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Conserved domains on  [gi|219786506|emb|CAW43769|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

pepsin-like aspartic protease; pepsin/retropepsin-like aspartic protease family protein( domain architecture ID 10144432)

pepsin-like (A1 family) peptidase is an aspartic endoprotease that hydrolyzes the peptide bonds of substrates| pepsin/retropepsin-like aspartic protease family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pepsin_A_like_plant cd05476
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ...
89-467 1.10e-83

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: 258.73  E-value: 1.10e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  89 GYSVSLSFGTPSQTIPFVFDTGSSLVWLPCtsrylcsgcdfsgldptliprfipknsssskiigcqspkcqflygpnvqc 168
Cdd:cd05476    1 EYLVTLSIGTPPQPFSLIVDTGSDLTWTQC-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 169 rgcdpntrnctvgcPPYILQYGLGS-TAGVLITEKLDFPD--LTVPDFVVGCS----IISTRQPAGIAGFGRGPVSLPSQ 241
Cdd:cd05476   31 --------------CSYEYSYGDGSsTSGVLATETFTFGDssVSVPNVAFGCGtdneGGSFGGADGILGLGRGPLSLVSQ 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 242 MNLK--RFSHCLVSrrFDDTNVTTDLDLdtgsGHNSGSKTPGLTYTPFRKNPnvsnkAFLEYYYLNLRRIYVGRKHVKIP 319
Cdd:cd05476   97 LGSTgnKFSYCLVP--HDDTGGSSPLIL----GDAADLGGSGVVYTPLVKNP-----ANPTYYYVNLEGISVGGKRLPIP 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 320 YKYLAPGTNGDGGSIVDSGSTFTFMERPVFelvaeefasqmsnytrekdleketglgpcfnisgkgdvtvPELIFEFKGG 399
Cdd:cd05476  166 PSVFAIDSDGSGGTIIDSGTTLTYLPDPAY----------------------------------------PDLTLHFDGG 205
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219786506 400 AKLELPLSNYFtFVGNTDTVCLTVVSDktvnpsgGTGPAIILGSFQQQNYLVEYDLENDRFGFAKKKC 467
Cdd:cd05476  206 ADLELPPENYF-VDVGEGVVCLAILSS-------SSGGVSILGNIQQQNFLVEYDLENSRLGFAPADC 265
pepsin_retropepsin_like super family cl11403
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
97-219 3.28e-09

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 cd05470:

Pssm-ID: 472175 [Multi-domain]  Cd Length: 109  Bit Score: 54.31  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  97 GTPSQTIPFVFDTGSSLVWLPCTsrylcsGCDFSGLDPtLIPRFIPKNSSSSKIIGCqspkcqflygpnvqcrgcdpntr 176
Cdd:cd05470    6 GTPPQTFNVLLDTGSSNLWVPSV------DCQSLAIYS-HSSYDDPSASSTYSDNGC----------------------- 55
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 219786506 177 nctvgcpPYILQYGLGSTAGVLITEKLDFPDLTVPDFVVGCSI 219
Cdd:cd05470   56 -------TFSITYGTGSLSGGLSTDTVSIGDIEVVGQAFGCAT 91
 
Name Accession Description Interval E-value
pepsin_A_like_plant cd05476
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ...
89-467 1.10e-83

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: 258.73  E-value: 1.10e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  89 GYSVSLSFGTPSQTIPFVFDTGSSLVWLPCtsrylcsgcdfsgldptliprfipknsssskiigcqspkcqflygpnvqc 168
Cdd:cd05476    1 EYLVTLSIGTPPQPFSLIVDTGSDLTWTQC-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 169 rgcdpntrnctvgcPPYILQYGLGS-TAGVLITEKLDFPD--LTVPDFVVGCS----IISTRQPAGIAGFGRGPVSLPSQ 241
Cdd:cd05476   31 --------------CSYEYSYGDGSsTSGVLATETFTFGDssVSVPNVAFGCGtdneGGSFGGADGILGLGRGPLSLVSQ 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 242 MNLK--RFSHCLVSrrFDDTNVTTDLDLdtgsGHNSGSKTPGLTYTPFRKNPnvsnkAFLEYYYLNLRRIYVGRKHVKIP 319
Cdd:cd05476   97 LGSTgnKFSYCLVP--HDDTGGSSPLIL----GDAADLGGSGVVYTPLVKNP-----ANPTYYYVNLEGISVGGKRLPIP 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 320 YKYLAPGTNGDGGSIVDSGSTFTFMERPVFelvaeefasqmsnytrekdleketglgpcfnisgkgdvtvPELIFEFKGG 399
Cdd:cd05476  166 PSVFAIDSDGSGGTIIDSGTTLTYLPDPAY----------------------------------------PDLTLHFDGG 205
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219786506 400 AKLELPLSNYFtFVGNTDTVCLTVVSDktvnpsgGTGPAIILGSFQQQNYLVEYDLENDRFGFAKKKC 467
Cdd:cd05476  206 ADLELPPENYF-VDVGEGVVCLAILSS-------SSGGVSILGNIQQQNFLVEYDLENSRLGFAPADC 265
PLN03146 PLN03146
aspartyl protease family protein; Provisional
22-468 3.90e-44

