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Conserved domains on  [gi|257723128|emb|CBD26183|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

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

pepsin/retropepsin-like aspartic protease family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pepsin_retropepsin_like super family cl11403
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
89-435 1.60e-38

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 cd05476:

Pssm-ID: 472175 [Multi-domain]  Cd Length: 265  Bit Score: 141.25  E-value: 1.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLPCncnstcvrsmetdqgeriklniynpskskssskvtcnstlcalrnrcispv 168
Cdd:cd05476    2 YLVTLSIGTPPQPFSLIVDTGSDLTWTQC--------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 169 sdCPYRIRYLSpGSKSTGVLVEDVIHMstEEGEARDARITFGCSESQLGLFKEVAvNGIMGLAIADIAVPNMLvkaGVAS 248
Cdd:cd05476   31 --CSYEYSYGD-GSSTSGVLATETFTF--GDSSVSVPNVAFGCGTDNEGGSFGGA-DGILGLGRGPLSLVSQL---GSTG 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 249 DSFSMCFGP----NGKGTISFGD---KGSSDQLETPL-SGTISPMFYDVSITKFKVGKVTVDTEFTATF----------- 309
Cdd:cd05476  102 NKFSYCLVPhddtGGSSPLILGDaadLGGSGVVYTPLvKNPANPTYYYVNLEGISVGGKRLPIPPSVFAidsdgsggtii 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 310 DSGTAVTWLIEPYYtalttnfhlsvpdrrlsksvdspfefcyiitstsdedklPSVSFEMKGGAAYDVFSPILVFDTSDG 389
Cdd:cd05476  182 DSGTTLTYLPDPAY---------------------------------------PDLTLHFDGGADLELPPENYFVDVGEG 222
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 257723128 390 sfqVYCLAVLKQVNADFSIIGQNFMTNYRIVHDRERRILGWKKSNC 435
Cdd:cd05476  223 ---VVCLAILSSSSGGVSILGNIQQQNFLVEYDLENSRLGFAPADC 265
 
Name Accession Description Interval E-value
pepsin_A_like_plant cd05476
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ...
89-435 1.60e-38

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: 141.25  E-value: 1.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLPCncnstcvrsmetdqgeriklniynpskskssskvtcnstlcalrnrcispv 168
Cdd:cd05476    2 YLVTLSIGTPPQPFSLIVDTGSDLTWTQC--------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 169 sdCPYRIRYLSpGSKSTGVLVEDVIHMstEEGEARDARITFGCSESQLGLFKEVAvNGIMGLAIADIAVPNMLvkaGVAS 248
Cdd:cd05476   31 --CSYEYSYGD-GSSTSGVLATETFTF--GDSSVSVPNVAFGCGTDNEGGSFGGA-DGILGLGRGPLSLVSQL---GSTG 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 249 DSFSMCFGP----NGKGTISFGD---KGSSDQLETPL-SGTISPMFYDVSITKFKVGKVTVDTEFTATF----------- 309
Cdd:cd05476  102 NKFSYCLVPhddtGGSSPLILGDaadLGGSGVVYTPLvKNPANPTYYYVNLEGISVGGKRLPIPPSVFAidsdgsggtii 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 310 DSGTAVTWLIEPYYtalttnfhlsvpdrrlsksvdspfefcyiitstsdedklPSVSFEMKGGAAYDVFSPILVFDTSDG 389
Cdd:cd05476  182 DSGTTLTYLPDPAY---------------------------------------PDLTLHFDGGADLELPPENYFVDVGEG 222
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 257723128 390 sfqVYCLAVLKQVNADFSIIGQNFMTNYRIVHDRERRILGWKKSNC 435
Cdd:cd05476  223 ---VVCLAILSSSSGGVSILGNIQQQNFLVEYDLENSRLGFAPADC 265
TAXi_N pfam14543
Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly ...
90-267 2.33e-32

