NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|332645705|gb|AEE79226|]
View 

Eukaryotic aspartyl protease family protein [Arabidopsis thaliana]

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 ...
88-424 8.35e-75

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 cd05472:

Pssm-ID: 472175 [Multi-domain]  Cd Length: 299  Bit Score: 235.63  E-value: 8.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCvgcsssvlfdpskssssrtlqceapqckqapnpsctvsksCGFNMTYG 167
Cdd:cd05472    2 YVVTVGLGTPARDQTVIVDTGSDLTWVQCQPC----------------------------------------CLYQVSYG 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 168 -GSTIEAYLTQDTLTLA-SDVIPNYTFGCINKASGTSLPAQGLMGLGRGPLSLISQSQNLYQSTFSYCLPnSKSSNFSGS 245
Cdd:cd05472   42 dGSYTTGDLATDTLTLGsSDVVPGFAFGCGHDNEGLFGGAAGLLGLGRGKLSLPSQTASSYGGVFSYCLP-DRSSSSSGY 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 246 LRLG-PKNQPIRIKTTPLLKNPRRSSLYYVNLVGIRVGNKIVDIPTSALAfdpatGAGTIFDSGTVYTRLVEPAYVAVRN 324
Cdd:cd05472  121 LSFGaAASVPAGASFTPMLSNPRVPTFYYVGLTGISVGGRRLPIPPASFG-----AGGVIIDSGTVITRLPPSAYAALRD 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 325 EFRRRVKN---ANATSLggFDTCYSGS----VVFPSVTFMFA-GMNVTLPPDNLLIHSSAGNLSCLAMAAApvNVNSVLN 396
Cdd:cd05472  196 AFRAAMAAyprAPGFSI--LDTCYDLSgfrsVSVPTVSLHFQgGADVELDASGVLYPVDDSSQVCLAFAGT--SDDGGLS 271
                        330       340
                 ....*....|....*....|....*...
gi 332645705 397 VIASMQQQNHRVLIDVPNSRLGISRETC 424
Cdd:cd05472  272 IIGNVQQQTFRVVYDVAGGRIGFAPGGC 299
 
Name Accession Description Interval E-value
cnd41_like cd05472
Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1, ...
88-424 8.35e-75

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: 235.63  E-value: 8.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCvgcsssvlfdpskssssrtlqceapqckqapnpsctvsksCGFNMTYG 167
Cdd:cd05472    2 YVVTVGLGTPARDQTVIVDTGSDLTWVQCQPC----------------------------------------CLYQVSYG 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 168 -GSTIEAYLTQDTLTLA-SDVIPNYTFGCINKASGTSLPAQGLMGLGRGPLSLISQSQNLYQSTFSYCLPnSKSSNFSGS 245
Cdd:cd05472   42 dGSYTTGDLATDTLTLGsSDVVPGFAFGCGHDNEGLFGGAAGLLGLGRGKLSLPSQTASSYGGVFSYCLP-DRSSSSSGY 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 246 LRLG-PKNQPIRIKTTPLLKNPRRSSLYYVNLVGIRVGNKIVDIPTSALAfdpatGAGTIFDSGTVYTRLVEPAYVAVRN 324
Cdd:cd05472  121 LSFGaAASVPAGASFTPMLSNPRVPTFYYVGLTGISVGGRRLPIPPASFG-----AGGVIIDSGTVITRLPPSAYAALRD 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 325 EFRRRVKN---ANATSLggFDTCYSGS----VVFPSVTFMFA-GMNVTLPPDNLLIHSSAGNLSCLAMAAApvNVNSVLN 396
Cdd:cd05472  196 AFRAAMAAyprAPGFSI--LDTCYDLSgfrsVSVPTVSLHFQgGADVELDASGVLYPVDDSSQVCLAFAGT--SDDGGLS 271
                        330       340
                 ....*....|....*....|....*...
gi 332645705 397 VIASMQQQNHRVLIDVPNSRLGISRETC 424
Cdd:cd05472  272 IIGNVQQQTFRVVYDVAGGRIGFAPGGC 299
PLN03146 PLN03146
aspartyl protease family protein; Provisional
75-388 1.20e-42

aspartyl protease family protein; Provisional


Pssm-ID: 178691 [Multi-domain]  Cd Length: 431  Bit Score: 155.17  E-value: 1.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  75 PIASGRAIVQSPT------YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCVGCSSSV--LFDPSKSSSSRTLQCEAPQC 146
Cdd:PLN03146  66 PTDASPNDPQSDLisnggeYLMNISIGTPPVPILAIADTGSDLIWTQCKPCDDCYKQVspLFDPKKSSTYKDVSCDSSQC 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 147 KQAPN-PSCTVSKSCGFNMTYG-GSTIEAYLTQDTLTLASD-----VIPNYTFGCINKASGT-SLPAQGLMGLGRGPLSL 218
Cdd:PLN03146 146 QALGNqASCSDENTCTYSYSYGdGSFTKGNLAVETLTIGSTsgrpvSFPGIVFGCGHNNGGTfDEKGSGIVGLGGGPLSL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 219 ISQSQNLYQSTFSYCL-PNSKSSNFSGSLRLGPKNQP--IRIKTTPLL-KNPrrSSLYYVNLVGIRVGNKivDIPTSALA 294
Cdd:PLN03146 226 ISQLGSSIGGKFSYCLvPLSSDSNGTSKINFGTNAIVsgSGVVSTPLVsKDP--DTFYYLTLEAISVGSK--KLPYTGSS 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 295 FDPATGAGTIFDSGTVYTRLVEPAYvavrNEFRRRVKNA-NATSL----GGFDTCYS--GSVVFPSVTFMFAGMNVTLPP 367
Cdd:PLN03146 302 KNGVEEGNIIIDSGTTLTLLPSDFY----SELESAVEEAiGGERVsdpqGLLSLCYSstSDIKLPIITAHFTGADVKLQP 377
                        330       340
                 ....*....|....*....|.
gi 332645705 368 DNLLIHSSAGnLSCLAMAAAP 388
Cdd:PLN03146 378 LNTFVKVSED-LVCFAMIPTS 397
TAXi_N pfam14543
Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly ...
88-249 1.61e-41