aspartyl protease family protein; Provisional


Pssm-ID: 178691 [Multi-domain]  Cd Length: 431  Bit Score: 160.18  E-value: 3.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  22 PLSPFSHSDQSPKDpylSLRRLAESSIARAHKLkhgtsikpdedalsSTTTASATVVKSPLSAKSyGGYSVSLSFGTPSQ 101
Cdd:PLN03146  35 PKSPFYNPSETPSQ---RLRNAFRRSISRVNHF--------------RPTDASPNDPQSDLISNG-GEYLMNISIGTPPV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 102 TIPFVFDTGSSLVW---LPCTSRYlcsgcdfsgldPTLIPRFIPKNSSSSKIIGCQSPKCQFLygpNVQCRGCDPNTrnC 178
Cdd:PLN03146  97 PILAIADTGSDLIWtqcKPCDDCY-----------KQVSPLFDPKKSSTYKDVSCDSSQCQAL---GNQASCSDENT--C 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 179 TvgcppYILQYGLGS-TAGVLITEKLDFPDLT-----VPDFVVGC----SIISTRQPAGIAGFGRGPVSLPSQMNL---K 245
Cdd:PLN03146 161 T-----YSYSYGDGSfTKGNLAVETLTIGSTSgrpvsFPGIVFGCghnnGGTFDEKGSGIVGLGGGPLSLISQLGSsigG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 246 RFSHCLVSRRfDDTNVTTDLDLDTgSGHNSGSktpGLTYTPF-RKNPNVsnkafleYYYLNLRRIYVGRKhvKIPYKYLA 324
Cdd:PLN03146 236 KFSYCLVPLS-SDSNGTSKINFGT-NAIVSGS---GVVSTPLvSKDPDT-------FYYLTLEAISVGSK--KLPYTGSS 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 325 PGTNGDGGSIVDSGSTFTFMERPVFELVAEEFASQMsNYTREKDleKETGLGPCFNISgkGDVTVPELIFEFKgGAKLEL 404
Cdd:PLN03146 302 KNGVEEGNIIIDSGTTLTLLPSDFYSELESAVEEAI-GGERVSD--PQGLLSLCYSST--SDIKLPIITAHFT-GADVKL 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219786506 405 PLSNYFTFVgNTDTVCLTVVSdktvNPSGGtgpaiILGSFQQQNYLVEYDLENDRFGFAKKKCS 468
Cdd:PLN03146 376 QPLNTFVKV-SEDLVCFAMIP----TSSIA-----IFGNLAQMNFLVGYDLESKTVSFKPTDCT 429
TAXi_C pfam14541
Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly ...
302-463 5.11e-35

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: 127.78  E-value: 5.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  302 YYLNLRRIYVGRKHVKIPYKYLAPGTNGDGGSIVDSGSTFTFMERPVFELVAEEFASQMSNYTREKdLEKETGLGPCFNI 381
Cdd:pfam14541   2 YYIPLKGISVNGKRLPLPPGLLDIDRTGSGGTILDTGTPYTVLRPSVYRAVVQAFDKALAALGPRV-VAPVAPFDLCYNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  382 SGKGD----VTVPELIFEFKGGAKLELPLSNYFTFVGNtDTVCLTVVSDKTvnpsgGTGPAIILGSFQQQNYLVEYDLEN 457
Cdd:pfam14541  81 TGLGStrlgPAVPPITLVFEGGADWTIFGANSMVQVDG-GVACLGFVDGGV-----PPASASVIGGHQQEDNLLEFDLEK 154

                  ....*.
gi 219786506  458 DRFGFA 463
Cdd:pfam14541 155 SRLGFS 160
pepsin_retropepsin_like cd05470
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
97-219 3.28e-09

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: 54.31  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  97 GTPSQTIPFVFDTGSSLVWLPCTsrylcsGCDFSGLDPtLIPRFIPKNSSSSKIIGCqspkcqflygpnvqcrgcdpntr 176
Cdd:cd05470    6 GTPPQTFNVLLDTGSSNLWVPSV------DCQSLAIYS-HSSYDDPSASSTYSDNGC----------------------- 55
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 219786506 177 nctvgcpPYILQYGLGSTAGVLITEKLDFPDLTVPDFVVGCSI 219
Cdd:cd05470   56 -------TFSITYGTGSLSGGLSTDTVSIGDIEVVGQAFGCAT 91
 
Name Accession Description Interval E-value
pepsin_A_like_plant cd05476
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ...
89-467 1.10e-83