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: 121.61  E-value: 2.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128   90 YANVTIGTPAQWFLVALDTGSDLFWLPCNCnstCVRSmetdqgerIKLNIYNPSKSKSSSKVTCNSTLCAL----RNRCI 165
Cdd:pfam14543   2 LVTISIGTPPVPFFLVVDTGSDLTWVQCDP---CCYS--------QPDPLFDPYKSSTYKPVPCSSPLCSLialsSPGPC 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  166 SPVSDCPYRIRYlSPGSKSTGVLVEDVIHMSTEEGEARDARITFGCSESQL-GLFKEVAvnGIMGLAIADIAVPNMLVKA 244
Cdd:pfam14543  71 CSNNTCDYEVSY-GDGSSTSGVLATDTLTLNSTGGSVSVPNFVFGCGYNLLgGLPAGAD--GILGLGRGKLSLPSQLASQ 147
                         170       180
                  ....*....|....*....|....*
gi 257723128  245 GVASDSFSMCFG--PNGKGTISFGD 267
Cdd:pfam14543 148 GIFGNKFSYCLSssSSGSGVLFFGD 172
PLN03146 PLN03146
aspartyl protease family protein; Provisional
92-435 1.14e-13

aspartyl protease family protein; Provisional


Pssm-ID: 178691 [Multi-domain]  Cd Length: 431  Bit Score: 72.74  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  92 NVTIGTPAQWFLVALDTGSDLFWLPCNCNSTCVRSMETdqgeriklnIYNPSKSKSSSKVTCNSTLC-ALRN-RCISPVS 169
Cdd:PLN03146  88 NISIGTPPVPILAIADTGSDLIWTQCKPCDDCYKQVSP---------LFDPKKSSTYKDVSCDSSQCqALGNqASCSDEN 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 170 DCPYRIRYlSPGSKSTGVLVEDVIHM-STEEGEARDARITFGCSESQLGLFKEVAvNGIMGLAIADIAVPNMLVKAgvAS 248
Cdd:PLN03146 159 TCTYSYSY-GDGSFTKGNLAVETLTIgSTSGRPVSFPGIVFGCGHNNGGTFDEKG-SGIVGLGGGPLSLISQLGSS--IG 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 249 DSFSMCFGP-----NGKGTISFGDKG---SSDQLETPLSGTISPMFYDVSITKFKVGKVTV---DTEFTAT------FDS 311
Cdd:PLN03146 235 GKFSYCLVPlssdsNGTSKINFGTNAivsGSGVVSTPLVSKDPDTFYYLTLEAISVGSKKLpytGSSKNGVeegniiIDS 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 312 GTAVTWLIEPYYTALTTNFHLSVPDRRLSKSvDSPFEFCYiitSTSDEDKLPSVSFEMKGGaayDV-FSPILVF-DTSDG 389
Cdd:PLN03146 315 GTTLTLLPSDFYSELESAVEEAIGGERVSDP-QGLLSLCY---SSTSDIKLPIITAHFTGA---DVkLQPLNTFvKVSED 387
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 257723128 390 sfqVYCLAVlkQVNADFSIIGQNFMTNYRIVHDRERRILGWKKSNC 435
Cdd:PLN03146 388 ---LVCFAM--IPTSSIAIFGNLAQMNFLVGYDLESKTVSFKPTDC 428
 
Name Accession Description Interval E-value
pepsin_A_like_plant cd05476
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ...
89-435 1.60e-38

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: 141.25  E-value: 1.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLPCncnstcvrsmetdqgeriklniynpskskssskvtcnstlcalrnrcispv 168
Cdd:cd05476    2 YLVTLSIGTPPQPFSLIVDTGSDLTWTQC--------------------------------------------------- 30
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 169 sdCPYRIRYLSpGSKSTGVLVEDVIHMstEEGEARDARITFGCSESQLGLFKEVAvNGIMGLAIADIAVPNMLvkaGVAS 248
Cdd:cd05476   31 --CSYEYSYGD-GSSTSGVLATETFTF--GDSSVSVPNVAFGCGTDNEGGSFGGA-DGILGLGRGPLSLVSQL---GSTG 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 249 DSFSMCFGP----NGKGTISFGD---KGSSDQLETPL-SGTISPMFYDVSITKFKVGKVTVDTEFTATF----------- 309
Cdd:cd05476  102 NKFSYCLVPhddtGGSSPLILGDaadLGGSGVVYTPLvKNPANPTYYYVNLEGISVGGKRLPIPPSVFAidsdgsggtii 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 310 DSGTAVTWLIEPYYtalttnfhlsvpdrrlsksvdspfefcyiitstsdedklPSVSFEMKGGAAYDVFSPILVFDTSDG 389
Cdd:cd05476  182 DSGTTLTYLPDPAY---------------------------------------PDLTLHFDGGADLELPPENYFVDVGEG 222
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 257723128 390 sfqVYCLAVLKQVNADFSIIGQNFMTNYRIVHDRERRILGWKKSNC 435
Cdd:cd05476  223 ---VVCLAILSSSSGGVSILGNIQQQNFLVEYDLENSRLGFAPADC 265
pepsin_like cd05471
Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH; ...
90-432 1.89e-32