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: 144.72  E-value: 1.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705   88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCVGCSSSVLFDPSKSSSSRTLQCEAPQCKQAPNP---SCTVSKSCGFNM 164
Cdd:pfam14543   1 YLVTISIGTPPVPFFLVVDTGSDLTWVQCDPCCYSQPDPLFDPYKSSTYKPVPCSSPLCSLIALSspgPCCSNNTCDYEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  165 TYG-GSTIEAYLTQDTLTLAS----DVIPNYTFGCINKASGTSLP-AQGLMGLGRGPLSLISQ--SQNLYQSTFSYCLPN 236
Cdd:pfam14543  81 SYGdGSSTSGVLATDTLTLNStggsVSVPNFVFGCGYNLLGGLPAgADGILGLGRGKLSLPSQlaSQGIFGNKFSYCLSS 160
                         170
                  ....*....|...
gi 332645705  237 skSSNFSGSLRLG 249
Cdd:pfam14543 161 --SSSGSGVLFFG 171
 
Name Accession Description Interval E-value
cnd41_like cd05472
Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1, ...
88-424 8.35e-75

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: 235.63  E-value: 8.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCvgcsssvlfdpskssssrtlqceapqckqapnpsctvsksCGFNMTYG 167
Cdd:cd05472    2 YVVTVGLGTPARDQTVIVDTGSDLTWVQCQPC----------------------------------------CLYQVSYG 41
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 168 -GSTIEAYLTQDTLTLA-SDVIPNYTFGCINKASGTSLPAQGLMGLGRGPLSLISQSQNLYQSTFSYCLPnSKSSNFSGS 245
Cdd:cd05472   42 dGSYTTGDLATDTLTLGsSDVVPGFAFGCGHDNEGLFGGAAGLLGLGRGKLSLPSQTASSYGGVFSYCLP-DRSSSSSGY 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 246 LRLG-PKNQPIRIKTTPLLKNPRRSSLYYVNLVGIRVGNKIVDIPTSALAfdpatGAGTIFDSGTVYTRLVEPAYVAVRN 324
Cdd:cd05472  121 LSFGaAASVPAGASFTPMLSNPRVPTFYYVGLTGISVGGRRLPIPPASFG-----AGGVIIDSGTVITRLPPSAYAALRD 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 325 EFRRRVKN---ANATSLggFDTCYSGS----VVFPSVTFMFA-GMNVTLPPDNLLIHSSAGNLSCLAMAAApvNVNSVLN 396
Cdd:cd05472  196 AFRAAMAAyprAPGFSI--LDTCYDLSgfrsVSVPTVSLHFQgGADVELDASGVLYPVDDSSQVCLAFAGT--SDDGGLS 271
                        330       340
                 ....*....|....*....|....*...
gi 332645705 397 VIASMQQQNHRVLIDVPNSRLGISRETC 424
Cdd:cd05472  272 IIGNVQQQTFRVVYDVAGGRIGFAPGGC 299
pepsin_A_like_plant cd05476
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ...
87-424 5.62e-66

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: 211.74  E-value: 5.62e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  87 TYIVRANIGTPAQPMLVALDTSNDAAWIPCsgcvgcsssvlfdpskssssrtlqceapqckqapnpsctvsksCGFNMTY 166
Cdd:cd05476    1 EYLVTLSIGTPPQPFSLIVDTGSDLTWTQC-------------------------------------------CSYEYSY 37
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 167 G-GSTIEAYLTQDTLTLASD--VIPNYTFGCINKASGTSLPAQ-GLMGLGRGPLSLISQSQNLYQStFSYCLPNSKSSNF 242
Cdd:cd05476   38 GdGSSTSGVLATETFTFGDSsvSVPNVAFGCGTDNEGGSFGGAdGILGLGRGPLSLVSQLGSTGNK-FSYCLVPHDDTGG 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 243 SGSLRLG--PKNQPIRIKTTPLLKNPRRSSLYYVNLVGIRVGNKIVDIPTSALAFDPATGAGTIFDSGTVYTRLVEPAYv 320
Cdd:cd05476  117 SSPLILGdaADLGGSGVVYTPLVKNPANPTYYYVNLEGISVGGKRLPIPPSVFAIDSDGSGGTIIDSGTTLTYLPDPAY- 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 321 avrnefrrrvknanatslggfdtcysgsvvfPSVTFMFAGMN-VTLPPDNLLIhSSAGNLSCLAMAAAPVNvnsVLNVIA 399
Cdd:cd05476  196 -------------------------------PDLTLHFDGGAdLELPPENYFV-DVGEGVVCLAILSSSSG---GVSILG 240
                        330       340
                 ....*....|....*....|....*
gi 332645705 400 SMQQQNHRVLIDVPNSRLGISRETC 424
Cdd:cd05476  241 NIQQQNFLVEYDLENSRLGFAPADC 265
pepsin_like cd05471
Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH; ...
88-359 2.72e-45

