FNTSFLVNIA---TIFESENFflpgikwNGILGLAYATLAkpSSSLETFFDSLVTQanipNVFSMQMCGAGL 237
Cdd:cd05486  77 TV-EGitvQNQQFAESVSepgSTFQDSEF-------DGILGLAYPSLA--VDGVTPVFDNMMAQ----NLVELPMFSVYM 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21040362 238 PVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNldCREynADKAIVDSGTTLLRLPQK 314
Cdd:cd05486 143 SRNPNSADGGELVFGGFDTSRFSGQLNWVPVTVQGYWQIQLDNIQVGGTVIF--CSD--GCQAIVDTGTSLITGPSG 215
phytepsin cd06098
Phytepsin, a plant homolog of mammalian lysosomal pepsins; Phytepsin, a plant homolog of ...
92-328 1.02e-23

Phytepsin, a plant homolog of mammalian lysosomal pepsins; Phytepsin, a plant homolog of mammalian lysosomal pepsins, resides in grains, roots, stems, leaves and flowers. Phytepsin may participate in metabolic turnover and in protein processing events. In addition, it highly expressed in several plant tissues undergoing apoptosis. Phytepsin contains an internal region consisting of about 100 residues not present in animal or microbial pepsins. This region is thus called a plant specific insert. The insert is highly similar to saponins, which are lysosomal sphingolipid-activating proteins in mammalian cells. The saponin-like domain may have a role in the vacuolar targeting of phytepsin. Phytepsin, as its animal counterparts, possesses a topology typical of all aspartic proteases. They are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe has probably evolved from the other through a gene duplication event in the distant past. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133162 [Multi-domain]  Cd Length: 317  Bit Score: 100.14  E-value: 1.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVagtPHS--------YIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLV 163
Cdd:cd06098  11 YFGEIGIGTPPQKFTVIFDTGSSNLWV---PSSkcyfsiacYFHSKYKSSKSSTYKKNGTSASIQYGTGSISGFFSQDSV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 164 TIpkgfnTSFLVN----IATIFESENFFLPGiKWNGILGLAYATL----AKP--SSSLEtffDSLVTQAnipnVFSMQmc 233
Cdd:cd06098  88 TV-----GDLVVKnqvfIEATKEPGLTFLLA-KFDGILGLGFQEIsvgkAVPvwYNMVE---QGLVKEP----VFSFW-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 234 gagLPVAGSGTNGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEILKLEIGGQSLNLdCREYNAdkAIVDSGTTLLRLPQ 313
Cdd:cd06098 153 ---LNRNPDEEEGGELVFGGVDPKHFKGEHTYVPVTRKGYWQFEMGDVLIGGKSTGF-CAGGCA--AIADSGTSLLAGPT 226
                       250
                ....*....|....*
gi 21040362 314 KVFDAVVEAVARASL 328
Cdd:cd06098 227 TIVTQINSAVDCNSL 241
Plasmepsin_5 cd06096
Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite; The ...
92-320 2.63e-22

Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite; The family contains a group of aspartic proteinases homologous to plasmepsin 5. Plasmepsins are a class of at least 10 enzymes produced by the plasmodium parasite. Through their haemoglobin-degrading activity, they are an important cause of symptoms in malaria sufferers. This family of enzymes is a potential target for anti-malarial drugs. Plasmepsins are aspartic acid proteases, which means their active site contains two aspartic acid residues. These two aspartic acid residue act respectively as proton donor and proton acceptor, catalyzing the hydrolysis of peptide bond in proteins. Aspartic proteinases are composed of two structurally similar beta barrel lobes, each lobe contributing an aspartic acid residue to form a catalytic dyad that acts to cleave the substrate peptide bond. The catalytic Asp residues are contained in an Asp-Thr-Gly-Ser/thr motif in both N- and C-terminal lobes of the enzyme. There are four types of plasmepsins, closely related but varying in the specificity of cleavage site. The name plasmepsin may come from plasmodium (the organism) and pepsin (a common aspartic acid protease with similar molecular structure). This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133160 [Multi-domain]  Cd Length: 326  Bit Score: 96.29  E-value: 2.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSS--NFAVAGTPH--SYIDTYFDTERSSTYRSKGFDV----------------TVKYTQ 151
Cdd:cd06096   4 YFIDIFIGNPPQKQSLILDTGSSslSFPCSQCKNcgIHMEPPYNLNNSITSSILYCDCnkccyclsclnnkceySISYSE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 152 GS-WTGFVGEDLVTIPKGFNTSFLVNI------ATIFEsENFFLPGIKwNGILGLAYatlaKPSSSLETFFDSLVTQANI 224
Cdd:cd06096  84 GSsISGFYFSDFVSFESYLNSNSEKESfkkifgCHTHE-TNLFLTQQA-TGILGLSL----TKNNGLPTPIILLFTKRPK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 225 PN---VFSmqMCgaglpvagSGTNGGSLVLGGIEPSLYKG----------DIWYTPIKEEWYYQIEILKLEIGGQSLNLD 291
Cdd:cd06096 158 LKkdkIFS--IC--------LSEDGGELTIGGYDKDYTVRnssignnkvsKIVWTPITRKYYYYVKLEGLSVYGTTSNSG 227
                       250       260
                ....*....|....*....|....*....
gi 21040362 292 crEYNADKAIVDSGTTLLRLPQKVFDAVV 320
Cdd:cd06096 228 --NTKGLGMLVDSGSTLSHFPEDLYNKIN 254
pepsin_retropepsin_like cd05470
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
95-199 3.65e-19

Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular and retroviral pepsin-like aspartate proteases. The cellular pepsin and pepsin-like enzymes are twice as long as their retroviral counterparts. The cellular pepsin-like aspartic proteases are found in mammals, plants, fungi and bacteria. These well known and extensively characterized enzymes include pepsins, chymosin, rennin, cathepsins, and fungal aspartic proteases. Several have long been known to be medically (rennin, cathepsin D and E, pepsin) or commercially (chymosin) important. The eukaryotic pepsin-like proteases contain two domains possessing similar topological features. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except in the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The eukaryotic pepsin-like proteases have two active site ASP residues with each N- and C-terminal lobe contributing one residue. While the fungal and mammalian pepsins are bilobal proteins, retropepsins function as dimers and the monomer resembles structure of the N- or C-terminal domains of eukaryotic enzyme. The active site motif (Asp-Thr/Ser-Gly-Ser) is conserved between the retroviral and eukaryotic proteases and between the N-and C-terminal of eukaryotic pepsin-like proteases. The retropepsin-like family includes pepsin-like aspartate proteases from retroviruses, retrotransposons and retroelements; as well as eukaryotic DNA-damage-inducible proteins (DDIs), and bacterial aspartate peptidases. Retropepsin 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. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A) and A2 (retropepsin family).


Pssm-ID: 133137 [Multi-domain]  Cd Length: 109  Bit Score: 82.04  E-value: 3.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  95 EMLIGTPPQKLQILVDTGSSNFAVAGTPHS-----YIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIpkGF 169
Cdd:cd05470   2 EIGIGTPPQTFNVLLDTGSSNLWVPSVDCQslaiySHSSYDDPSASSTYSDNGCTFSITYGTGSLSGGLSTDTVSI--GD 79
                        90       100       110
                ....*....|....*....|....*....|
gi 21040362 170 NTSFLVNIATIFESENFFLPGIKWNGILGL 199
Cdd:cd05470  80 IEVVGQAFGCATDEPGATFLPALFDGILGL 109
Aspergillopepsin_like cd06097
Aspergillopepsin_like, aspartic proteases of fungal origin; The members of this family are ...
92-336 1.22e-17