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: 125.23  E-value: 1.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  90 YANVTIGTPAQWFLVALDTGSDLFWLPC-NCNSTCVRSMetdqgeriKLNIYNPSKSKssskvTCNSTlcalrnrcispv 168
Cdd:cd05471    2 YGEITIGTPPQKFSVIFDTGSSLLWVPSsNCTSCSCQKH--------PRFKYDSSKSS-----TYKDT------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 169 sDCPYRIRYLSpgSKSTGVLVEDVIHMsteeGEARDARITFGCSESQLGLFKEVAVNGIMGLAIADIAVPNM------LV 242
Cdd:cd05471   57 -GCTFSITYGD--GSVTGGLGTDTVTI----GGLTIPNQTFGCATSESGDFSSSGFDGILGLGFPSLSVDGVpsffdqLK 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 243 KAGVASDS-FSMCFGPNGK----GTISFG----DKGSSDQLETPLSgTISPMFYDVSITKFKVGKVTVDTEF---TATFD 310
Cdd:cd05471  130 SQGLISSPvFSFYLGRDGDggngGELTFGgidpSKYTGDLTYTPVV-SNGPGYWQVPLDGISVGGKSVISSSgggGAIVD 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 311 SGTAVTWLIEPYYTALTTNFHLSVpdrrlsksvdsPFEFCYIITSTSDEDKLPSVSFEMkggaaydvfspilvfdtsdgs 390
Cdd:cd05471  209 SGTSLIYLPSSVYDAILKALGAAV-----------SSSDGGYGVDCSPCDTLPDITFTF--------------------- 256
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 257723128 391 fqvyclavlkqvnadFSIIGQNFMTNYRIVHDRERRILGWKK 432
Cdd:cd05471  257 ---------------LWILGDVFLRNYYTVFDLDNNRIGFAP 283
TAXi_N pfam14543
Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly ...
90-267 2.33e-32

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: 121.61  E-value: 2.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128   90 YANVTIGTPAQWFLVALDTGSDLFWLPCNCnstCVRSmetdqgerIKLNIYNPSKSKSSSKVTCNSTLCAL----RNRCI 165
Cdd:pfam14543   2 LVTISIGTPPVPFFLVVDTGSDLTWVQCDP---CCYS--------QPDPLFDPYKSSTYKPVPCSSPLCSLialsSPGPC 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  166 SPVSDCPYRIRYlSPGSKSTGVLVEDVIHMSTEEGEARDARITFGCSESQL-GLFKEVAvnGIMGLAIADIAVPNMLVKA 244
Cdd:pfam14543  71 CSNNTCDYEVSY-GDGSSTSGVLATDTLTLNSTGGSVSVPNFVFGCGYNLLgGLPAGAD--GILGLGRGKLSLPSQLASQ 147
                         170       180
                  ....*....|....*....|....*
gi 257723128  245 GVASDSFSMCFG--PNGKGTISFGD 267
Cdd:pfam14543 148 GIFGNKFSYCLSssSSGSGVLFFGD 172
nucellin_like cd05475
Nucellins, plant aspartic proteases specifically expressed in nucellar cells during ...
88-435 5.79e-30