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: 158.36  E-value: 2.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCVGCSSsvlfdpskssssrtlQCEAPQCKQAPNPSCTVSKSCGFNMTYG 167
Cdd:cd05471    1 YYGEITIGTPPQKFSVIFDTGSSLLWVPSSNCTSCSC---------------QKHPRFKYDSSKSSTYKDTGCTFSITYG 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 168 GSTIEAYLTQDTLTLASDVIPNYTFGCINKASG--TSLPAQGLMGLGRGPLSLISQS---QNLYQST------FSYCLPN 236
Cdd:cd05471   66 DGSVTGGLGTDTVTIGGLTIPNQTFGCATSESGdfSSSGFDGILGLGFPSLSVDGVPsffDQLKSQGlisspvFSFYLGR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 237 SKSSNFSGSLRLG---PKNQPIRIKTTPLLKNPrrSSLYYVNLVGIRVGNKIVdiptsalaFDPATGAGTIFDSGTVYTR 313
Cdd:cd05471  146 DGDGGNGGELTFGgidPSKYTGDLTYTPVVSNG--PGYWQVPLDGISVGGKSV--------ISSSGGGGAIVDSGTSLIY 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 332645705 314 LVEPAYVAVRNEFRRRVKNanatSLGGFDTCYSGSVVFPSVTFMFA 359
Cdd:cd05471  216 LPSSVYDAILKALGAAVSS----SDGGYGVDCSPCDTLPDITFTFL 257
PLN03146 PLN03146
aspartyl protease family protein; Provisional
75-388 1.20e-42

aspartyl protease family protein; Provisional


Pssm-ID: 178691 [Multi-domain]  Cd Length: 431  Bit Score: 155.17  E-value: 1.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  75 PIASGRAIVQSPT------YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCVGCSSSV--LFDPSKSSSSRTLQCEAPQC 146
Cdd:PLN03146  66 PTDASPNDPQSDLisnggeYLMNISIGTPPVPILAIADTGSDLIWTQCKPCDDCYKQVspLFDPKKSSTYKDVSCDSSQC 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 147 KQAPN-PSCTVSKSCGFNMTYG-GSTIEAYLTQDTLTLASD-----VIPNYTFGCINKASGT-SLPAQGLMGLGRGPLSL 218
Cdd:PLN03146 146 QALGNqASCSDENTCTYSYSYGdGSFTKGNLAVETLTIGSTsgrpvSFPGIVFGCGHNNGGTfDEKGSGIVGLGGGPLSL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 219 ISQSQNLYQSTFSYCL-PNSKSSNFSGSLRLGPKNQP--IRIKTTPLL-KNPrrSSLYYVNLVGIRVGNKivDIPTSALA 294
Cdd:PLN03146 226 ISQLGSSIGGKFSYCLvPLSSDSNGTSKINFGTNAIVsgSGVVSTPLVsKDP--DTFYYLTLEAISVGSK--KLPYTGSS 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 295 FDPATGAGTIFDSGTVYTRLVEPAYvavrNEFRRRVKNA-NATSL----GGFDTCYS--GSVVFPSVTFMFAGMNVTLPP 367
Cdd:PLN03146 302 KNGVEEGNIIIDSGTTLTLLPSDFY----SELESAVEEAiGGERVsdpqGLLSLCYSstSDIKLPIITAHFTGADVKLQP 377
                        330       340
                 ....*....|....*....|.
gi 332645705 368 DNLLIHSSAGnLSCLAMAAAP 388
Cdd:PLN03146 378 LNTFVKVSED-LVCFAMIPTS 397
TAXi_N pfam14543
Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly ...
88-249 1.61e-41

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: 144.72  E-value: 1.61e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705   88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCVGCSSSVLFDPSKSSSSRTLQCEAPQCKQAPNP---SCTVSKSCGFNM 164
Cdd:pfam14543   1 YLVTISIGTPPVPFFLVVDTGSDLTWVQCDPCCYSQPDPLFDPYKSSTYKPVPCSSPLCSLIALSspgPCCSNNTCDYEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  165 TYG-GSTIEAYLTQDTLTLAS----DVIPNYTFGCINKASGTSLP-AQGLMGLGRGPLSLISQ--SQNLYQSTFSYCLPN 236
Cdd:pfam14543  81 SYGdGSSTSGVLATDTLTLNStggsVSVPNFVFGCGYNLLGGLPAgADGILGLGRGKLSLPSQlaSQGIFGNKFSYCLSS 160
                         170
                  ....*....|...
gi 332645705  237 skSSNFSGSLRLG 249
Cdd:pfam14543 161 --SSSGSGVLFFG 171
TAXi_C pfam14541
Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly ...
272-420 2.33e-32

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


Pssm-ID: 434029  Cd Length: 160  Bit Score: 120.07  E-value: 2.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  272 YYVNLVGIRVGNKIVDIPTSALAFDPATGAGTIFDSGTVYTRLVEPAYVAVRNEFRR---RVKNANATSLGGFDTCYSGS 348
Cdd:pfam14541   2 YYIPLKGISVNGKRLPLPPGLLDIDRTGSGGTILDTGTPYTVLRPSVYRAVVQAFDKalaALGPRVVAPVAPFDLCYNST 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  349 VV--------FPSVTFMFA-GMNVTLPPDNLLIHSSaGNLSCLAMAAAPVNVNSvLNVIASMQQQNHRVLIDVPNSRLGI 419
Cdd:pfam14541  82 GLgstrlgpaVPPITLVFEgGADWTIFGANSMVQVD-GGVACLGFVDGGVPPAS-ASVIGGHQQEDNLLEFDLEKSRLGF 159

                  .
gi 332645705  420 S 420
Cdd:pfam14541 160 S 160
xylanase_inhibitor_I_like cd05489
TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a ...
129-421 1.48e-30

TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a member of potent TAXI-type inhibitors of fungal and bacterial family 11 xylanases. Plants developed a diverse battery of defense mechanisms in response to continual challenges by a broad spectrum of pathogenic microorganisms. Their defense arsenal includes inhibitors of cell wall-degrading enzymes, which hinder a possible invasion and colonization by antagonists. Xylanases of fungal and bacterial pathogens are the key enzymes in the degradation of xylan in the cell wall. Plants secrete proteins that inhibit these degradation glycosidases, including xylanase. Surprisingly, TAXI-I displays structural homology with the pepsin-like family of aspartic proteases but is proteolytically nonfunctional, because one or more residues of the essential catalytic triad are absent. The structure of the TAXI-inhibitor, Aspergillus niger xylanase I complex, illustrates the ability of tight binding and inhibition with subnanomolar affinity and indicates the importance of the C-terminal end for the differences in xylanase specificity among different TAXI-type inhibitors. This family also contains pepsin-like aspartic proteinases homologous to TAXI-I. Unlike TAXI-I, they have active site aspartates and are functionally active. This family of aspartate proteases is classified by MEROPS as the peptidase family A1 (pepsin A, clan AA).


Pssm-ID: 133156 [Multi-domain]  Cd Length: 362  Bit Score: 120.53  E-value: 1.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 129 DPSKSSSSRTLQCEAPQCKQAPNPSCTVS-----------KSCG---FNmTYGGSTIEAYLTQDTLTLAS--------DV 186
Cdd:cd05489   26 DAGHSSTYQTVPCSSSVCSLANRYHCPGTcggapgpgcgnNTCTahpYN-PVTGECATGDLTQDVLSANTtdgsnpllVV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 187 IPNYTFGCINKASGTSLP--AQGLMGLGRGPLSLISQ--SQNLYQSTFSYCLPNSKSSN----FSGS---LRLGPKNQPI 255
Cdd:cd05489  105 IFNFVFSCAPSLLLKGLPpgAQGVAGLGRSPLSLPAQlaSAFGVARKFALCLPSSPGGPgvaiFGGGpyyLFPPPIDLSK 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 256 RIKTTPLLKNPRRSSLYYVNLVGIRVGNKIVDIPTSALAFDPATGAGTIFDSGTVYTRLVEPAYVAVRNEFRRRVK--NA 333
Cdd:cd05489  185 SLSYTPLLTNPRKSGEYYIGVTSIAVNGHAVPLNPTLSANDRLGPGGVKLSTVVPYTVLRSDIYRAFTQAFAKATAriPR 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 334 NATSLGGFDTCYSGSVVF--------PSVTFMFAGMNV--TLPPDNLLIHSSaGNLSCLA---MAAAPvnVNSVlnVIAS 400
Cdd:cd05489  265 VPAAAVFPELCYPASALGntrlgyavPAIDLVLDGGGVnwTIFGANSMVQVK-GGVACLAfvdGGSEP--RPAV--VIGG 339
                        330       340
                 ....*....|....*....|.
gi 332645705 401 MQQQNHRVLIDVPNSRLGISR 421
Cdd:cd05489  340 HQMEDNLLVFDLEKSRLGFSS 360
Asp pfam00026
Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and ...
88-382 1.39e-20

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: 91.57  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705   88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGC---VGCSSSVLFDPSKSSSSRTLqceapqckqapnpsctvskSCGFNM 164
Cdd:pfam00026   2 YFGTISIGTPPQKFTVIFDTGSSDLWVPSSYCtksSACKSHGTFDPSSSSTYKLN-------------------GTTFSI 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  165 TYGGSTIEAYLTQDTLTLASDVIPNYTFGCINKASGTSL---PAQGLMGLGRGPLS----------LISQ---SQNLY-- 226
Cdd:pfam00026  63 SYGDGSASGFLGQDTVTVGGLTITNQEFGLATKEPGSFFeyaKFDGILGLGFPSISavgatpvfdnLKSQgliDSPAFsv 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  227 ------QSTFSYCLPNSKSSNFSGSlrlgpknqpirIKTTPLLknprrSSLYY-VNLVGIRVGNKivdiptsalAFDPAT 299
Cdd:pfam00026 143 ylnspdAAGGEIIFGGVDPSKYTGS-----------LTYVPVT-----SQGYWqITLDSVTVGGS---------TSACSS 197
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  300 GAGTIFDSGTVYTRLVEPAYVAVRNEFrrrvkNANATSLGGFDTCYSGSVVFPSVTFMFAGMNVTLPPDNLLIHSSAGNL 379
Cdd:pfam00026 198 GCQAILDTGTSLLYGPTSIVSKIAKAV-----GASSSEYGEYVVDCDSISTLPDITFVIGGAKITVPPSAYVLQNSQGGS 272

                  ...
gi 332645705  380 SCL 382
Cdd:pfam00026 273 TCL 275
nucellin_like cd05475
Nucellins, plant aspartic proteases specifically expressed in nucellar cells during ...
88-424 3.01e-20

Nucellins, plant aspartic proteases specifically expressed in nucellar cells during degradation; Nucellins are important regulators of nucellar cell's progressive degradation after ovule fertilization. This degradation is a characteristic of programmed cell death. Nucellins are plant aspartic proteases specifically expressed in nucellar cells during degradation. 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, and two other regions nearly identical to two regions of plant aspartic proteases. 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. 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.