Aspergillopepsin_like, aspartic proteases of fungal origin; The members of this family are aspartic proteases of fungal origin, including aspergillopepsin, rhizopuspepsin, endothiapepsin, and rodosporapepsin. The various fungal species in this family may be the most economically important genus of fungi. They may serve as virulence factors or as industrial aids. For example, Aspergillopepsin from A. fumigatus is involved in invasive aspergillosis owing to its elastolytic activity and Aspergillopepsins from the mold A. saitoi are used in fermentation industry. Aspartic proteinases are a group of proteolytic enzymes in which the scissile peptide bond is attacked by a nucleophilic water molecule activated by two aspartic residues in a DT(S)G motif at the active site. They have a similar fold composed of two beta-barrel domains. Between the N-terminal and C-terminal domains, each of which contributes one catalytic aspartic residue, there is an extended active-site cleft capable of interacting with multiple residues of a substrate. Although members of the aspartic protease family of enzymes have very similar three-dimensional structures and catalytic mechanisms, each has unique substrate specificity. The members of this family has an optimal acidic pH (5.5) and cleaves protein substrates with similar specificity to that of porcine pepsin A, preferring hydrophobic residues at P1 and P1' in the cleave site. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133161 [Multi-domain]  Cd Length: 278  Bit Score: 82.35  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGT----PHSYIDTYFDTERSSTYRSK-GFDVTVKYTQGSW-TGFVGEDLVTI 165
Cdd:cd06097   1 YLTPVKIGTPPQTLNLDLDTGSSDLWVFSSetpaAQQGGHKLYDPSKSSTAKLLpGATWSISYGDGSSaSGIVYTDTVSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 166 pkGfntSFLVNIATI----FESENFFLPGIKwNGILGLAYATLAKPSS-SLETFFDSLVTQANIPnVFSmqmcgAGLPVA 240
Cdd:cd06097  81 --G---GVEVPNQAIelatAVSASFFSDTAS-DGLLGLAFSSINTVQPpKQKTFFENALSSLDAP-LFT-----ADLRKA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 241 GSGTnggsLVLGGIEPSLYKGDIWYTPI-KEEWYYQIEILKLEIGGQSLNLdcreYNADKAIVDSGTTLLRLPqkvfDAV 319
Cdd:cd06097 149 APGF----YTFGYIDESKYKGEISWTPVdNSSGFWQFTSTSYTVGGDAPWS----RSGFSAIADTGTTLILLP----DAI 216
                       250       260
                ....*....|....*....|
gi 21040362 320 VEAVARA---SLIPEFSDGF 336
Cdd:cd06097 217 VEAYYSQvpgAYYDSEYGGW 236
PTZ00147 PTZ00147
plasmepsin-1; Provisional
92-321 2.05e-17

plasmepsin-1; Provisional


Pssm-ID: 140176 [Multi-domain]  Cd Length: 453  Bit Score: 83.38  E-value: 2.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   92 YYLEMLIGTPPQKLQILVDTGSSNFAVAG----TPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPk 167
Cdd:PTZ00147 140 SYGEAKLGDNGQKFNFIFDTGSANLWVPSikctTEGCETKNLYDSSKSKTYEKDGTKVEMNYVSGTVSGFFSKDLVTIG- 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  168 gfNTSFLVNIATIFESENF--FLPGIKWNGILGLAYATLAkpSSSLETFFDSLVTQANIPN-VFSMQmcgagLPVagSGT 244
Cdd:PTZ00147 219 --NLSVPYKFIEVTDTNGFepFYTESDFDGIFGLGWKDLS--IGSVDPYVVELKNQNKIEQaVFTFY-----LPP--EDK 287
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21040362  245 NGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEiLKLEIGgqslNLDCREYNadkAIVDSGTTLLRLPQKVFDAVVE 321
Cdd:PTZ00147 288 HKGYLTIGGIEERFYEGPLTYEKLNHDLYWQVD-LDVHFG----NVSSEKAN---VIVDSGTSVITVPTEFLNKFVE 356
PTZ00013 PTZ00013
plasmepsin 4 (PM4); Provisional
92-312 8.61e-17

plasmepsin 4 (PM4); Provisional


Pssm-ID: 140051 [Multi-domain]  Cd Length: 450  Bit Score: 81.57  E-value: 8.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   92 YYLEMLIGTPPQKLQILVDTGSSNFAVAG----TPHSYIDTYFDTERSSTYRSKGFDVTVKYTQGSWTGFVGEDLVTIPk 167
Cdd:PTZ00013 139 FYGEGEVGDNHQKFMLIFDTGSANLWVPSkkcdSIGCSIKNLYDSSKSKSYEKDGTKVDITYGSGTVKGFFSKDLVTLG- 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  168 gfNTSFLVNIATIFESENF--FLPGIKWNGILGLAYATLAkpSSSLETFFDSLVTQANIPN-VFSMQmcgagLPVagSGT 244
Cdd:PTZ00013 218 --HLSMPYKFIEVTDTDDLepIYSSSEFDGILGLGWKDLS--IGSIDPIVVELKNQNKIDNaLFTFY-----LPV--HDV 286
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21040362  245 NGGSLVLGGIEPSLYKGDIWYTPIKEEWYYQIEiLKLEIGGQSLnldcreyNADKAIVDSGTTLLRLP 312
Cdd:PTZ00013 287 HAGYLTIGGIEEKFYEGNITYEKLNHDLYWQID-LDVHFGKQTM-------QKANVIVDSGTTTITAP 346
PTZ00165 PTZ00165
aspartyl protease; Provisional
92-324 3.77e-16