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: 117.86  E-value: 5.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  88 LHYANVTIGTPAQWFLVALDTGSDLFWLpcNCNSTCVRsmetdqgeriklniynpskskssskvtCNstlcalrnrcisp 167
Cdd:cd05475    2 YYYVTINIGNPPKPYFLDIDTGSDLTWL--QCDAPCTG---------------------------CQ------------- 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 168 vsdCPYRIRYlSPGSKSTGVLVEDVIHMSTEEGEARDARITFGCSESQLGLFKEV--AVNGIMGLAIADIAVPNMLVKAG 245
Cdd:cd05475   40 ---CDYEIEY-ADGGSSMGVLVTDIFSLKLTNGSRAKPRIAFGCGYDQQGPLLNPppPTDGILGLGRGKISLPSQLASQG 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 246 VASDSFSMCFGPNGKGTISFGDK--GSSDQLETPLSGTISPMFYDVSITKFKV-GKVTVDTEFTATFDSGTAVTWLI-EP 321
Cdd:cd05475  116 IIKNVIGHCLSSNGGGFLFFGDDlvPSSGVTWTPMRRESQKKHYSPGPASLLFnGQPTGGKGLEVVFDSGSSYTYFNaQA 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 322 YYTALTTNFhlsvPDRRLSKSVDSPFEfCYIITStsdedklpsvsfeMKGGAaydvfspilvfdtsdgsfqvyCLAVL-- 399
Cdd:cd05475  196 YFKPLTLKF----GKGWRTRLLEIPPE-NYLIIS-------------EKGNV---------------------CLGILng 236
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 257723128 400 KQVN-ADFSIIGQNFMTNYRIVHDRERRILGWKKSNC 435
Cdd:cd05475  237 SEIGlGNTNIIGDISMQGLMVIYDNEKQQIGWVRSDC 273
cnd41_like cd05472
Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1, ...
90-435 3.43e-22

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: 96.57  E-value: 3.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  90 YANVTIGTPAQWFLVALDTGSDLFWLPCncnSTCvrsmetdqgeriklniynpskskssskvtcnstlcalrnrcispvs 169
Cdd:cd05472    3 VVTVGLGTPARDQTVIVDTGSDLTWVQC---QPC---------------------------------------------- 33
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 170 dCPYRIRYlSPGSKSTGVLVEDVIhmsTEEGEARDARITFGCSESQLGLFKEVAvnGIMGLAIADIAVPNMLvkAGVASD 249
Cdd:cd05472   34 -CLYQVSY-GDGSYTTGDLATDTL---TLGSSDVVPGFAFGCGHDNEGLFGGAA--GLLGLGRGKLSLPSQT--ASSYGG 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 250 SFSMCFGP---NGKGTISFGDKGSSDQLE--TPL-SGTISPMFYDVSITKFKVG--KVTVDTEFTAT----FDSGTAVTW 317
Cdd:cd05472  105 VFSYCLPDrssSSSGYLSFGAAASVPAGAsfTPMlSNPRVPTFYYVGLTGISVGgrRLPIPPASFGAggviIDSGTVITR 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 318 LIEPYYTALTTNFHLSVPDRRLSKSVdSPFEFCYIITSTsDEDKLPSVSFEMKGGAAYDVFSPILVFDTSDGSfqVYCLA 397
Cdd:cd05472  185 LPPSAYAALRDAFRAAMAAYPRAPGF-SILDTCYDLSGF-RSVSVPTVSLHFQGGADVELDASGVLYPVDDSS--QVCLA 260
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 257723128 398 VL-KQVNADFSIIGQNFMTNYRIVHDRERRILGWKKSNC 435
Cdd:cd05472  261 FAgTSDDGGLSIIGNVQQQTFRVVYDVAGGRIGFAPGGC 299
Plasmepsin_5 cd06096
Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite; The ...
89-436 6.45e-16

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: 78.57  E-value: 6.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLPCNCNSTCVRSMEtdqgeriklNIYNPSKSKSSSKVTCNSTLCALRNRCISpv 168
Cdd:cd06096    4 YFIDIFIGNPPQKQSLILDTGSSSLSFPCSQCKNCGIHME---------PPYNLNNSITSSILYCDCNKCCYCLSCLN-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 169 SDCPYRIRYlSPGSKSTGVLVEDVIHMSTEEGEARDARI---TFGCSESQLGLFKEVAVNGIMGLAIAD---IAVPNMLV 242
Cdd:cd06096   73 NKCEYSISY-SEGSSISGFYFSDFVSFESYLNSNSEKESfkkIFGCHTHETNLFLTQQATGILGLSLTKnngLPTPIILL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 243 KAGVASDS----FSMCFGPNGkGTISFG--------------DKGSSDQLETPlsgTISPMFYDVSITKFKVGK----VT 300
Cdd:cd06096  152 FTKRPKLKkdkiFSICLSEDG-GELTIGgydkdytvrnssigNNKVSKIVWTP---ITRKYYYYVKLEGLSVYGttsnSG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 301 VDTEFTATFDSGTAVTWLIEPYYTALTTNFhlsvPDRrlsksvdspfefcYIITSTSDEDKLPSVSFemkggaaydvfsp 380
Cdd:cd06096  228 NTKGLGMLVDSGSTLSHFPEDLYNKINNFF----PTI-------------TIIFENNLKIDWKPSSY------------- 277
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 257723128 381 iLVFDTSdgsfQVYCLAVlKQVNaDFSIIGQNFMTNYRIVHDRERRILGWKKSNCN 436
Cdd:cd06096  278 -LYKKES----FWCKGGE-KSVS-NKPILGASFFKNKQIIFDLDNNRIGFVESNCP 326
Asp pfam00026
Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and ...
90-424 6.63e-15