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: 258.73  E-value: 1.10e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  89 GYSVSLSFGTPSQTIPFVFDTGSSLVWLPCtsrylcsgcdfsgldptliprfipknsssskiigcqspkcqflygpnvqc 168
Cdd:cd05476    1 EYLVTLSIGTPPQPFSLIVDTGSDLTWTQC-------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 169 rgcdpntrnctvgcPPYILQYGLGS-TAGVLITEKLDFPD--LTVPDFVVGCS----IISTRQPAGIAGFGRGPVSLPSQ 241
Cdd:cd05476   31 --------------CSYEYSYGDGSsTSGVLATETFTFGDssVSVPNVAFGCGtdneGGSFGGADGILGLGRGPLSLVSQ 96
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 242 MNLK--RFSHCLVSrrFDDTNVTTDLDLdtgsGHNSGSKTPGLTYTPFRKNPnvsnkAFLEYYYLNLRRIYVGRKHVKIP 319
Cdd:cd05476   97 LGSTgnKFSYCLVP--HDDTGGSSPLIL----GDAADLGGSGVVYTPLVKNP-----ANPTYYYVNLEGISVGGKRLPIP 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 320 YKYLAPGTNGDGGSIVDSGSTFTFMERPVFelvaeefasqmsnytrekdleketglgpcfnisgkgdvtvPELIFEFKGG 399
Cdd:cd05476  166 PSVFAIDSDGSGGTIIDSGTTLTYLPDPAY----------------------------------------PDLTLHFDGG 205
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219786506 400 AKLELPLSNYFtFVGNTDTVCLTVVSDktvnpsgGTGPAIILGSFQQQNYLVEYDLENDRFGFAKKKC 467
Cdd:cd05476  206 ADLELPPENYF-VDVGEGVVCLAILSS-------SSGGVSILGNIQQQNFLVEYDLENSRLGFAPADC 265
cnd41_like cd05472
Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1, ...
90-467 1.03e-51

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: 176.69  E-value: 1.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  90 YSVSLSFGTPSQTIPFVFDTGSSLVWLPCtsrylcsgcdfsgldptliprfipknsssskiigcqSPKCQflygpnvqcr 169
Cdd:cd05472    2 YVVTVGLGTPARDQTVIVDTGSDLTWVQC------------------------------------QPCCL---------- 35
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 170 gcdpntrnctvgcppYILQYGLGS-TAGVLITEKLDF-PDLTVPDFVVGCSiisTRQ------PAGIAGFGRGPVSLPSQ 241
Cdd:cd05472   36 ---------------YQVSYGDGSyTTGDLATDTLTLgSSDVVPGFAFGCG---HDNeglfggAAGLLGLGRGKLSLPSQ 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 242 M---NLKRFSHCLVSRRfddtnvttdldlDTGSGH----NSGSKTPGLTYTPFRKNPNVSNkafleYYYLNLRRIYVGRK 314
Cdd:cd05472   98 TassYGGVFSYCLPDRS------------SSSSGYlsfgAAASVPAGASFTPMLSNPRVPT-----FYYVGLTGISVGGR 160
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 315 HVKIPykylaPGTNGDGGSIVDSGSTFTFMERPVFELVAEEFASQMSNYTREKDLekeTGLGPCFNISGKGDVTVPELIF 394
Cdd:cd05472  161 RLPIP-----PASFGAGGVIIDSGTVITRLPPSAYAALRDAFRAAMAAYPRAPGF---SILDTCYDLSGFRSVSVPTVSL 232
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219786506 395 EFKGGAKLELPLSNYFTFVGNTDTVCLTVVSDktvnpSGGTGPAIIlGSFQQQNYLVEYDLENDRFGFAKKKC 467
Cdd:cd05472  233 HFQGGADVELDASGVLYPVDDSSQVCLAFAGT-----SDDGGLSII-GNVQQQTFRVVYDVAGGRIGFAPGGC 299
pepsin_like cd05471
Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH; ...
90-464 2.02e-44

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: 157.20  E-value: 2.02e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  90 YSVSLSFGTPSQTIPFVFDTGSSLVWLPCTSrylcsgCDFSGLDPTLIPRFIPKNSSSSKIIGCqspkcqflygpnvqcr 169
Cdd:cd05471    1 YYGEITIGTPPQKFSVIFDTGSSLLWVPSSN------CTSCSCQKHPRFKYDSSKSSTYKDTGC---------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 170 gcdpntrnctvgcpPYILQYGLGSTAGVLITEKLDFPDLTVPDFVVGCS-----IISTRQPAGIAGFGRGP------VSL 238
Cdd:cd05471   59 --------------TFSITYGDGSVTGGLGTDTVTIGGLTIPNQTFGCAtsesgDFSSSGFDGILGLGFPSlsvdgvPSF 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 239 PSQMNL------KRFSHCLVsrRFDDTNVTTDLDLDtgsGHNSGSKTPGLTYTPFRKNPNvsnkaflEYYYLNLRRIYVG 312
Cdd:cd05471  125 FDQLKSqglissPVFSFYLG--RDGDGGNGGELTFG---GIDPSKYTGDLTYTPVVSNGP-------GYWQVPLDGISVG 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 313 RKHVKipykylapGTNGDGGSIVDSGSTFTFMERPVFELVAEEFASQMSNYTREkdleketGLGPCFNISgkgdvTVPEL 392
Cdd:cd05471  193 GKSVI--------SSSGGGGAIVDSGTSLIYLPSSVYDAILKALGAAVSSSDGG-------YGVDCSPCD-----TLPDI 252
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219786506 393 IFEFkggaklelplsnyftfvgntdtvcltvvsdktvnpsggtgpAIILGSFQQQNYLVEYDLENDRFGFAK 464
Cdd:cd05471  253 TFTF-----------------------------------------LWILGDVFLRNYYTVFDLDNNRIGFAP 283
PLN03146 PLN03146
aspartyl protease family protein; Provisional
22-468 3.90e-44