aspartyl protease; Provisional


Pssm-ID: 240300 [Multi-domain]  Cd Length: 482  Bit Score: 79.80  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGT--------PHsyidTYFDTERSSTYR--SKGFDVTVKYTQ---GSWTGFV 158
Cdd:PTZ00165 121 YFGEIQVGTPPKSFVVVFDTGSSNLWIPSKecksggcaPH----RKFDPKKSSTYTklKLGDESAETYIQygtGECVLAL 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  159 GEDLVTIpKGFNTSFLVNIATIFESENFF--LPgikWNGILGLAYA-TLAKPSSSLETFFDSLVTQANIP-NVFSMQMcg 234
Cdd:PTZ00165 197 GKDTVKI-GGLKVKHQSIGLAIEESLHPFadLP---FDGLVGLGFPdKDFKESKKALPIVDNIKKQNLLKrNIFSFYM-- 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  235 aglpvAGSGTNGGSLVLGGIEPS-LYKGD-IWYTPIKEEWYYQIEILKLEIGGQSLNLDCREYNadkAIVDSGTTLLRLP 312
Cdd:PTZ00165 271 -----SKDLNQPGSISFGSADPKyTLEGHkIWWFPVISTDYWEIEVVDILIDGKSLGFCDRKCK---AAIDTGSSLITGP 342
                        250
                 ....*....|..
gi 21040362  313 QKVFDAVVEAVA 324
Cdd:PTZ00165 343 SSVINPLLEKIP 354
SAP_like cd05474
SAPs, pepsin-like proteinases secreted from pathogens to degrade host proteins; SAPs (Secreted ...
92-323 1.64e-15

SAPs, pepsin-like proteinases secreted from pathogens to degrade host proteins; SAPs (Secreted aspartic proteinases) are secreted from a group of pathogenic fungi, predominantly Candida species. They are secreted from the pathogen to degrade host proteins. SAP is one of the most significant extracellular hydrolytic enzymes produced by C. albicans. SAP proteins, encoded by a family of 10 SAP genes. All 10 SAP genes of C. albicans encode preproenzymes, approximately 60 amino acid longer than the mature enzyme, which are processed when transported via the secretory pathway. The mature enzymes contain sequence motifs typical for all aspartyl proteinases, including the two conserved aspartate residues other active site and conserved cysteine residues implicated in the maintenance of the three-dimensional structure. Most Sap proteins contain putative N-glycosylation sites, but it remains to be determined which Sap proteins are glycosylated. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA). The overall structure of Sap protein conforms to the classical aspartic proteinase fold typified by pepsin. SAP is a bilobal enzyme, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. More recently evolved enzymes have similar three-dimensional structures, however their amino acid sequences are more divergent except for the conserved catalytic site motif. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133141 [Multi-domain]  Cd Length: 295  Bit Score: 76.45  E-value: 1.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  92 YYLEMLIGTPPQKLQILVDTGSSNFAVagtPHSYIdTYFDTersstyrskgfdvtvKYTQGSWtgfvGEDLVTIPKGFNT 171
Cdd:cd05474   3 YSAELSVGTPPQKVTVLLDTGSSDLWV---PDFSI-SYGDG---------------TSASGTW----GTDTVSIGGATVK 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 172 SF---LVNIATIFesenfflpgikwNGILGLAYATL---AKPSSSLETFFDSLVTQANIP-NVFSMQmcgagLPVAGSGT 244
Cdd:cd05474  60 NLqfaVANSTSSD------------VGVLGIGLPGNeatYGTGYTYPNFPIALKKQGLIKkNAYSLY-----LNDLDAST 122
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 245 ngGSLVLGGIEPSLYKGDIWYTPIKEEwYYQIEILKLEIGGQSLNLDCREYNADK------AIVDSGTTLLRLPQKVFDA 318
Cdd:cd05474 123 --GSILFGGVDTAKYSGDLVTLPIVND-NGGSEPSELSVTLSSISVNGSSGNTTLlsknlpALLDSGTTLTYLPSDIVDA 199