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: 75.39  E-value: 6.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128   90 YANVTIGTPAQWFLVALDTGSDLFWLP---CNCNSTCVRSmetdqgeriklNIYNPSKskssskvtcnSTLCALRNRCIS 166
Cdd:pfam00026   3 FGTISIGTPPQKFTVIFDTGSSDLWVPssyCTKSSACKSH-----------GTFDPSS----------SSTYKLNGTTFS 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  167 pvsdcpyrIRYlspGSKS-TGVLVEDVIHMsteeGEARDARITFGCSESQLGLFKEVAVN-GIMGLAIADIAV------- 237
Cdd:pfam00026  62 --------ISY---GDGSaSGFLGQDTVTV----GGLTITNQEFGLATKEPGSFFEYAKFdGILGLGFPSISAvgatpvf 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  238 PNMLVKAGVASDSFS--MCFGPNGKGTISFG----DKGSSDQLETPLSgtiSPMFYDVSITKFKVGKVTVDTEFT--ATF 309
Cdd:pfam00026 127 DNLKSQGLIDSPAFSvyLNSPDAAGGEIIFGgvdpSKYTGSLTYVPVT---SQGYWQITLDSVTVGGSTSACSSGcqAIL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  310 DSGTAvtwliepyYTALTTNFHLSVPDRRLSKSVdspfEFCYIITSTSDEDKLPSVSFEMkGGAAYDVFSPILVFDTSDG 389
Cdd:pfam00026 204 DTGTS--------LLYGPTSIVSKIAKAVGASSS----EYGEYVVDCDSISTLPDITFVI-GGAKITVPPSAYVLQNSQG 270
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 257723128  390 SFQVYcLAVLKQVNADFSIIGQNFMTNYRIVHDRE 424
Cdd:pfam00026 271 GSTCL-SGFQPPPGGPLWILGDVFLRSAYVVFDRD 304
PLN03146 PLN03146
aspartyl protease family protein; Provisional
92-435 1.14e-13

aspartyl protease family protein; Provisional


Pssm-ID: 178691 [Multi-domain]  Cd Length: 431  Bit Score: 72.74  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  92 NVTIGTPAQWFLVALDTGSDLFWLPCNCNSTCVRSMETdqgeriklnIYNPSKSKSSSKVTCNSTLC-ALRN-RCISPVS 169
Cdd:PLN03146  88 NISIGTPPVPILAIADTGSDLIWTQCKPCDDCYKQVSP---------LFDPKKSSTYKDVSCDSSQCqALGNqASCSDEN 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 170 DCPYRIRYlSPGSKSTGVLVEDVIHM-STEEGEARDARITFGCSESQLGLFKEVAvNGIMGLAIADIAVPNMLVKAgvAS 248
Cdd:PLN03146 159 TCTYSYSY-GDGSFTKGNLAVETLTIgSTSGRPVSFPGIVFGCGHNNGGTFDEKG-SGIVGLGGGPLSLISQLGSS--IG 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 249 DSFSMCFGP-----NGKGTISFGDKG---SSDQLETPLSGTISPMFYDVSITKFKVGKVTV---DTEFTAT------FDS 311
Cdd:PLN03146 235 GKFSYCLVPlssdsNGTSKINFGTNAivsGSGVVSTPLVSKDPDTFYYLTLEAISVGSKKLpytGSSKNGVeegniiIDS 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 312 GTAVTWLIEPYYTALTTNFHLSVPDRRLSKSvDSPFEFCYiitSTSDEDKLPSVSFEMKGGaayDV-FSPILVF-DTSDG 389
Cdd:PLN03146 315 GTTLTLLPSDFYSELESAVEEAIGGERVSDP-QGLLSLCY---SSTSDIKLPIITAHFTGA---DVkLQPLNTFvKVSED 387
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 257723128 390 sfqVYCLAVlkQVNADFSIIGQNFMTNYRIVHDRERRILGWKKSNC 435
Cdd:PLN03146 388 ---LVCFAM--IPTSSIAIFGNLAQMNFLVGYDLESKTVSFKPTDC 428
Aspergillopepsin_like cd06097
Aspergillopepsin_like, aspartic proteases of fungal origin; The members of this family are ...
90-378 5.24e-13

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: 69.25  E-value: 5.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  90 YANVTIGTPAQWFLVALDTGSDLFWlpcncnstcVRSMETDQGERIKLNIYNPSkskssskvtcNSTLCALrnrcispVS 169
Cdd:cd06097    2 LTPVKIGTPPQTLNLDLDTGSSDLW---------VFSSETPAAQQGGHKLYDPS----------KSSTAKL-------LP 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 170 DCPYRIRYlSPGSKSTGVLVEDVIhmSTEEGEARDARITFGCSESQlGLFKEVAVNGIMGLAIADIA----------VPN 239
Cdd:cd06097   56 GATWSISY-GDGSSASGIVYTDTV--SIGGVEVPNQAIELATAVSA-SFFSDTASDGLLGLAFSSINtvqppkqktfFEN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 240 ML--VKAGVasdsFSMCFGPNGKGTISFgdkGSSDqlETPLSGTI-------SPMFYDVSITKFKVG--KVTVDTEFTAT 308
Cdd:cd06097  132 ALssLDAPL----FTADLRKAAPGFYTF---GYID--ESKYKGEIswtpvdnSSGFWQFTSTSYTVGgdAPWSRSGFSAI 202
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257723128 309 FDSGTAVTWLIEPyytaLTTNFHLSVPDRRLSKSVDSpfefcYIITSTSdedKLPSVSF-------EMKGGAAYDVF 378
Cdd:cd06097  203 ADTGTTLILLPDA----IVEAYYSQVPGAYYDSEYGG-----WVFPCDT---TLPDLSFavfsilgDVFLKAQYVVF 267
TAXi_C pfam14541
Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly ...
308-429 4.56e-08

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: 52.28  E-value: 4.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  308 TFDSGTAVTWLIEPYYTALTTNF--HLSVPDRRLSKSVDsPFEFCY---IITSTSDEDKLPSVSFEMKGGAAYDVFSPIL 382
Cdd:pfam14541  34 ILDTGTPYTVLRPSVYRAVVQAFdkALAALGPRVVAPVA-PFDLCYnstGLGSTRLGPAVPPITLVFEGGADWTIFGANS 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 257723128  383 VFDTSDGsfqVYCLAVLKQVNADF--SIIGQNFMTNYRIVHDRERRILG 429
Cdd:pfam14541 113 MVQVDGG---VACLGFVDGGVPPAsaSVIGGHQQEDNLLEFDLEKSRLG 158
xylanase_inhibitor_I_like cd05489
TAXI-I inhibits degradation of xylan in the cell wall; Xylanase inhibitor-I (TAXI-I) is a ...
151-429 1.98e-07