Pssm-ID: 133142 [Multi-domain]  Cd Length: 273  Bit Score: 89.74  E-value: 3.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWipcsgcvgcsssvlfdpskssssrtLQCEAPqckqapnpsCTvSKSCGFNMTY- 166
Cdd:cd05475    3 YYVTINIGNPPKPYFLDIDTGSDLTW-------------------------LQCDAP---------CT-GCQCDYEIEYa 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 167 -GGSTIEAyLTQDTLTL----ASDVIPNYTFGCINKASGTSL----PAQGLMGLGRGPLSLISQ--SQNLYQSTFSYCLp 235
Cdd:cd05475   48 dGGSSMGV-LVTDIFSLkltnGSRAKPRIAFGCGYDQQGPLLnpppPTDGILGLGRGKISLPSQlaSQGIIKNVIGHCL- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 236 nskSSNFSGSLRLGPKNQP-IRIKTTPLLKNPRRSSlYYVNLVGIRVGNKIVDIPtsalafdpatGAGTIFDSGTVYTRL 314
Cdd:cd05475  126 ---SSNGGGFLFFGDDLVPsSGVTWTPMRRESQKKH-YSPGPASLLFNGQPTGGK----------GLEVVFDSGSSYTYF 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 315 VEPAYvavrnefrrrvknanatslggfdtcysgsvvFPSVTFMFAG----MNVTLPPDNLLIHSSAGNLsCLAMAAAPVN 390
Cdd:cd05475  192 NAQAY-------------------------------FKPLTLKFGKgwrtRLLEIPPENYLIISEKGNV-CLGILNGSEI 239
                        330       340       350
                 ....*....|....*....|....*....|....
gi 332645705 391 VNSVLNVIASMQQQNHRVLIDVPNSRLGISRETC 424
Cdd:cd05475  240 GLGNTNIIGDISMQGLMVIYDNEKQQIGWVRSDC 273
Plasmepsin_5 cd06096
Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite; The ...
88-326 2.51e-13

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: 70.49  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCVGCSSSVL--FDPSKSSSSRTLQCEAPQCkqaPNPSCTVSKSCGFNMT 165
Cdd:cd06096    4 YFIDIFIGNPPQKQSLILDTGSSSLSFPCSQCKNCGIHMEppYNLNNSITSSILYCDCNKC---CYCLSCLNNKCEYSIS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 166 YG-GSTIEAYLTQDTLTLASDVIPNY-------TFGCINKASGTSL--PAQGLMGLGR-GPLSLISQSQNLYQST----- 229
Cdd:cd06096   81 YSeGSSISGFYFSDFVSFESYLNSNSekesfkkIFGCHTHETNLFLtqQATGILGLSLtKNNGLPTPIILLFTKRpklkk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 230 ---FSYCLpnsksSNFSGSLRLGPKNQPIRIKTTPLLKNPR---------RSSLYYVNLVGIRVGNkivdipTSALAFDp 297
Cdd:cd06096  161 dkiFSICL-----SEDGGELTIGGYDKDYTVRNSSIGNNKVskivwtpitRKYYYYVKLEGLSVYG------TTSNSGN- 228
                        250       260
                 ....*....|....*....|....*....
gi 332645705 298 ATGAGTIFDSGTVYTRLVEPAYVAVRNEF 326
Cdd:cd06096  229 TKGLGMLVDSGSTLSHFPEDLYNKINNFF 257
pepsin_retropepsin_like cd05470
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
90-211 5.25e-13

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: 65.09  E-value: 5.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  90 VRANIGTPAQPMLVALDTSNDAAWIPCSGC---VGCSSSVLFDPSKSSSSRTLQCEapqckqapnpsctvskscgFNMTY 166
Cdd:cd05470    1 IEIGIGTPPQTFNVLLDTGSSNLWVPSVDCqslAIYSHSSYDDPSASSTYSDNGCT-------------------FSITY 61
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 332645705 167 GGSTIEAYLTQDTLTLASDVIPNYTFGCINKASGT---SLPAQGLMGL 211
Cdd:cd05470   62 GTGSLSGGLSTDTVSIGDIEVVGQAFGCATDEPGAtflPALFDGILGL 109
Proteinase_A_fungi cd05488
Fungal Proteinase A , aspartic proteinase superfamily; Fungal Proteinase A, a proteolytic ...
88-383 2.15e-11

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: 64.77  E-value: 2.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGC--VGCSSSVLFDPSKSSSSRtlqceapqckqapnpsctvSKSCGFNMT 165
Cdd:cd05488   11 YFTDITLGTPPQKFKVILDTGSSNLWVPSVKCgsIACFLHSKYDSSASSTYK-------------------ANGTEFKIQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 166 YGGSTIEAYLTQDTLTLASDVIPNYTFgcinkASGTSLPA--------QGLMGLGRGPLS----------LISQSQnLYQ 227
Cdd:cd05488   72 YGSGSLEGFVSQDTLSIGDLTIKKQDF-----AEATSEPGlafafgkfDGILGLAYDTISvnkivppfynMINQGL-LDE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 228 STFSYCLPNSKS------------SNFSGslrlgpknqpiRIKTTPLlknpRRSSLYYVNLVGIRVGNKIVDIptsalaf 295
Cdd:cd05488  146 PVFSFYLGSSEEdggeatfggideSRFTG-----------KITWLPV----RRKAYWEVELEKIGLGDEELEL------- 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 296 dpaTGAGTIFDSGTvyTRLVEPAYVAvrnEFRRRVKNANATSLGGFDTCYSGSVVFPSVTFMFAGMNVTLPPDNLLIHSS 375
Cdd:cd05488  204 ---ENTGAAIDTGT--SLIALPSDLA---EMLNAEIGAKKSWNGQYTVDCSKVDSLPDLTFNFDGYNFTLGPFDYTLEVS 275

                 ....*...
gi 332645705 376 AgnlSCLA 383
Cdd:cd05488  276 G---SCIS 280
SAP_like cd05474
SAPs, pepsin-like proteinases secreted from pathogens to degrade host proteins; SAPs (Secreted ...
88-378 2.86e-11

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: 63.74  E-value: 2.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDT-SNDAaWIPcsgcvgcsssvlfdpskssssrtlqceapqckqapnpsctvskscGFNMTY 166
Cdd:cd05474    3 YSAELSVGTPPQKVTVLLDTgSSDL-WVP---------------------------------------------DFSISY 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 167 G-GSTIEAYLTQDTLTLASDVIPNYTFGCINKASGTslpaQGLMGLGRG---------------PLSLISQ---SQNLYq 227
Cdd:cd05474   37 GdGTSASGTWGTDTVSIGGATVKNLQFAVANSTSSD----VGVLGIGLPgneatygtgytypnfPIALKKQgliKKNAY- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 228 stfSYCLPNSKSSN------------FSGSLrlgpknqpiriKTTPLLKNPRRSSLYY--VNLVGIRVGNKIVDIPTSAL 293
Cdd:cd05474  112 ---SLYLNDLDASTgsilfggvdtakYSGDL-----------VTLPIVNDNGGSEPSElsVTLSSISVNGSSGNTTLLSK 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 294 AFDpatgagTIFDSGTVYTRLVEPAYVAVRNEFrrrvkNANATSLGG--FDTCYSGSVvfPSVTFMFAGMNVTLPPDNLL 371
Cdd:cd05474  178 NLP------ALLDSGTTLTYLPSDIVDAIAKQL-----GATYDSDEGlyVVDCDAKDD--GSLTFNFGGATISVPLSDLV 244

                 ....*..
gi 332645705 372 IHSSAGN 378
Cdd:cd05474  245 LPASTDD 251
gastricsin cd05477
Gastricsins, asparate proteases produced in gastric mucosa; Gastricsin is also called ...
87-375 1.05e-08

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: 56.43  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  87 TYIVRANIGTPAQPMLVALDTSNDAAWIPCSGC--VGCSSSVLFDPSKSSSSRTLQCEapqckqapnpsctvskscgFNM 164
Cdd:cd05477    3 SYYGEISIGTPPQNFLVLFDTGSSNLWVPSVLCqsQACTNHTKFNPSQSSTYSTNGET-------------------FSL 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 165 TYGGSTIEAYLTQDTLTLASDVIPNYTFGCINKASGTSL---PAQGLMGLGRGPLSLISQ--------SQNLYQS-TFSY 232
Cdd:cd05477   64 QYGSGSLTGIFGYDTVTVQGIIITNQEFGLSETEPGTNFvyaQFDGILGLAYPSISAGGAttvmqgmmQQNLLQApIFSF 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 233 CLPNSKSSNfSGSLRLGPKNQpiRIKTTPLLKNPRRSSLYY-VNLVGIRVGNK-----------IVDIPTSALafdpaTG 300
Cdd:cd05477  144 YLSGQQGQQ-GGELVFGGVDN--NLYTGQIYWTPVTSETYWqIGIQGFQINGQatgwcsqgcqaIVDTGTSLL-----TA 215
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 332645705 301 AGTIFDSGTVYTrlvepayvavrnefrrrvkNANATSLGGFDTCYSGSVVFPSVTFMFAGMNVTLPPDNLLIHSS 375
Cdd:cd05477  216 PQQVMSTLMQSI-------------------GAQQDQYGQYVVNCNNIQNLPTLTFTINGVSFPLPPSAYILQNN 271
Aspergillopepsin_like cd06097
Aspergillopepsin_like, aspartic proteases of fungal origin; The members of this family are ...
88-421 3.11e-08

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: 54.61  E-value: 3.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCVGCSSS--VLFDPSKSSSSRtlqceapqckqaPNPSCTVSkscgfnMT 165
Cdd:cd06097    1 YLTPVKIGTPPQTLNLDLDTGSSDLWVFSSETPAAQQGghKLYDPSKSSTAK------------LLPGATWS------IS 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 166 YG-GSTIEAYLTQDTLTLASDVIPNYTFGCINKASGTS---LPAQGLMGLGrgpLSLISQSQNLYQSTFsycLPNSKSSN 241
Cdd:cd06097   63 YGdGSSASGIVYTDTVSIGGVEVPNQAIELATAVSASFfsdTASDGLLGLA---FSSINTVQPPKQKTF---FENALSSL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 242 ----FSGSLRlgpKNQPIR--------------IKTTPllknPRRSSLYY-VNLVGIRVGNkivDIPTSALAFDPatgag 302
Cdd:cd06097  137 daplFTADLR---KAAPGFytfgyideskykgeISWTP----VDNSSGFWqFTSTSYTVGG---DAPWSRSGFSA----- 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 303 tIFDSGTVYTRLVEPayvaVRNEFRRRVKNANATSLggfdtcySGSVVFPSvtfmfagmNVTLPPdnLLIHssagnlscl 382
Cdd:cd06097  202 -IADTGTTLILLPDA----IVEAYYSQVPGAYYDSE-------YGGWVFPC--------DTTLPD--LSFA--------- 250
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 332645705 383 amaaapvnvnsVLNVIASMQQQNHRVLIDVPNSRLGISR 421
Cdd:cd06097  251 -----------VFSILGDVFLKAQYVVFDVGGPKLGFAP 278
Cathepsin_D2 cd05490
Cathepsin_D2, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase of ...
94-291 4.45e-08

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: 54.41  E-value: 4.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  94 IGTPAQPMLVALDTSNDAAWIPCSGC----VGCSSSVLFDPSKSSSsrtlqceapqckqapnpscTVSKSCGFNMTYGGS 169
Cdd:cd05490   13 IGTPPQTFTVVFDTGSSNLWVPSVHCslldIACWLHHKYNSSKSST-------------------YVKNGTEFAIQYGSG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 170 TIEAYLTQDTLTLASDVIPNYTFGCINKASGTSLPA---QGLMGLGRGPLSL---------ISQSQNLYQSTFSYCLPNS 237
Cdd:cd05490   74 SLSGYLSQDTVSIGGLQVEGQLFGEAVKQPGITFIAakfDGILGMAYPRISVdgvtpvfdnIMAQKLVEQNVFSFYLNRD 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332645705 238 KSSNFSGSLRLGPKNqPIRIKTTPLLKNPRRSSLYYVNLVGIRVGNK----------IVDIPTS 291
Cdd:cd05490  154 PDAQPGGELMLGGTD-PKYYTGDLHYVNVTRKAYWQIHMDQVDVGSGltlckggceaIVDTGTS 216
pepsin_A cd05478
Pepsin A, aspartic protease produced in gastric mucosa of mammals; Pepsin, a well-known ...
94-212 1.72e-07

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: 52.45  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  94 IGTPAQPMLVALDTSNDAAWIPCSGC--VGCSSSVLFDPSKSSSSRtlqceapqckqapNPSCTVSkscgfnMTYGGSTI 171
Cdd:cd05478   17 IGTPPQDFTVIFDTGSSNLWVPSVYCssQACSNHNRFNPRQSSTYQ-------------STGQPLS------IQYGTGSM 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 332645705 172 EAYLTQDTLTLASDVIPNYTFGCINKASGTSL---PAQGLMGLG 212
Cdd:cd05478   78 TGILGYDTVQVGGISDTNQIFGLSETEPGSFFyyaPFDGILGLA 121
renin_like cd05487
Renin stimulates production of angiotensin and thus affects blood pressure; Renin, also known ...
93-285 2.15e-07

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: 52.47  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  93 NIGTPAQPMLVALDTSNDAAWIPCSGC----VGCSSSVLFDPSKSSSSRtlqceapqckqaPNPSctvskscGFNMTYGG 168
Cdd:cd05487   14 GIGTPPQTFKVVFDTGSSNLWVPSSKCsplyTACVTHNLYDASDSSTYK------------ENGT-------EFTIHYAS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 169 STIEAYLTQDTLTLASdvIP-NYTFGCInkasgTSLPA--------QGLMGLGRGPLSL---------ISQSQNLYQSTF 230
Cdd:cd05487   75 GTVKGFLSQDIVTVGG--IPvTQMFGEV-----TALPAipfmlakfDGVLGMGYPKQAIggvtpvfdnIMSQGVLKEDVF 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 332645705 231 SYCLPNSKSSNFSGSLRLGPKNqPIRIKTTPLLKNPRRSSLYYVNLVGIRVGNKI 285
Cdd:cd05487  148 SVYYSRDSSHSLGGEIVLGGSD-PQHYQGDFHYINTSKTGFWQIQMKGVSVGSST 201
PTZ00013 PTZ00013
plasmepsin 4 (PM4); Provisional
94-235 2.67e-07

plasmepsin 4 (PM4); Provisional


Pssm-ID: 140051 [Multi-domain]  Cd Length: 450  Bit Score: 52.68  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  94 IGTPAQPMLVALDTSNDAAWIPCSGC--VGCSSSVLFDPSKSSSSRtlqceapqckqapnpsctvSKSCGFNMTYGGSTI 171
Cdd:PTZ00013 145 VGDNHQKFMLIFDTGSANLWVPSKKCdsIGCSIKNLYDSSKSKSYE-------------------KDGTKVDITYGSGTV 205
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332645705 172 EAYLTQDTLTLASDVIPnYTFGCINKASG-----TSLPAQGLMGLGRGPLSLIS--------QSQN-LYQSTFSYCLP 235
Cdd:PTZ00013 206 KGFFSKDLVTLGHLSMP-YKFIEVTDTDDlepiySSSEFDGILGLGWKDLSIGSidpivvelKNQNkIDNALFTFYLP 282
PTZ00165 PTZ00165
aspartyl protease; Provisional
88-284 2.00e-06

aspartyl protease; Provisional


Pssm-ID: 240300 [Multi-domain]  Cd Length: 482  Bit Score: 49.76  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDTSNDAAWIPCSGCV--GCSSSVLFDPSKSSSSRTLqceapqcKQAPNPSCTVskscgfnMT 165
Cdd:PTZ00165 121 YFGEIQVGTPPKSFVVVFDTGSSNLWIPSKECKsgGCAPHRKFDPKKSSTYTKL-------KLGDESAETY-------IQ 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 166 YG-GSTIEAYlTQDTLTLASDVIPNYTFGCINKASG---TSLPAQGLMGLG---------RGPLSLIS--QSQN-LYQST 229
Cdd:PTZ00165 187 YGtGECVLAL-GKDTVKIGGLKVKHQSIGLAIEESLhpfADLPFDGLVGLGfpdkdfkesKKALPIVDniKKQNlLKRNI 265
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332645705 230 FSYCLPNSKSSnfSGSLRLGPKNQPI-----RIKTTPLLknprrsSLYY--VNLVGIRVGNK 284
Cdd:PTZ00165 266 FSFYMSKDLNQ--PGSISFGSADPKYtleghKIWWFPVI------STDYweIEVVDILIDGK 319
phytepsin cd06098
Phytepsin, a plant homolog of mammalian lysosomal pepsins; Phytepsin, a plant homolog of ...
94-212 8.62e-06

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: 47.37  E-value: 8.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  94 IGTPAQPMLVALDTSNDAAWIPCSGCVGCSSSVLFDPSKSSSSRTLQCEAPQCKqapnpsctvskscgfnMTYGGSTIEA 173
Cdd:cd06098   17 IGTPPQKFTVIFDTGSSNLWVPSSKCYFSIACYFHSKYKSSKSSTYKKNGTSAS----------------IQYGTGSISG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 332645705 174 YLTQDTLTLASDVIPNYTFGCINKASG-TSLPAQ--GLMGLG 212
Cdd:cd06098   81 FFSQDSVTVGDLVVKNQVFIEATKEPGlTFLLAKfdGILGLG 122
beta_secretase_like cd05473
Beta-secretase, aspartic-acid protease important in the pathogenesis of Alzheimer's disease; ...
88-424 1.23e-05

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: 47.03  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  88 YIVRANIGTPAQPMLVALDT--SNDAawipcsgcVGCSS----SVLFDPSKSSSSRtlqceapqckqapnpsctvSKSCG 161
Cdd:cd05473    4 YYIEMLIGTPPQKLNILVDTgsSNFA--------VAAAPhpfiHTYFHRELSSTYR-------------------DLGKG 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 162 FNMTYGGSTIEAYLTQDTLTLASDviPNYTFgCINKASGTS-----LPA---QGLMGLGRGPL------------SLISQ 221
Cdd:cd05473   57 VTVPYTQGSWEGELGTDLVSIPKG--PNVTF-RANIAAITEsenffLNGsnwEGILGLAYAELarpdssvepffdSLVKQ 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 222 SQnlYQSTFS-------YCLPNSKSSNFSGSLRLGPKNQpiRIKTTPLLKNPRRSSLYY-VNLVGIRVGNKIVDIPTSAL 293
Cdd:cd05473  134 TG--IPDVFSlqmcgagLPVNGSASGTVGGSMVIGGIDP--SLYKGDIWYTPIREEWYYeVIILKLEVGGQSLNLDCKEY 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 294 AFDPAtgagtIFDSGTVYTRLVEPAYVAVRNEFRRRVKNANATSlgGFDT-----CYSGSV----VFPSVTFMFAGMN-- 362
Cdd:cd05473  210 NYDKA-----IVDSGTTNLRLPVKVFNAAVDAIKAASLIEDFPD--GFWLgsqlaCWQKGTtpweIFPKISIYLRDENss 282
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332645705 363 ----VTLPPDNLL--IHSSAGNLSCLAMAAAPvNVNSVlnVIASMQQQNHRVLIDVPNSRLGISRETC 424
Cdd:cd05473  283 qsfrITILPQLYLrpVEDHGTQLDCYKFAISQ-STNGT--VIGAVIMEGFYVVFDRANKRVGFAVSTC 347
PTZ00147 PTZ00147
plasmepsin-1; Provisional
83-324 3.17e-05

plasmepsin-1; Provisional


Pssm-ID: 140176 [Multi-domain]  Cd Length: 453  Bit Score: 46.01  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  83 VQSPTYIVRANIGTPAQPMLVALDTSNDAAWIPCSGC--VGCSSSVLFDpskSSSSRTLQCEAPQCKqapnpsctvsksc 160
Cdd:PTZ00147 135 LANVMSYGEAKLGDNGQKFNFIFDTGSANLWVPSIKCttEGCETKNLYD---SSKSKTYEKDGTKVE------------- 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 161 gfnMTYGGSTIEAYLTQDTLTLASDVIPnYTFGCINKASG-----TSLPAQGLMGLGRGPLSLIS--------QSQN-LY 226
Cdd:PTZ00147 199 ---MNYVSGTVSGFFSKDLVTIGNLSVP-YKFIEVTDTNGfepfyTESDFDGIFGLGWKDLSIGSvdpyvvelKNQNkIE 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 227 QSTFSYCLPNSKSSnfSGSLRLGPKNQpiRIKTTPLLKNPRRSSLYYVNLVGIRVGN-------KIVDIPTSALAFdPAT 299
Cdd:PTZ00147 275 QAVFTFYLPPEDKH--KGYLTIGGIEE--RFYEGPLTYEKLNHDLYWQVDLDVHFGNvssekanVIVDSGTSVITV-PTE 349
                        250       260
                 ....*....|....*....|....*
gi 332645705 300 GAGTIFDSGTVYTRLVEPAYVAVRN 324
Cdd:PTZ00147 350 FLNKFVESLDVFKVPFLPLYVTTCN 374
Cathepsin_D_like cd05485
Cathepsin_D_like, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase ...
94-249 2.38e-04

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: 42.92  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705  94 IGTPAQPMLVALDTSNDAAWIPCSGC----VGCSSSVLFDPSKSSSSRtlqceapqckqapnpsctvSKSCGFNMTYGGS 169
Cdd:cd05485   18 IGTPPQSFKVVFDTGSSNLWVPSKKCswtnIACLLHNKYDSTKSSTYK-------------------KNGTEFAIQYGSG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332645705 170 TIEAYLTQDTLTLASDVIPNYTFG-CINKASGTSLPAQ--GLMGLGRGPLSLISQSQNLY---------QSTFSYCLPNS 237
Cdd:cd05485   79 SLSGFLSTDTVSVGGVSVKGQTFAeAINEPGLTFVAAKfdGILGMGYSSISVDGVVPVFYnmvnqklvdAPVFSFYLNRD 158
                        170
                 ....*....|..
gi 332645705 238 KSSNFSGSLRLG 249
Cdd:cd05485  159 PSAKEGGELILG 170
 
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