                ....*
gi 21040362 319 VVEAV 323
Cdd:cd05474 200 IAKQL 204
pepsin_A_like_plant cd05476
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ...
91-320 3.08e-12

Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from plants; This family contains pepsin like aspartic proteases from plants including Chloroplast Nucleoids DNA-binding Protease and Nucellin. Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in senescent leaves of tobacco and Nucellins are important regulators of nucellar cell's progressive degradation after ovule fertilization. Structurally, aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. The N- and C-terminal domains, although structurally related by a 2-fold axis, have only limited sequence homology except the vicinity of the active site. This suggests that the enzymes evolved by an ancient duplication event. The enzymes specifically cleave bonds in peptides which have at least six residues in length with hydrophobic residues in both the P1 and P1' positions. The active site is located at the groove formed by the two lobes, with an extended loop projecting over the cleft to form an 11-residue flap, which encloses substrates and inhibitors in the active site. Specificity is determined by nearest-neighbor hydrophobic residues surrounding the catalytic aspartates, and by three residues in the flap. The enzymes are mostly secreted from cells as inactive proenzymes that activate autocatalytically at acidic pH.


Pssm-ID: 133143 [Multi-domain]  Cd Length: 265  Bit Score: 66.13  E-value: 3.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  91 GYYLEMLIGTPPQKLQILVDTGSSnfavagtpHSYID--TYfdtersstyrskgfdvTVKYTQGSWT-GFVGEDLVTIPK 167
Cdd:cd05476   1 EYLVTLSIGTPPQPFSLIVDTGSD--------LTWTQccSY----------------EYSYGDGSSTsGVLATETFTFGD 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 168 GFNTsfLVNIA---TIFESENFFLPGIkwnGILGLAYATLakpsssletffdSLVTQANI-PNVFSMqmCgagLPVAGSG 243
Cdd:cd05476  57 SSVS--VPNVAfgcGTDNEGGSFGGAD---GILGLGRGPL------------SLVSQLGStGNKFSY--C---LVPHDDT 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 244 TNGGSLVLGGIePSLYKGDIWYTPI----KEEWYYQIEILKLEIGGQSLNLDCREYNADKA-----IVDSGTTLLRLPQK 314
Cdd:cd05476 115 GGSSPLILGDA-ADLGGSGVVYTPLvknpANPTYYYVNLEGISVGGKRLPIPPSVFAIDSDgsggtIIDSGTTLTYLPDP 193

                ....*.
gi 21040362 315 VFDAVV 320
Cdd:cd05476 194 AYPDLT 199
TAXi_N pfam14543
Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly ...
92-253 5.24e-12

Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly necessary for creating the catalytic pocket necessary for cleaving xylanase. Phytopathogens produce xylanase that destroys plant cells, so its destruction through proteolysis is vital for plant-survival.


Pssm-ID: 464203 [Multi-domain]  Cd Length: 172  Bit Score: 63.83  E-value: 5.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362    92 YYLEMLIGTPPQKLQILVDTGSSNFAVAGTPHSYI--DTYFDTERSSTYR----------------------SKGFDVTV 147
Cdd:pfam14543   1 YLVTISIGTPPVPFFLVVDTGSDLTWVQCDPCCYSqpDPLFDPYKSSTYKpvpcssplcslialsspgpccsNNTCDYEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   148 KYTQGSWT-GFVGEDLVTIPKGFNTSFLVNIA---TIFESENFFLPGikwNGILGLAYATLakpsssletffdSLVTQAN 223
Cdd:pfam14543  81 SYGDGSSTsGVLATDTLTLNSTGGSVSVPNFVfgcGYNLLGGLPAGA---DGILGLGRGKL------------SLPSQLA 145
                         170       180       190
                  ....*....|....*....|....*....|....
gi 21040362   224 ----IPNVFSmqMCgagLPvaGSGTNGGSLVLGG 253
Cdd:pfam14543 146 sqgiFGNKFS--YC---LS--SSSSGSGVLFFGD 172
PLN03146 PLN03146
aspartyl protease family protein; Provisional
88-326 7.94e-06