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: 53.12  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 151 VTCNSTLCALRNRC-------ISPVSDC--------PYrirylSP--GSKSTGVLVEDVIHMSTEEG------EARDAri 207
Cdd:cd05489   36 VPCSSSVCSLANRYhcpgtcgGAPGPGCgnntctahPY-----NPvtGECATGDLTQDVLSANTTDGsnpllvVIFNF-- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 208 TFGCSESQL--GLFKEVAvnGIMGLAIADIAVPNMLVKA-GVASdSFSMCF--GPNGKGTISFGDKG----------SSD 272
Cdd:cd05489  109 VFSCAPSLLlkGLPPGAQ--GVAGLGRSPLSLPAQLASAfGVAR-KFALCLpsSPGGPGVAIFGGGPyylfpppidlSKS 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 273 QLETPL--SGTISPMFYdVSITKFKVGKVTVDTEFTATFD--SGTAVTWL--IEPY-------YTALTTNFHLSVPDRRL 339
Cdd:cd05489  186 LSYTPLltNPRKSGEYY-IGVTSIAVNGHAVPLNPTLSANdrLGPGGVKLstVVPYtvlrsdiYRAFTQAFAKATARIPR 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 340 SKSVDSPFEFCY---IITSTSDEDKLPSVSFEMKG-GAAYDVFSPILVFDTSDGsfqVYCLAVL--KQVNADFSIIGQNF 413
Cdd:cd05489  265 VPAAAVFPELCYpasALGNTRLGYAVPAIDLVLDGgGVNWTIFGANSMVQVKGG---VACLAFVdgGSEPRPAVVIGGHQ 341
                        330
                 ....*....|....*.
gi 257723128 414 MTNYRIVHDRERRILG 429
Cdd:cd05489  342 MEDNLLVFDLEKSRLG 357
pepsin_A cd05478
Pepsin A, aspartic protease produced in gastric mucosa of mammals; Pepsin, a well-known ...
89-429 3.03e-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: 52.06  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLPcncnstcvrsmetdqgeriklniynpsksksssKVTCNSTLCALRNRcISPV 168
Cdd:cd05478   11 YYGTISIGTPPQDFTVIFDTGSSNLWVP---------------------------------SVYCSSQACSNHNR-FNPR 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 169 SDCPYR-------IRYlspGSKS-TGVLVEDVIHMsteeGEARDARITFGCSESQLGLFKEVA-VNGIMGLAI----ADI 235
Cdd:cd05478   57 QSSTYQstgqplsIQY---GTGSmTGILGYDTVQV----GGISDTNQIFGLSETEPGSFFYYApFDGILGLAYpsiaSSG 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 236 AVP---NMLVKAGVASDSFSMCFGPNgkgtisfGDKGSsdqleTPLSGTISPMFYDVSIT----------KFKVGKVTVD 302
Cdd:cd05478  130 ATPvfdNMMSQGLVSQDLFSVYLSSN-------GQQGS-----VVTFGGIDPSYYTGSLNwvpvtaetywQITVDSVTIN 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 303 TEFTATF-------DSGTAVtwLIEPYYTALTTNFHLSVpdrrlSKSVDSPFEfcyiiTSTSDEDKLPSVSFEMkGGAAY 375
Cdd:cd05478  198 GQVVACSggcqaivDTGTSL--LVGPSSDIANIQSDIGA-----SQNQNGEMV-----VNCSSISSMPDVVFTI-NGVQY 264
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 257723128 376 DVfSPILVFDTSDGSfqvyCLAVLKQVNA-DFSIIGQNFMTNYRIVHDRERRILG 429
Cdd:cd05478  265 PL-PPSAYILQDQGS----CTSGFQSMGLgELWILGDVFIRQYYSVFDRANNKVG 314
pepsin_retropepsin_like cd05470
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
92-230 8.16e-07

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: 47.37  E-value: 8.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  92 NVTIGTPAQWFLVALDTGSDLFWLPCN----CNSTCVRSMETDQGERiklniynpskskssskvtcnstlCALRNRcisp 167
Cdd:cd05470    2 EIGIGTPPQTFNVLLDTGSSNLWVPSVdcqsLAIYSHSSYDDPSASS-----------------------TYSDNG---- 54
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 257723128 168 vsdCPYRIRYlsPGSKSTGVLVEDVIHMSTEEgearDARITFGCSESQLGLFKEVA-VNGIMGL 230
Cdd:cd05470   55 ---CTFSITY--GTGSLSGGLSTDTVSIGDIE----VVGQAFGCATDEPGATFLPAlFDGILGL 109
Proteinase_A_fungi cd05488
Fungal Proteinase A , aspartic proteinase superfamily; Fungal Proteinase A, a proteolytic ...
89-315 2.51e-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: 46.28  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLPcncnstcvrsmetdqgeriklniynpsksksssKVTCNSTLCALRNRCISPV 168
Cdd:cd05488   11 YFTDITLGTPPQKFKVILDTGSSNLWVP---------------------------------SVKCGSIACFLHSKYDSSA 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 169 SDC------PYRIRYlspGSKS-TGVLVEDVIHMSTEEGEARDaritFGCSESQLGL-FKEVAVNGIMGLAIADIAVP-- 238
Cdd:cd05488   58 SSTykangtEFKIQY---GSGSlEGFVSQDTLSIGDLTIKKQD----FAEATSEPGLaFAFGKFDGILGLAYDTISVNki 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 239 -----NMLVKAGVASDSFSMCFG--PNGKGTISFGDKGSSDqletpLSGTISPM------FYDVSITKFKVGKVTVDTEF 305
Cdd:cd05488  131 vppfyNMINQGLLDEPVFSFYLGssEEDGGEATFGGIDESR-----FTGKITWLpvrrkaYWEVELEKIGLGDEELELEN 205
                        250
                 ....*....|.
gi 257723128 306 T-ATFDSGTAV 315
Cdd:cd05488  206 TgAAIDTGTSL 216
beta_secretase_like cd05473
Beta-secretase, aspartic-acid protease important in the pathogenesis of Alzheimer's disease; ...
225-451 3.06e-04

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: 42.80  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 225 NGIMGLAIADIAVP--------NMLVKAGVASDSFS--MC---FGPNGK------GTISFGDKGSS----DQLETPLsgt 281
Cdd:cd05473  106 EGILGLAYAELARPdssvepffDSLVKQTGIPDVFSlqMCgagLPVNGSasgtvgGSMVIGGIDPSlykgDIWYTPI--- 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 282 ISPMFYDVSITKFKVGKVTVD---TEFT---ATFDSGTAVTWLIEPYYTALTTNFhlsvpdRRLSKSVDSPFEF------ 349
Cdd:cd05473  183 REEWYYEVIILKLEVGGQSLNldcKEYNydkAIVDSGTTNLRLPVKVFNAAVDAI------KAASLIEDFPDGFwlgsql 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 350 -CYIITSTSDEdKLPSVSFEMKGGAAYDVFS----------PILVFDTSDgsfQVYCLAVLKQVNAdfSIIGQNFMTNYR 418
Cdd:cd05473  257 aCWQKGTTPWE-IFPKISIYLRDENSSQSFRitilpqlylrPVEDHGTQL---DCYKFAISQSTNG--TVIGAVIMEGFY 330
                        250       260       270
                 ....*....|....*....|....*....|...
gi 257723128 419 IVHDRERRILGWKKSNCNDTNGFtgPTALAKPP 451
Cdd:cd05473  331 VVFDRANKRVGFAVSTCAEHDGF--RTSEIEGP 361
gastricsin cd05477
Gastricsins, asparate proteases produced in gastric mucosa; Gastricsin is also called ...
89-237 2.48e-03

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: 39.87  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLPcncnstcvrsmetdqgeriklniynpsksksssKVTCNSTLCALRNRcISPV 168
Cdd:cd05477    4 YYGEISIGTPPQNFLVLFDTGSSNLWVP---------------------------------SVLCQSQACTNHTK-FNPS 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257723128 169 SDCPYRIR----YLSPGSKS-TGVLVEDV-----IHMSTEEgeardaritFGCSESQLGL-FKEVAVNGIMGLAIADIAV 237
Cdd:cd05477   50 QSSTYSTNgetfSLQYGSGSlTGIFGYDTvtvqgIIITNQE---------FGLSETEPGTnFVYAQFDGILGLAYPSISA 120
SAP_like cd05474
SAPs, pepsin-like proteinases secreted from pathogens to degrade host proteins; SAPs (Secreted ...
90-116 2.91e-03

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: 39.47  E-value: 2.91e-03
                         10        20
                 ....*....|....*....|....*...
gi 257723128  90 YANVTIGTPAQWFLVALDTGS-DLfWLP 116
Cdd:cd05474    4 SAELSVGTPPQKVTVLLDTGSsDL-WVP 30
renin_like cd05487
Renin stimulates production of angiotensin and thus affects blood pressure; Renin, also known ...
89-124 4.72e-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: 38.99  E-value: 4.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLPC-NCN---STCV 124
Cdd:cd05487    9 YYGEIGIGTPPQTFKVVFDTGSSNLWVPSsKCSplyTACV 48
Cathepsin_D_like cd05485
Cathepsin_D_like, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase ...
89-116 7.86e-03

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: 38.29  E-value: 7.86e-03
                         10        20
                 ....*....|....*....|....*...
gi 257723128  89 HYANVTIGTPAQWFLVALDTGSDLFWLP 116
Cdd:cd05485   12 YYGVITIGTPPQSFKVVFDTGSSNLWVP 39
 
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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