aspartyl protease family protein; Provisional


Pssm-ID: 178691 [Multi-domain]  Cd Length: 431  Bit Score: 160.18  E-value: 3.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  22 PLSPFSHSDQSPKDpylSLRRLAESSIARAHKLkhgtsikpdedalsSTTTASATVVKSPLSAKSyGGYSVSLSFGTPSQ 101
Cdd:PLN03146  35 PKSPFYNPSETPSQ---RLRNAFRRSISRVNHF--------------RPTDASPNDPQSDLISNG-GEYLMNISIGTPPV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 102 TIPFVFDTGSSLVW---LPCTSRYlcsgcdfsgldPTLIPRFIPKNSSSSKIIGCQSPKCQFLygpNVQCRGCDPNTrnC 178
Cdd:PLN03146  97 PILAIADTGSDLIWtqcKPCDDCY-----------KQVSPLFDPKKSSTYKDVSCDSSQCQAL---GNQASCSDENT--C 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 179 TvgcppYILQYGLGS-TAGVLITEKLDFPDLT-----VPDFVVGC----SIISTRQPAGIAGFGRGPVSLPSQMNL---K 245
Cdd:PLN03146 161 T-----YSYSYGDGSfTKGNLAVETLTIGSTSgrpvsFPGIVFGCghnnGGTFDEKGSGIVGLGGGPLSLISQLGSsigG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 246 RFSHCLVSRRfDDTNVTTDLDLDTgSGHNSGSktpGLTYTPF-RKNPNVsnkafleYYYLNLRRIYVGRKhvKIPYKYLA 324
Cdd:PLN03146 236 KFSYCLVPLS-SDSNGTSKINFGT-NAIVSGS---GVVSTPLvSKDPDT-------FYYLTLEAISVGSK--KLPYTGSS 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 325 PGTNGDGGSIVDSGSTFTFMERPVFELVAEEFASQMsNYTREKDleKETGLGPCFNISgkGDVTVPELIFEFKgGAKLEL 404
Cdd:PLN03146 302 KNGVEEGNIIIDSGTTLTLLPSDFYSELESAVEEAI-GGERVSD--PQGLLSLCYSST--SDIKLPIITAHFT-GADVKL 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219786506 405 PLSNYFTFVgNTDTVCLTVVSdktvNPSGGtgpaiILGSFQQQNYLVEYDLENDRFGFAKKKCS 468
Cdd:PLN03146 376 QPLNTFVKV-SEDLVCFAMIP----TSSIA-----IFGNLAQMNFLVGYDLESKTVSFKPTDCT 429
TAXi_C pfam14541
Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly ...
302-463 5.11e-35

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: 127.78  E-value: 5.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  302 YYLNLRRIYVGRKHVKIPYKYLAPGTNGDGGSIVDSGSTFTFMERPVFELVAEEFASQMSNYTREKdLEKETGLGPCFNI 381
Cdd:pfam14541   2 YYIPLKGISVNGKRLPLPPGLLDIDRTGSGGTILDTGTPYTVLRPSVYRAVVQAFDKALAALGPRV-VAPVAPFDLCYNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  382 SGKGD----VTVPELIFEFKGGAKLELPLSNYFTFVGNtDTVCLTVVSDKTvnpsgGTGPAIILGSFQQQNYLVEYDLEN 457
Cdd:pfam14541  81 TGLGStrlgPAVPPITLVFEGGADWTIFGANSMVQVDG-GVACLGFVDGGV-----PPASASVIGGHQQEDNLLEFDLEK 154

                  ....*.
gi 219786506  458 DRFGFA 463
Cdd:pfam14541 155 SRLGFS 160
TAXi_N pfam14543
Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly ...
90-253 4.31e-31

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: 117.76  E-value: 4.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506   90 YSVSLSFGTPSQTIPFVFDTGSSLVWLPCTSrylcsgCDFSGLDPTliprFIPKNSSSSKIIGCQSPKCQFLYGPNVQCr 169
Cdd:pfam14543   1 YLVTISIGTPPVPFFLVVDTGSDLTWVQCDP------CCYSQPDPL----FDPYKSSTYKPVPCSSPLCSLIALSSPGP- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  170 GCDPNTrnCTvgcppYILQYG-LGSTAGVLITEKLDFPD----LTVPDFVVGCSIISTRQ----PAGIAGFGRGPVSLPS 240
Cdd:pfam14543  70 CCSNNT--CD-----YEVSYGdGSSTSGVLATDTLTLNStggsVSVPNFVFGCGYNLLGGlpagADGILGLGRGKLSLPS 142
                         170
                  ....*....|....*...
gi 219786506  241 QMNLK-----RFSHCLVS 253
Cdd:pfam14543 143 QLASQgifgnKFSYCLSS 160
xylanase_inhibitor_I_like cd05489
TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a ...
101-463 1.20e-26

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: 110.52  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 101 QTIPFVFDTGSSLVWLPCTSRYlcsgcdfsgldptliprfipknSSSSKIIGCQSPKCQFLygPNVQCRGCD-----PNT 175
Cdd:cd05489    8 GAVPLVLDLAGPLLWSTCDAGH----------------------SSTYQTVPCSSSVCSLA--NRYHCPGTCggapgPGC 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 176 RNCTVGCPPY---ILQYGLGS-TAGVLITEKLDFPDL---TVPDFVVGC--SIISTRQP---AGIAGFGRGPVSLPSQMN 243
Cdd:cd05489   64 GNNTCTAHPYnpvTGECATGDlTQDVLSANTTDGSNPllvVIFNFVFSCapSLLLKGLPpgaQGVAGLGRSPLSLPAQLA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 244 -----LKRFSHCLVSrrfddtnvttdldLDTGSG-----------HNSGSKTP-GLTYTPFRKNPNVSNKafleyYYLNL 306
Cdd:cd05489  144 safgvARKFALCLPS-------------SPGGPGvaifgggpyylFPPPIDLSkSLSYTPLLTNPRKSGE-----YYIGV 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 307 RRIYVGRKHVKIPYKYLAPGTNGDGGSIVDSGSTFTFMERPVFELVAEEFASQMSNYTREKDLEKETGLgpCFNISGKGD 386
Cdd:cd05489  206 TSIAVNGHAVPLNPTLSANDRLGPGGVKLSTVVPYTVLRSDIYRAFTQAFAKATARIPRVPAAAVFPEL--CYPASALGN 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 387 VT----VPELIFEFKGGAKlelplsNYFTFVGNT------DTVCLTVVsDKTVNPSggtgPAIILGSFQQQNYLVEYDLE 456
Cdd:cd05489  284 TRlgyaVPAIDLVLDGGGV------NWTIFGANSmvqvkgGVACLAFV-DGGSEPR----PAVVIGGHQMEDNLLVFDLE 352

                 ....*..
gi 219786506 457 NDRFGFA 463
Cdd:cd05489  353 KSRLGFS 359
nucellin_like cd05475
Nucellins, plant aspartic proteases specifically expressed in nucellar cells during ...
88-467 3.34e-15

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: 75.49  E-value: 3.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  88 GGYSVSLSFGTPSQTIPFVFDTGSSLVWLPCTsrYLCSGCDfsgldptliprfipknsssskiigcqspkcqflygpnvq 167
Cdd:cd05475    1 GYYYVTINIGNPPKPYFLDIDTGSDLTWLQCD--APCTGCQ--------------------------------------- 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 168 crgCDpntrnctvgcppYILQYGL-GSTAGVLITEKLDFP----DLTVPDFVVGC----SIISTRQPA---GIAGFGRGP 235
Cdd:cd05475   40 ---CD------------YEIEYADgGSSMGVLVTDIFSLKltngSRAKPRIAFGCgydqQGPLLNPPPptdGILGLGRGK 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 236 VSLPSQMNLKR-----FSHCLVSRR-----FDDTNVTtdldldtgsghnsgskTPGLTYTPFRKNPnvsnkaFLEYYYLN 305
Cdd:cd05475  105 ISLPSQLASQGiiknvIGHCLSSNGggflfFGDDLVP----------------SSGVTWTPMRRES------QKKHYSPG 162
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 306 LRRIYVGRKhvkipykylapGTNGDGGSIV-DSGSTFT-FMERPVFELVAEEFASQmsnytrekdleketglgpcfnisg 383
Cdd:cd05475  163 PASLLFNGQ-----------PTGGKGLEVVfDSGSSYTyFNAQAYFKPLTLKFGKG------------------------ 207
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 384 kgdvtvpelifefKGGAKLELPLSNYFtFVGNTDTVCLTVVsDKTVNPSGGTgpaIILGSFQQQNYLVEYDLENDRFGFA 463
Cdd:cd05475  208 -------------WRTRLLEIPPENYL-IISEKGNVCLGIL-NGSEIGLGNT---NIIGDISMQGLMVIYDNEKQQIGWV 269

                 ....
gi 219786506 464 KKKC 467
Cdd:cd05475  270 RSDC 273
Plasmepsin_5 cd06096
Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite; The ...
87-349 1.07e-12

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: 68.94  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  87 YGGYSVSLSFGTPSQTIPFVFDTGSSLVWLPCTSrylCSGCDFSGLDPtliprFIPKNSSSSKIIGCQSPKCqflygpnv 166
Cdd:cd06096    1 YAYYFIDIFIGNPPQKQSLILDTGSSSLSFPCSQ---CKNCGIHMEPP-----YNLNNSITSSILYCDCNKC-------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 167 qCRGCDPNTRNCTvgcppYILQYGLGST-AGVLITEKLDFPDL--TVPDF-----VVGCSIIST----RQPA-GIAGFGR 233
Cdd:cd06096   65 -CYCLSCLNNKCE-----YSISYSEGSSiSGFYFSDFVSFESYlnSNSEKesfkkIFGCHTHETnlflTQQAtGILGLSL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 234 G-------PV-----SLPSQMNLKRFSHCLVSrrfDDTNVT---TDLDLDTGSGHNSGSKTPGLTYTPFRKnpnvsnkaf 298
Cdd:cd06096  139 TknnglptPIillftKRPKLKKDKIFSICLSE---DGGELTiggYDKDYTVRNSSIGNNKVSKIVWTPITR--------- 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 219786506 299 LEYYYLNLRRIYVGRKhvkipyKYLAPGTNGdGGSIVDSGSTFTFMERPVF 349
Cdd:cd06096  207 KYYYYVKLEGLSVYGT------TSNSGNTKG-LGMLVDSGSTLSHFPEDLY 250
Asp pfam00026
Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and ...
89-464 3.31e-12

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: 67.30  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506   89 GYSVSLSFGTPSQTIPFVFDTGSSLVWLPCTSRYLCSGCDFSGldptlipRFIPKNSSSSKiigcqspkcqflygpnvqc 168
Cdd:pfam00026   1 EYFGTISIGTPPQKFTVIFDTGSSDLWVPSSYCTKSSACKSHG-------TFDPSSSSTYK------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  169 rgcdpntrncTVGCPPYIlQYGLGSTAGVLITEKLDFPDLTVPDFVVGcsiISTRQPA---------GIAGFGrgpvsLP 239
Cdd:pfam00026  55 ----------LNGTTFSI-SYGDGSASGFLGQDTVTVGGLTITNQEFG---LATKEPGsffeyakfdGILGLG-----FP 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  240 SQ--MNLKRFSHCLVSRRFDDTNV-TTDLDLDTGSG-----------HNSGSktpgLTYTPfrknpnVSNKAfleYYYLN 305
Cdd:pfam00026 116 SIsaVGATPVFDNLKSQGLIDSPAfSVYLNSPDAAGgeiifggvdpsKYTGS----LTYVP------VTSQG---YWQIT 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  306 LRRIYVGRKHVKIPYKYLApgtngdggsIVDSGSTFTFMErpvfelvaEEFASQMSNYTREKDLEKETGLGPCFNISGKG 385
Cdd:pfam00026 183 LDSVTVGGSTSACSSGCQA---------ILDTGTSLLYGP--------TSIVSKIAKAVGASSSEYGEYVVDCDSISTLP 245
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219786506  386 DVTvpeliFEFkGGAKLELPLSNYFTFVGNTDTVCLTVVSdktvnpSGGTGPAIILGSFQQQNYLVEYDLENDRFGFAK 464
Cdd:pfam00026 246 DIT-----FVI-GGAKITVPPSAYVLQNSQGGSTCLSGFQ------PPPGGPLWILGDVFLRSAYVVFDRDNNRIGFAP 312
SAP_like cd05474
SAPs, pepsin-like proteinases secreted from pathogens to degrade host proteins; SAPs (Secreted ...
88-464 4.14e-12

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: 66.82  E-value: 4.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  88 GGYSVSLSFGTPSQTIPFVFDTGSSLVWLPctsrylcsgcDFSgldptliprfipknsssskiigcqspkcqflygpnvq 167
Cdd:cd05474    1 TYYSAELSVGTPPQKVTVLLDTGSSDLWVP----------DFS------------------------------------- 33
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 168 crgcdpntrnctvgcppyiLQYGLGSTA-GVLITEKLDFPDLTVPDFVVGCSIISTRQpAGIagFGRGPVSLPSQMNLKR 246
Cdd:cd05474   34 -------------------ISYGDGTSAsGTWGTDTVSIGGATVKNLQFAVANSTSSD-VGV--LGIGLPGNEATYGTGY 91
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 247 ----FSHCLVSRRFDDTNV----TTDLDLDTGS----GHNSGSKTPGLTYTPFrKNPNVSNKAFleYYYLNLRRIYVGRK 314
Cdd:cd05474   92 typnFPIALKKQGLIKKNAyslyLNDLDASTGSilfgGVDTAKYSGDLVTLPI-VNDNGGSEPS--ELSVTLSSISVNGS 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 315 HVKIPykylapGTNGDGGSIVDSGSTFTFMERPVFELVAEEFASQMSNYTrekdlekETGLGPCfniSGKGDVTvpeLIF 394
Cdd:cd05474  169 SGNTT------LLSKNLPALLDSGTTLTYLPSDIVDAIAKQLGATYDSDE-------GLYVVDC---DAKDDGS---LTF 229
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219786506 395 EFkGGAKLELPLSNYF---TFVGNTDTVC-LTVVSdktvnpsgGTGPAIILG-SFQQQNYLVeYDLENDRFGFAK 464
Cdd:cd05474  230 NF-GGATISVPLSDLVlpaSTDDGGDGACyLGIQP--------STSDYNILGdTFLRSAYVV-YDLDNNEISLAQ 294
pepsin_retropepsin_like cd05470
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
97-219 3.28e-09

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: 54.31  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  97 GTPSQTIPFVFDTGSSLVWLPCTsrylcsGCDFSGLDPtLIPRFIPKNSSSSKIIGCqspkcqflygpnvqcrgcdpntr 176
Cdd:cd05470    6 GTPPQTFNVLLDTGSSNLWVPSV------DCQSLAIYS-HSSYDDPSASSTYSDNGC----------------------- 55
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 219786506 177 nctvgcpPYILQYGLGSTAGVLITEKLDFPDLTVPDFVVGCSI 219
Cdd:cd05470   56 -------TFSITYGTGSLSGGLSTDTVSIGDIEVVGQAFGCAT 91
Cathepsin_D2 cd05490
Cathepsin_D2, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase of ...
82-464 1.15e-05

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: 47.09  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  82 LSAKSYGgysvSLSFGTPSQTIPFVFDTGSSLVWLPCTSrylCSGCDFSGLdptLIPRFIPKNSSSSkiigcqspkcqfl 161
Cdd:cd05490    3 MDAQYYG----EIGIGTPPQTFTVVFDTGSSNLWVPSVH---CSLLDIACW---LHHKYNSSKSSTY------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 162 ygpnVQCRgcdpntrnctvgcPPYILQYGLGSTAGVLITEKLDFPDLTVPDFVVGCSIistRQPA---------GIAGFG 232
Cdd:cd05490   60 ----VKNG-------------TEFAIQYGSGSLSGYLSQDTVSIGGLQVEGQLFGEAV---KQPGitfiaakfdGILGMA 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 233 RGPVSLpsqMNLKRFSHCLVSRRFDDTNVTT-----DLDLDTG-----SGHNSGSKTPGLTYTpfrknpNVSNKAfleYY 302
Cdd:cd05490  120 YPRISV---DGVTPVFDNIMAQKLVEQNVFSfylnrDPDAQPGgelmlGGTDPKYYTGDLHYV------NVTRKA---YW 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 303 YLNLRRIYVGRKHvkipykylapgTNGDGG--SIVDSGStfTFMERPVFELVAeefasqMSNYTREKDLEKETGLGPCFN 380
Cdd:cd05490  188 QIHMDQVDVGSGL-----------TLCKGGceAIVDTGT--SLITGPVEEVRA------LQKAIGAVPLIQGEYMIDCEK 248
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 381 ISgkgdvTVPELIFEFkGGAKLELPLSNYFTFVGNT-DTVCLTVVSDKTVNPSGgtGPAIILGS-FQQQNYLVeYDLEND 458
Cdd:cd05490  249 IP-----TLPVISFSL-GGKVYPLTGEDYILKVSQRgTTICLSGFMGLDIPPPA--GPLWILGDvFIGRYYTV-FDRDND 319

                 ....*.
gi 219786506 459 RFGFAK 464
Cdd:cd05490  320 RVGFAK 325
Proteinase_A_fungi cd05488
Fungal Proteinase A , aspartic proteinase superfamily; Fungal Proteinase A, a proteolytic ...
80-464 4.60e-05

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: 45.12  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  80 SPLSAKSYGGYSVSLSFGTPSQTIPFVFDTGSSLVWLP---CTSR--YLCSGCDFSgldptliprfipkNSSSSKIIGcq 154
Cdd:cd05488    1 VPLTNYLNAQYFTDITLGTPPQKFKVILDTGSSNLWVPsvkCGSIacFLHSKYDSS-------------ASSTYKANG-- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 155 spkcqflygpnvqcrgcdpntrnctvgcPPYILQYGLGSTAGVLITEKLDFPDLTVP--DFVVgcsiiSTRQPA------ 226
Cdd:cd05488   66 ----------------------------TEFKIQYGSGSLEGFVSQDTLSIGDLTIKkqDFAE-----ATSEPGlafafg 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 227 ---GIAGFGRGPVSLP-------SQMNLKRFSHCLVSRRFDDTNvtTDLDLDTGSGHNSGSKTPGLTYTPFRKnpnvsnK 296
Cdd:cd05488  113 kfdGILGLAYDTISVNkivppfyNMINQGLLDEPVFSFYLGSSE--EDGGEATFGGIDESRFTGKITWLPVRR------K 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 297 AfleYYYLNLRRIYVGRKHVKIPykylapgtngDGGSIVDSGSTFTFMERPVFELVAEEFASQMS---NYTreKDLEKET 373
Cdd:cd05488  185 A---YWEVELEKIGLGDEELELE----------NTGAAIDTGTSLIALPSDLAEMLNAEIGAKKSwngQYT--VDCSKVD 249
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 374 GLgpcfnisgkgdvtvPELIFEFkGGAKLELPLSNYFTFVGNTdtvCLTVVSDktVNPSGGTGPAIILGSFQQQNYLVEY 453
Cdd:cd05488  250 SL--------------PDLTFNF-DGYNFTLGPFDYTLEVSGS---CISAFTG--MDFPEPVGPLAIVGDAFLRKYYSVY 309
                        410
                 ....*....|.
gi 219786506 454 DLENDRFGFAK 464
Cdd:cd05488  310 DLGNNAVGLAK 320
phytepsin cd06098
Phytepsin, a plant homolog of mammalian lysosomal pepsins; Phytepsin, a plant homolog of ...
79-232 8.87e-05

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: 44.29  E-value: 8.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  79 KSPLSAKSYGgysvSLSFGTPSQTIPFVFDTGSSLVWLPCTSRYLCSGCDFSgldptliPRFIPKNSSSSKIIGcqspkc 158
Cdd:cd06098    4 KNYLDAQYFG----EIGIGTPPQKFTVIFDTGSSNLWVPSSKCYFSIACYFH-------SKYKSSKSSTYKKNG------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 159 qflygpnvqcrgcdpntRNCTVgcppyilQYGLGSTAGVLITEKLDFPDLTVPDFVVgcsIISTRQPA---------GIA 229
Cdd:cd06098   67 -----------------TSASI-------QYGTGSISGFFSQDSVTVGDLVVKNQVF---IEATKEPGltfllakfdGIL 119

                 ...
gi 219786506 230 GFG 232
Cdd:cd06098  120 GLG 122
pepsin_A cd05478
Pepsin A, aspartic protease produced in gastric mucosa of mammals; Pepsin, a well-known ...
90-464 8.15e-04

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: 41.28  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  90 YSVSLSFGTPSQTIPFVFDTGSSLVWLP---CTSRyLCSGCDfsgldptlipRFIPKNSSSSKIIGcqspkcqflygpnv 166
Cdd:cd05478   11 YYGTISIGTPPQDFTVIFDTGSSNLWVPsvyCSSQ-ACSNHN----------RFNPRQSSTYQSTG-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 167 qcrgcdpntrnctvgcPPYILQYGLGSTAGVLITEKLDFPDLTVPDFVVGcsiISTRQPA---------GIAGFGRGPVS 237
Cdd:cd05478   66 ----------------QPLSIQYGTGSMTGILGYDTVQVGGISDTNQIFG---LSETEPGsffyyapfdGILGLAYPSIA 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 238 ----LPSQMNLkrFSHCLVSRrfDDTNVTTDLDLDTGS-----GHNSGSKTPGLTYTPfrknpnVSNKAfleYYYLNLRR 308
Cdd:cd05478  127 ssgaTPVFDNM--MSQGLVSQ--DLFSVYLSSNGQQGSvvtfgGIDPSYYTGSLNWVP------VTAET---YWQITVDS 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506 309 IYVGRKHVkipykylapGTNGDGGSIVDSG-STFTFMERPVFELVAEEFASQMSNytrekdlekETGLGPCFNISgkgdv 387
Cdd:cd05478  194 VTINGQVV---------ACSGGCQAIVDTGtSLLVGPSSDIANIQSDIGASQNQN---------GEMVVNCSSIS----- 250
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219786506 388 TVPELIFEFkGGAKLELPLSNYftfVGNTDTVCLTVVSdktvnpSGGTGPAIILGSFQQQNYLVEYDLENDRFGFAK 464
Cdd:cd05478  251 SMPDVVFTI-NGVQYPLPPSAY---ILQDQGSCTSGFQ------SMGLGELWILGDVFIRQYYSVFDRANNKVGLAP 317
Cathespin_E cd05486
Cathepsin E, non-lysosomal aspartic protease; Cathepsin E is an intracellular, non-lysosomal ...
90-210 4.05e-03

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: 39.10  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219786506  90 YSVSLSFGTPSQTIPFVFDTGSSLVWLP---CTSRyLCSGCDfsgldptlipRFIPKNSSSskiigcqspkcqflYGPNV 166
Cdd:cd05486    1 YFGQISIGTPPQNFTVIFDTGSSNLWVPsiyCTSQ-ACTKHN----------RFQPSESST--------------YVSNG 55
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 219786506 167 QcrgcdpntrnctvgcpPYILQYGLGSTAGVLITEKLDFPDLTV 210
Cdd:cd05486   56 E----------------AFSIQYGTGSLTGIIGIDQVTVEGITV 83
renin_like cd05487
Renin stimulates production of angiotensin and thus affects blood pressure; Renin, also known ...
90-125 6.24e-03

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: 38.61  E-value: 6.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 219786506  90 YSVSLSFGTPSQTIPFVFDTGSSLVWLPCTSrylCS 125
Cdd:cd05487    9 YYGEIGIGTPPQTFKVVFDTGSSNLWVPSSK---CS 41
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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