aspartyl protease family protein; Provisional


Pssm-ID: 178691 [Multi-domain]  Cd Length: 431  Bit Score: 47.70  E-value: 7.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362   88 SGRGYYL-EMLIGTPPQKLQILVDTGSSNFAVAGTP--HSY--IDTYFDTERSSTYRS--------------------KG 142
Cdd:PLN03146  80 SNGGEYLmNISIGTPPVPILAIADTGSDLIWTQCKPcdDCYkqVSPLFDPKKSSTYKDvscdssqcqalgnqascsdeNT 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  143 FDVTVKYTQGSWT-GFVGEDLVTIPK--GFNTSFLvNIA--------TIFESenfflpgiKWNGILGLAYATLAKPS--- 208
Cdd:PLN03146 160 CTYSYSYGDGSFTkGNLAVETLTIGStsGRPVSFP-GIVfgcghnngGTFDE--------KGSGIVGLGGGPLSLISqlg 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  209 SSLETFFD-SLVTQANIPNVFSMQMCGAGLPVAGSGTNGGSLVLGgiEPSLYkgdiwytpikeeWYYQIEIL-----KLE 282
Cdd:PLN03146 231 SSIGGKFSyCLVPLSSDSNGTSKINFGTNAIVSGSGVVSTPLVSK--DPDTF------------YYLTLEAIsvgskKLP 296
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 21040362  283 IGGQSLNlDCREYNadkAIVDSGTTLLRLPQKVFDAVVEAVARA 326
Cdd:PLN03146 297 YTGSSKN-GVEEGN---IIIDSGTTLTLLPSDFYSELESAVEEA 336
cnd41_like cd05472
Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1, ...
98-326 2.73e-05

Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase; Chloroplast Nucleoids DNA-binding Protease catalyzes the degradation of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in senescent leaves of tobacco. Antisense tobacco with reduced amount of CND41 maintained green leaves and constant protein levels, especially Rubisco. CND41 has DNA-binding as well as aspartic protease activities. The pepsin-like aspartic protease domain is located at the C-terminus of the protein. The enzyme is characterized by having two aspartic protease catalytic site motifs, the Asp-Thr-Gly-Ser in the N-terminal and Asp-Ser-Gly-Ser in the C-terminal region. Aspartic proteases are bilobal enzymes, each lobe contributing a catalytic Asp residue, with an extended active site cleft localized between the two lobes of the molecule. One lobe may be evolved from the other through ancient gene-duplication event. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133139 [Multi-domain]  Cd Length: 299  Bit Score: 45.73  E-value: 2.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362  98 IGTPPQKLQILVDTGSsnfavagtphsyidtyfdtersstyrskgfDVT-----------VKYTQGSWT-GFVGEDLVTi 165
Cdd:cd05472   8 LGTPARDQTVIVDTGS------------------------------DLTwvqcqpcclyqVSYGDGSYTtGDLATDTLT- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 166 pkgFNTSFLVNiatifeseNFFL--------PGIKWNGILGLAYATLAKPSSSLETFfdslvtqaniPNVFSMqmCgagL 237
Cdd:cd05472  57 ---LGSSDVVP--------GFAFgcghdnegLFGGAAGLLGLGRGKLSLPSQTASSY----------GGVFSY--C---L 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21040362 238 PvAGSGTNGGSLVLGGiePSLYKGDIWYTPI----KEEWYYQIEILKLEIGGQSLNLDCREYNADKAIVDSGTTLLRLPQ 313
Cdd:cd05472 111 P-DRSSSSSGYLSFGA--AASVPAGASFTPMlsnpRVPTFYYVGLTGISVGGRRLPIPPASFGAGGVIIDSGTVITRLPP 187
                       250
                ....*....|...
gi 21040362 314 KVFDAVVEAVARA 326
Cdd:cd05472 188 SAYAALRDAFRAA 200
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH