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Conserved domains on  [gi|4503143|ref|NP_001900|]
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cathepsin D preproprotein [Homo sapiens]

Protein Classification

pepsin-like aspartic protease( domain architecture ID 10546413)

pepsin-like (A1 family) peptidase is an aspartic endoprotease that hydrolyzes the peptide bonds of substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cathepsin_D2 cd05490
Cathepsin_D2, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase of ...
73-408 0e+00

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: 692.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   73 NYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLS 152
Cdd:cd05490   1 NYMDAQYYGEIGIGTPPQTFTVVFDTGSSNLWVPSVHCSLLDIACWLHHKYNSSKSSTYVKNGTEFAIQYGSGSLSGYLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  153 QDTVSVPCQsassasalggvKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFY 232
Cdd:cd05490  81 QDTVSIGGL-----------QVEGQLFGEAVKQPGITFIAAKFDGILGMAYPRISVDGVTPVFDNIMAQKLVEQNVFSFY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  233 LSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQ 312
Cdd:cd05490 150 LNRDPDAQPGGELMLGGTDPKYYTGDLHYVNVTRKAYWQIHMDQVDVGSGLTLCKGGCEAIVDTGTSLITGPVEEVRALQ 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  313 KAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGR 392
Cdd:cd05490 230 KAIGAVPLIQGEYMIDCEKIPTLPVISFSLGGKVYPLTGEDYILKVSQRGTTICLSGFMGLDIPPPAGPLWILGDVFIGR 309
                       330
                ....*....|....*.
gi 4503143  393 YYTVFDRDNNRVGFAE 408
Cdd:cd05490 310 YYTVFDRDNDRVGFAK 325
A1_Propeptide pfam07966
A1 Propeptide; Most eukaryotic endopeptidases (Merops Family A1) are synthesized with signal ...
23-49 2.97e-05

A1 Propeptide; Most eukaryotic endopeptidases (Merops Family A1) are synthesized with signal and propeptides. The animal pepsin-like endopeptidase propeptides form a distinct family of propeptides, which contain a conserved motif approximately 30 residues long. In pepsinogen A, the first 11 residues of the mature pepsin sequence are displaced by residues of the propeptide. The propeptide contains two helices that block the active site cleft, in particular the conserved Asp11 residue, in pepsin, hydrogen bonds to a conserved Arg residues in the propeptide. This hydrogen bond stabilizes the propeptide conformation and is probably responsible for triggering the conversion of pepsinogen to pepsin under acidic conditions.


:

Pssm-ID: 462326  Cd Length: 27  Bit Score: 40.40  E-value: 2.97e-05
                          10        20
                  ....*....|....*....|....*..
gi 4503143     23 RIPLHKFTSIRRTMSEvGGSVEDLIAK 49
Cdd:pfam07966   1 RIPLKKGKSIRETLRE-KGLLEEFLKE 26
 
Name Accession Description Interval E-value
Cathepsin_D2 cd05490
Cathepsin_D2, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase of ...
73-408 0e+00

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: 692.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   73 NYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLS 152
Cdd:cd05490   1 NYMDAQYYGEIGIGTPPQTFTVVFDTGSSNLWVPSVHCSLLDIACWLHHKYNSSKSSTYVKNGTEFAIQYGSGSLSGYLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  153 QDTVSVPCQsassasalggvKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFY 232
Cdd:cd05490  81 QDTVSIGGL-----------QVEGQLFGEAVKQPGITFIAAKFDGILGMAYPRISVDGVTPVFDNIMAQKLVEQNVFSFY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  233 LSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQ 312
Cdd:cd05490 150 LNRDPDAQPGGELMLGGTDPKYYTGDLHYVNVTRKAYWQIHMDQVDVGSGLTLCKGGCEAIVDTGTSLITGPVEEVRALQ 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  313 KAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGR 392
Cdd:cd05490 230 KAIGAVPLIQGEYMIDCEKIPTLPVISFSLGGKVYPLTGEDYILKVSQRGTTICLSGFMGLDIPPPAGPLWILGDVFIGR 309
                       330
                ....*....|....*.
gi 4503143  393 YYTVFDRDNNRVGFAE 408
Cdd:cd05490 310 YYTVFDRDNDRVGFAK 325
Asp pfam00026
Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and ...
78-409 2.32e-153

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: 435.94  E-value: 2.32e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143     78 QYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLlDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVS 157
Cdd:pfam00026   1 EYFGTISIGTPPQKFTVIFDTGSSDLWVPSSYCTK-SSACKSHGTFDPSSSSTYKLNGTTFSISYGDGSASGFLGQDTVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    158 VpcqsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDp 237
Cdd:pfam00026  80 V-----------GGLTITNQEFGLATKEPGSFFEYAKFDGILGLGFPSISAVGATPVFDNLKSQGLIDSPAFSVYLNSP- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    238 dAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGA 317
Cdd:pfam00026 148 -DAAGGEIIFGGVDPSKYTGSLTYVPVTSQGYWQITLDSVTVGGSTSACSSGCQAILDTGTSLLYGPTSIVSKIAKAVGA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    318 VPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTlCLSGFMgmdiPPPSGPLWILGDVFIGRYYTVF 397
Cdd:pfam00026 227 SSSEYGEYVVDCDSISTLPDITFVIGGAKITVPPSAYVLQNSQGGST-CLSGFQ----PPPGGPLWILGDVFLRSAYVVF 301
                         330
                  ....*....|..
gi 4503143    398 DRDNNRVGFAEA 409
Cdd:pfam00026 302 DRDNNRIGFAPA 313
PTZ00165 PTZ00165
aspartyl protease; Provisional
24-410 3.48e-84

aspartyl protease; Provisional


Pssm-ID: 240300 [Multi-domain]  Cd Length: 482  Bit Score: 265.47  E-value: 3.48e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    24 IPLHKFTSI--RRTMSEVGGSVEDLIAKgpvSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSS 101
Cdd:PTZ00165  67 VELHRFALLkkKRKKNSEKGYISRVLTK---HKYLETKDPNGLQYLQQDLLNFHNSQYFGEIQVGTPPKSFVVVFDTGSS 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   102 NLWVPSIHCKllDIACWIHHKYNSDKSSTYVKNGTSFD-----IHYGSGSLSGYLSQDTVSvpcqsassasaLGGVKVER 176
Cdd:PTZ00165 144 NLWIPSKECK--SGGCAPHRKFDPKKSSTYTKLKLGDEsaetyIQYGTGECVLALGKDTVK-----------IGGLKVKH 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   177 QVFGEATKQPGITFIAAKFDGILGMAYP---RISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDaQPgGELMLGGTDSK 253
Cdd:PTZ00165 211 QSIGLAIEESLHPFADLPFDGLVGLGFPdkdFKESKKALPIVDNIKKQNLLKRNIFSFYMSKDLN-QP-GSISFGSADPK 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   254 Y-YKG-SLSYLNVTRKAYWQVHLDQVEVA-SGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGavplIQGEymipCE 330
Cdd:PTZ00165 289 YtLEGhKIWWFPVISTDYWEIEVVDILIDgKSLGFCDRKCKAAIDTGSSLITGPSSVINPLLEKIP----LEED----CS 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   331 KVSTLPAITLKL---GGK--GYKLSPEDYTLK--VSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNR 403
Cdd:PTZ00165 361 NKDSLPRISFVLedvNGRkiKFDMDPEDYVIEegDSEEQEHQCVIGIIPMDVPAPRGPLFVLGNNFIRKYYSIFDRDHMM 440

                 ....*..
gi 4503143   404 VGFAEAA 410
Cdd:PTZ00165 441 VGLVPAK 447
A1_Propeptide pfam07966
A1 Propeptide; Most eukaryotic endopeptidases (Merops Family A1) are synthesized with signal ...
23-49 2.97e-05

A1 Propeptide; Most eukaryotic endopeptidases (Merops Family A1) are synthesized with signal and propeptides. The animal pepsin-like endopeptidase propeptides form a distinct family of propeptides, which contain a conserved motif approximately 30 residues long. In pepsinogen A, the first 11 residues of the mature pepsin sequence are displaced by residues of the propeptide. The propeptide contains two helices that block the active site cleft, in particular the conserved Asp11 residue, in pepsin, hydrogen bonds to a conserved Arg residues in the propeptide. This hydrogen bond stabilizes the propeptide conformation and is probably responsible for triggering the conversion of pepsinogen to pepsin under acidic conditions.


Pssm-ID: 462326  Cd Length: 27  Bit Score: 40.40  E-value: 2.97e-05
                          10        20
                  ....*....|....*....|....*..
gi 4503143     23 RIPLHKFTSIRRTMSEvGGSVEDLIAK 49
Cdd:pfam07966   1 RIPLKKGKSIRETLRE-KGLLEEFLKE 26
 
Name Accession Description Interval E-value
Cathepsin_D2 cd05490
Cathepsin_D2, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase of ...
73-408 0e+00

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: 692.69  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   73 NYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLS 152
Cdd:cd05490   1 NYMDAQYYGEIGIGTPPQTFTVVFDTGSSNLWVPSVHCSLLDIACWLHHKYNSSKSSTYVKNGTEFAIQYGSGSLSGYLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  153 QDTVSVPCQsassasalggvKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFY 232
Cdd:cd05490  81 QDTVSIGGL-----------QVEGQLFGEAVKQPGITFIAAKFDGILGMAYPRISVDGVTPVFDNIMAQKLVEQNVFSFY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  233 LSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQ 312
Cdd:cd05490 150 LNRDPDAQPGGELMLGGTDPKYYTGDLHYVNVTRKAYWQIHMDQVDVGSGLTLCKGGCEAIVDTGTSLITGPVEEVRALQ 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  313 KAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGR 392
Cdd:cd05490 230 KAIGAVPLIQGEYMIDCEKIPTLPVISFSLGGKVYPLTGEDYILKVSQRGTTICLSGFMGLDIPPPAGPLWILGDVFIGR 309
                       330
                ....*....|....*.
gi 4503143  393 YYTVFDRDNNRVGFAE 408
Cdd:cd05490 310 YYTVFDRDNDRVGFAK 325
Cathepsin_D_like cd05485
Cathepsin_D_like, pepsin family of proteinases; Cathepsin D is the major aspartic proteinase ...
68-408 0e+00

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: 508.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   68 PEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSL 147
Cdd:cd05485   1 PEPLSNYMDAQYYGVITIGTPPQSFKVVFDTGSSNLWVPSKKCSWTNIACLLHNKYDSTKSSTYKKNGTEFAIQYGSGSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  148 SGYLSQDTVSVpcqsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQN 227
Cdd:cd05485  81 SGFLSTDTVSV-----------GGVSVKGQTFAEAINEPGLTFVAAKFDGILGMGYSSISVDGVVPVFYNMVNQKLVDAP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  228 IFSFYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGlTLCKEGCEAIVDTGTSLMVGPVDE 307
Cdd:cd05485 150 VFSFYLNRDPSAKEGGELILGGSDPKHYTGNFTYLPVTRKGYWQFKMDSVSVGEG-EFCSGGCQAIADTGTSLIAGPVDE 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  308 VRELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGD 387
Cdd:cd05485 229 IEKLNNAIGAKPIIGGEYMVNCSAIPSLPDITFVLGGKSFSLTGKDYVLKVTQMGQTICLSGFMGIDIPPPAGPLWILGD 308
                       330       340
                ....*....|....*....|.
gi 4503143  388 VFIGRYYTVFDRDNNRVGFAE 408
Cdd:cd05485 309 VFIGKYYTEFDLGNNRVGFAT 329
phytepsin cd06098
Phytepsin, a plant homolog of mammalian lysosomal pepsins; Phytepsin, a plant homolog of ...
71-408 4.16e-161

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: 455.68  E-value: 4.16e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   71 LKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCkLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGY 150
Cdd:cd06098   3 LKNYLDAQYFGEIGIGTPPQKFTVIFDTGSSNLWVPSSKC-YFSIACYFHSKYKSSKSSTYKKNGTSASIQYGTGSISGF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  151 LSQDTVSVpcqsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFS 230
Cdd:cd06098  82 FSQDSVTV-----------GDLVVKNQVFIEATKEPGLTFLLAKFDGILGLGFQEISVGKAVPVWYNMVEQGLVKEPVFS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  231 FYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLT-LCKEGCEAIVDTGTSLMVGPVDEVR 309
Cdd:cd06098 151 FWLNRNPDEEEGGELVFGGVDPKHFKGEHTYVPVTRKGYWQFEMGDVLIGGKSTgFCAGGCAAIADSGTSLLAGPTTIVT 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  310 ELQKAIGavpliqgeymipCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVF 389
Cdd:cd06098 231 QINSAVD------------CNSLSSMPNVSFTIGGKTFELTPEQYILKVGEGAAAQCISGFTALDVPPPRGPLWILGDVF 298
                       330
                ....*....|....*....
gi 4503143  390 IGRYYTVFDRDNNRVGFAE 408
Cdd:cd06098 299 MGAYHTVFDYGNLRVGFAE 317
Asp pfam00026
Eukaryotic aspartyl protease; Aspartyl (acid) proteases include pepsins, cathepsins, and ...
78-409 2.32e-153

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: 435.94  E-value: 2.32e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143     78 QYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLlDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVS 157
Cdd:pfam00026   1 EYFGTISIGTPPQKFTVIFDTGSSDLWVPSSYCTK-SSACKSHGTFDPSSSSTYKLNGTTFSISYGDGSASGFLGQDTVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    158 VpcqsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDp 237
Cdd:pfam00026  80 V-----------GGLTITNQEFGLATKEPGSFFEYAKFDGILGLGFPSISAVGATPVFDNLKSQGLIDSPAFSVYLNSP- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    238 dAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGA 317
Cdd:pfam00026 148 -DAAGGEIIFGGVDPSKYTGSLTYVPVTSQGYWQITLDSVTVGGSTSACSSGCQAILDTGTSLLYGPTSIVSKIAKAVGA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    318 VPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTlCLSGFMgmdiPPPSGPLWILGDVFIGRYYTVF 397
Cdd:pfam00026 227 SSSEYGEYVVDCDSISTLPDITFVIGGAKITVPPSAYVLQNSQGGST-CLSGFQ----PPPGGPLWILGDVFLRSAYVVF 301
                         330
                  ....*....|..
gi 4503143    398 DRDNNRVGFAEA 409
Cdd:pfam00026 302 DRDNNRIGFAPA 313
renin_like cd05487
Renin stimulates production of angiotensin and thus affects blood pressure; Renin, also known ...
71-409 2.96e-152

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: 433.82  E-value: 2.96e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   71 LKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGY 150
Cdd:cd05487   1 LTNYLDTQYYGEIGIGTPPQTFKVVFDTGSSNLWVPSSKCSPLYTACVTHNLYDASDSSTYKENGTEFTIHYASGTVKGF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  151 LSQDTVSVpcqsassasalGGVKVErQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFS 230
Cdd:cd05487  81 LSQDIVTV-----------GGIPVT-QMFGEVTALPAIPFMLAKFDGVLGMGYPKQAIGGVTPVFDNIMSQGVLKEDVFS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  231 FYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRE 310
Cdd:cd05487 149 VYYSRDSSHSLGGEIVLGGSDPQHYQGDFHYINTSKTGFWQIQMKGVSVGSSTLLCEDGCTAVVDTGASFISGPTSSISK 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  311 LQKAIGAVpLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFI 390
Cdd:cd05487 229 LMEALGAK-ERLGDYVVKCNEVPTLPDISFHLGGKEYTLSSSDYVLQDSDFSDKLCTVAFHAMDIPPPTGPLWVLGATFI 307
                       330
                ....*....|....*....
gi 4503143  391 GRYYTVFDRDNNRVGFAEA 409
Cdd:cd05487 308 RKFYTEFDRQNNRIGFALA 326
pepsin_A cd05478
Pepsin A, aspartic protease produced in gastric mucosa of mammals; Pepsin, a well-known ...
69-407 3.03e-139

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: 400.28  E-value: 3.03e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   69 EVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLdiACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLS 148
Cdd:cd05478   1 EPLTNYLDMEYYGTISIGTPPQDFTVIFDTGSSNLWVPSVYCSSQ--ACSNHNRFNPRQSSTYQSTGQPLSIQYGTGSMT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  149 GYLSQDTVSVpcqsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNI 228
Cdd:cd05478  79 GILGYDTVQV-----------GGISDTNQIFGLSETEPGSFFYYAPFDGILGLAYPSIASSGATPVFDNMMSQGLVSQDL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  229 FSFYLSRDPdaQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEV 308
Cdd:cd05478 148 FSVYLSSNG--QQGSVVTFGGIDPSYYTGSLNWVPVTAETYWQITVDSVTINGQVVACSGGCQAIVDTGTSLLVGPSSDI 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  309 RELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKvSQAGktlCLSGFMGMDIpppsGPLWILGDV 388
Cdd:cd05478 226 ANIQSDIGASQNQNGEMVVNCSSISSMPDVVFTINGVQYPLPPSAYILQ-DQGS---CTSGFQSMGL----GELWILGDV 297
                       330
                ....*....|....*....
gi 4503143  389 FIGRYYTVFDRDNNRVGFA 407
Cdd:cd05478 298 FIRQYYSVFDRANNKVGLA 316
Cathespin_E cd05486
Cathepsin E, non-lysosomal aspartic protease; Cathepsin E is an intracellular, non-lysosomal ...
79-407 2.29e-134

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: 387.70  E-value: 2.29e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   79 YYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCklLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSV 158
Cdd:cd05486   1 YFGQISIGTPPQNFTVIFDTGSSNLWVPSIYC--TSQACTKHNRFQPSESSTYVSNGEAFSIQYGTGSLTGIIGIDQVTV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  159 PcqsassasalgGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPD 238
Cdd:cd05486  79 E-----------GITVQNQQFAESVSEPGSTFQDSEFDGILGLAYPSLAVDGVTPVFDNMMAQNLVELPMFSVYMSRNPN 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  239 AQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGAV 318
Cdd:cd05486 148 SADGGELVFGGFDTSRFSGQLNWVPVTVQGYWQIQLDNIQVGGTVIFCSDGCQAIVDTGTSLITGPSGDIKQLQNYIGAT 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  319 PlIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFD 398
Cdd:cd05486 228 A-TDGEYGVDCSTLSLMPSVTFTINGIPYSLSPQAYTLEDQSDGGGYCSSGFQGLDIPPPAGPLWILGDVFIRQYYSVFD 306

                ....*....
gi 4503143  399 RDNNRVGFA 407
Cdd:cd05486 307 RGNNRVGFA 315
Proteinase_A_fungi cd05488
Fungal Proteinase A , aspartic proteinase superfamily; Fungal Proteinase A, a proteolytic ...
71-408 1.38e-133

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: 386.02  E-value: 1.38e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   71 LKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKllDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGY 150
Cdd:cd05488   3 LTNYLNAQYFTDITLGTPPQKFKVILDTGSSNLWVPSVKCG--SIACFLHSKYDSSASSTYKANGTEFKIQYGSGSLEGF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  151 LSQDTVSVpcqsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFS 230
Cdd:cd05488  81 VSQDTLSI-----------GDLTIKKQDFAEATSEPGLAFAFGKFDGILGLAYDTISVNKIVPPFYNMINQGLLDEPVFS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  231 FYL-SRDPDaqpGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEVASGlTLCKEGCEAIVDTGTSLMVGPVDEVR 309
Cdd:cd05488 150 FYLgSSEED---GGEATFGGIDESRFTGKITWLPVRRKAYWEVELEKIGLGDE-ELELENTGAAIDTGTSLIALPSDLAE 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  310 ELQKAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQAgktlCLSGFMGMDIPPPSGPLWILGDVF 389
Cdd:cd05488 226 MLNAEIGAKKSWNGQYTVDCSKVDSLPDLTFNFDGYNFTLGPFDYTLEVSGS----CISAFTGMDFPEPVGPLAIVGDAF 301
                       330
                ....*....|....*....
gi 4503143  390 IGRYYTVFDRDNNRVGFAE 408
Cdd:cd05488 302 LRKYYSVYDLGNNAVGLAK 320
pepsin_like cd05471
Pepsin-like aspartic proteases, bilobal enzymes that cleave bonds in peptides at acidic pH; ...
79-407 9.27e-110

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: 323.99  E-value: 9.27e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   79 YYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSV 158
Cdd:cd05471   1 YYGEITIGTPPQKFSVIFDTGSSLLWVPSSNCTSCSCQKHPRFKYDSSKSSTYKDTGCTFSITYGDGSVTGGLGTDTVTI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  159 pcqsassasalGGVKVERQVFGEATKQPGiTFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPD 238
Cdd:cd05471  81 -----------GGLTIPNQTFGCATSESG-DFSSSGFDGILGLGFPSLSVDGVPSFFDQLKSQGLISSPVFSFYLGRDGD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  239 AQPGGELMLGGTDSKYYKGSLSYLNVT--RKAYWQVHLDQVEVAS-GLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAI 315
Cdd:cd05471 149 GGNGGELTFGGIDPSKYTGDLTYTPVVsnGPGYWQVPLDGISVGGkSVISSSGGGGAIVDSGTSLIYLPSSVYDAILKAL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  316 GA-VPLIQGEYMIPCEKVSTLPAITLKLggkgyklspedytlkvsqagktlclsgfmgmdipppsgpLWILGDVFIGRYY 394
Cdd:cd05471 229 GAaVSSSDGGYGVDCSPCDTLPDITFTF---------------------------------------LWILGDVFLRNYY 269
                       330
                ....*....|...
gi 4503143  395 TVFDRDNNRVGFA 407
Cdd:cd05471 270 TVFDLDNNRIGFA 282
gastricsin cd05477
Gastricsins, asparate proteases produced in gastric mucosa; Gastricsin is also called ...
76-409 1.47e-102

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: 306.81  E-value: 1.47e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   76 DAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKllDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDT 155
Cdd:cd05477   1 DMSYYGEISIGTPPQNFLVLFDTGSSNLWVPSVLCQ--SQACTNHTKFNPSQSSTYSTNGETFSLQYGSGSLTGIFGYDT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  156 VSVpcqsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNIFSFYLSR 235
Cdd:cd05477  79 VTV-----------QGIIITNQEFGLSETEPGTNFVYAQFDGILGLAYPSISAGGATTVMQGMMQQNLLQAPIFSFYLSG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  236 DpDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEV---ASGltLCKEGCEAIVDTGTSLMVGPVDEVRELQ 312
Cdd:cd05477 148 Q-QGQQGGELVFGGVDNNLYTGQIYWTPVTSETYWQIGIQGFQIngqATG--WCSQGCQAIVDTGTSLLTAPQQVMSTLM 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  313 KAIGAVPLIQGEYMIPCEKVSTLPAITLKLGGKGYKLSPEDYTLKVSQagktLCLSGFMGMDIPPPSG-PLWILGDVFIG 391
Cdd:cd05477 225 QSIGAQQDQYGQYVVNCNNIQNLPTLTFTINGVSFPLPPSAYILQNNG----YCTVGIEPTYLPSQNGqPLWILGDVFLR 300
                       330
                ....*....|....*...
gi 4503143  392 RYYTVFDRDNNRVGFAEA 409
Cdd:cd05477 301 QYYSVYDLGNNQVGFATA 318
PTZ00165 PTZ00165
aspartyl protease; Provisional
24-410 3.48e-84

aspartyl protease; Provisional


Pssm-ID: 240300 [Multi-domain]  Cd Length: 482  Bit Score: 265.47  E-value: 3.48e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    24 IPLHKFTSI--RRTMSEVGGSVEDLIAKgpvSKYSQAVPAVTEGPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSS 101
Cdd:PTZ00165  67 VELHRFALLkkKRKKNSEKGYISRVLTK---HKYLETKDPNGLQYLQQDLLNFHNSQYFGEIQVGTPPKSFVVVFDTGSS 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   102 NLWVPSIHCKllDIACWIHHKYNSDKSSTYVKNGTSFD-----IHYGSGSLSGYLSQDTVSvpcqsassasaLGGVKVER 176
Cdd:PTZ00165 144 NLWIPSKECK--SGGCAPHRKFDPKKSSTYTKLKLGDEsaetyIQYGTGECVLALGKDTVK-----------IGGLKVKH 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   177 QVFGEATKQPGITFIAAKFDGILGMAYP---RISVNNVLPVFDNLMQQKLVDQNIFSFYLSRDPDaQPgGELMLGGTDSK 253
Cdd:PTZ00165 211 QSIGLAIEESLHPFADLPFDGLVGLGFPdkdFKESKKALPIVDNIKKQNLLKRNIFSFYMSKDLN-QP-GSISFGSADPK 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   254 Y-YKG-SLSYLNVTRKAYWQVHLDQVEVA-SGLTLCKEGCEAIVDTGTSLMVGPVDEVRELQKAIGavplIQGEymipCE 330
Cdd:PTZ00165 289 YtLEGhKIWWFPVISTDYWEIEVVDILIDgKSLGFCDRKCKAAIDTGSSLITGPSSVINPLLEKIP----LEED----CS 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   331 KVSTLPAITLKL---GGK--GYKLSPEDYTLK--VSQAGKTLCLSGFMGMDIPPPSGPLWILGDVFIGRYYTVFDRDNNR 403
Cdd:PTZ00165 361 NKDSLPRISFVLedvNGRkiKFDMDPEDYVIEegDSEEQEHQCVIGIIPMDVPAPRGPLFVLGNNFIRKYYSIFDRDHMM 440

                 ....*..
gi 4503143   404 VGFAEAA 410
Cdd:PTZ00165 441 VGLVPAK 447
PTZ00147 PTZ00147
plasmepsin-1; Provisional
71-411 9.79e-61

plasmepsin-1; Provisional


Pssm-ID: 140176 [Multi-domain]  Cd Length: 453  Bit Score: 203.56  E-value: 9.79e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    71 LKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKllDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGY 150
Cdd:PTZ00147 132 LKDLANVMSYGEAKLGDNGQKFNFIFDTGSANLWVPSIKCT--TEGCETKNLYDSSKSKTYEKDGTKVEMNYVSGTVSGF 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   151 LSQDTVSVpcqsassasalGGVKVERQvFGEATKQPGI--TFIAAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNI 228
Cdd:PTZ00147 210 FSKDLVTI-----------GNLSVPYK-FIEVTDTNGFepFYTESDFDGIFGLGWKDLSIGSVDPYVVELKNQNKIEQAV 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   229 FSFYLSrdPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDqVEVASgLTLCKEGCeaIVDTGTSLMVGPVDEV 308
Cdd:PTZ00147 278 FTFYLP--PEDKHKGYLTIGGIEERFYEGPLTYEKLNHDLYWQVDLD-VHFGN-VSSEKANV--IVDSGTSVITVPTEFL 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   309 RELQKAIGA--VPLIQgEYMIPCEKvSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSgplWILG 386
Cdd:PTZ00147 352 NKFVESLDVfkVPFLP-LYVTTCNN-TKLPTLEFRSPNKVYTLEPEYYLQPIEDIGSALCMLNIIPIDLEKNT---FILG 426
                        330       340
                 ....*....|....*....|....*
gi 4503143   387 DVFIGRYYTVFDRDNNRVGFAEAAR 411
Cdd:PTZ00147 427 DPFMRKYFTVFDYDNHTVGFALAKK 451
PTZ00013 PTZ00013
plasmepsin 4 (PM4); Provisional
71-409 5.89e-59

plasmepsin 4 (PM4); Provisional


Pssm-ID: 140051 [Multi-domain]  Cd Length: 450  Bit Score: 198.67  E-value: 5.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    71 LKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKllDIACWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGY 150
Cdd:PTZ00013 131 LDDVANIMFYGEGEVGDNHQKFMLIFDTGSANLWVPSKKCD--SIGCSIKNLYDSSKSKSYEKDGTKVDITYGSGTVKGF 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   151 LSQDTVSvpcqsassasaLGGVKVERQvFGEATKQPGITFI--AAKFDGILGMAYPRISVNNVLPVFDNLMQQKLVDQNI 228
Cdd:PTZ00013 209 FSKDLVT-----------LGHLSMPYK-FIEVTDTDDLEPIysSSEFDGILGLGWKDLSIGSIDPIVVELKNQNKIDNAL 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   229 FSFYLS-RDPDAqpgGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDqveVASGlTLCKEGCEAIVDTGTSLMVGPVDE 307
Cdd:PTZ00013 277 FTFYLPvHDVHA---GYLTIGGIEEKFYEGNITYEKLNHDLYWQIDLD---VHFG-KQTMQKANVIVDSGTTTITAPSEF 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   308 VRELQKAIGA--VPLIQgEYMIPCEKvSTLPAITLKLGGKGYKLSPEDYTLKVSQAGKTLCLSGFMGMDIPPPSgplWIL 385
Cdd:PTZ00013 350 LNKFFANLNVikVPFLP-FYVTTCDN-KEMPTLEFKSANNTYTLEPEYYMNPLLDVDDTLCMITMLPVDIDDNT---FIL 424
                        330       340
                 ....*....|....*....|....
gi 4503143   386 GDVFIGRYYTVFDRDNNRVGFAEA 409
Cdd:PTZ00013 425 GDPFMRKYFTVFDYDKESVGFAIA 448
Aspergillopepsin_like cd06097
Aspergillopepsin_like, aspartic proteases of fungal origin; The members of this family are ...
79-407 1.08e-46

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: 161.31  E-value: 1.08e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   79 YYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIAcwIHHKYNSDKSSTY-VKNGTSFDIHYGSGS-LSGYLSQDTV 156
Cdd:cd06097   1 YLTPVKIGTPPQTLNLDLDTGSSDLWVFSSETPAAQQG--GHKLYDPSKSSTAkLLPGATWSISYGDGSsASGIVYTDTV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  157 SVpcqsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGMAYPRIsvNNVLPV-----FDNLMQQKlvDQNIFSF 231
Cdd:cd06097  79 SI-----------GGVEVPNQAIELATAVSASFFSDTASDGLLGLAFSSI--NTVQPPkqktfFENALSSL--DAPLFTA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  232 YLSRDPDaqpgGELMLGGTDSKYYKGSLSYLNVTR-KAYWQVHLDQVEVASGLTLCKEGCEAIVDTGTSLMVGPVDEVRE 310
Cdd:cd06097 144 DLRKAAP----GFYTFGYIDESKYKGEISWTPVDNsSGFWQFTSTSYTVGGDAPWSRSGFSAIADTGTTLILLPDAIVEA 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  311 LQKAI-GAV--PLIQGeYMIPCEkvSTLPaitlklggkgyklspeDYTLKVSQagktlclsgfmgmdipppsgplwILGD 387
Cdd:cd06097 220 YYSQVpGAYydSEYGG-WVFPCD--TTLP----------------DLSFAVFS-----------------------ILGD 257
                       330       340
                ....*....|....*....|
gi 4503143  388 VFIGRYYTVFDRDNNRVGFA 407
Cdd:cd06097 258 VFLKAQYVVFDVGGPKLGFA 277
beta_secretase_like cd05473
Beta-secretase, aspartic-acid protease important in the pathogenesis of Alzheimer's disease; ...
79-407 4.35e-40

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: 146.41  E-value: 4.35e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   79 YYGEIGIGTPPQCFTVVFDTGSSNLWVP-SIHCklldiacWIHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVS 157
Cdd:cd05473   4 YYIEMLIGTPPQKLNILVDTGSSNFAVAaAPHP-------FIHTYFHRELSSTYRDLGKGVTVPYTQGSWEGELGTDLVS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  158 VPCqsassasalgGVKVERQVFGEATKQPGITFI-AAKFDGILGMAYPRISV--NNVLPVFDNLMQQKLVdQNIFS---- 230
Cdd:cd05473  77 IPK----------GPNVTFRANIAAITESENFFLnGSNWEGILGLAYAELARpdSSVEPFFDSLVKQTGI-PDVFSlqmc 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  231 ---FYLSRDPDAQPGGELMLGGTDSKYYKGSLSYLNVTRKAYWQVHLDQVEV-ASGLTL-CKE--GCEAIVDTGTSLMVG 303
Cdd:cd05473 146 gagLPVNGSASGTVGGSMVIGGIDPSLYKGDIWYTPIREEWYYEVIILKLEVgGQSLNLdCKEynYDKAIVDSGTTNLRL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  304 PVDEVRELQKAIGAVPLIQ--------GEYMIPCEKVST----LPAITLKL----GGKGYKLS--PEDYTLKVSQAGKTL 365
Cdd:cd05473 226 PVKVFNAAVDAIKAASLIEdfpdgfwlGSQLACWQKGTTpweiFPKISIYLrdenSSQSFRITilPQLYLRPVEDHGTQL 305
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 4503143  366 CLSGFMgmdIPPPSGPLwILGDVFIGRYYTVFDRDNNRVGFA 407
Cdd:cd05473 306 DCYKFA---ISQSTNGT-VIGAVIMEGFYVVFDRANKRVGFA 343
SAP_like cd05474
SAPs, pepsin-like proteinases secreted from pathogens to degrade host proteins; SAPs (Secreted ...
79-409 7.28e-40

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: 143.86  E-value: 7.28e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   79 YYGEIGIGTPPQCFTVVFDTGSSNLWVPsihcklldiacwihhkynsdksstyvkngtSFDIHYGSGS-LSGYLSQDTVS 157
Cdd:cd05474   3 YSAELSVGTPPQKVTVLLDTGSSDLWVP------------------------------DFSISYGDGTsASGTWGTDTVS 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  158 vpcqsassasaLGGVKVERQVFGEATKQPGITfiaakfdGILGMAYPRI-SVNNVLPVFDN----LMQQKLVDQNIFSFY 232
Cdd:cd05474  53 -----------IGGATVKNLQFAVANSTSSDV-------GVLGIGLPGNeATYGTGYTYPNfpiaLKKQGLIKKNAYSLY 114
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  233 LSrDPDAQpGGELMLGGTDSKYYKGSLSYLNVTRKAYW------QVHLDQVEVASGL---TLCKEGCEAIVDTGTSLMVG 303
Cdd:cd05474 115 LN-DLDAS-TGSILFGGVDTAKYSGDLVTLPIVNDNGGsepselSVTLSSISVNGSSgntTLLSKNLPALLDSGTTLTYL 192
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  304 PVDEVRELQKAIGAVpLIQGE--YMIPCEKVSTLPaITLKLGGKGYKLSPEDYTLKVS--QAGKTLCLSGFMgmdipPPS 379
Cdd:cd05474 193 PSDIVDAIAKQLGAT-YDSDEglYVVDCDAKDDGS-LTFNFGGATISVPLSDLVLPAStdDGGDGACYLGIQ-----PST 265
                       330       340       350
                ....*....|....*....|....*....|
gi 4503143  380 GPLWILGDVFIGRYYTVFDRDNNRVGFAEA 409
Cdd:cd05474 266 SDYNILGDTFLRSAYVVYDLDNNEISLAQA 295
pepsin_retropepsin_like cd05470
Cellular and retroviral pepsin-like aspartate proteases; This family includes both cellular ...
81-201 8.66e-40

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: 137.90  E-value: 8.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   81 GEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWiHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVpc 160
Cdd:cd05470   1 IEIGIGTPPQTFNVLLDTGSSNLWVPSVDCQSLAIYSH-SSYDDPSASSTYSDNGCTFSITYGTGSLSGGLSTDTVSI-- 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 4503143  161 qsassasalGGVKVERQVFGEATKQPGITFIAAKFDGILGM 201
Cdd:cd05470  78 ---------GDIEVVGQAFGCATDEPGATFLPALFDGILGL 109
Plasmepsin_5 cd06096
Plasmepsins are a class of aspartic proteinases produced by the plasmodium parasite; The ...
77-409 1.56e-27

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: 111.32  E-value: 1.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   77 AQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKlldiACWIHHK--YNSDKSSTY----------------VKNGTSF 138
Cdd:cd06096   2 AYYFIDIFIGNPPQKQSLILDTGSSSLSFPCSQCK----NCGIHMEppYNLNNSITSsilycdcnkccyclscLNNKCEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  139 DIHYGSGS-LSGYLSQDTVSVPcqsaSSASALGGVKVERQVFGEATKQPGItFIAAKFDGILGMAYpriSVNNVLPVF-D 216
Cdd:cd06096  78 SISYSEGSsISGFYFSDFVSFE----SYLNSNSEKESFKKIFGCHTHETNL-FLTQQATGILGLSL---TKNNGLPTPiI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  217 NLMQQKLVDQN--IFSFYLSRDpdaqpGGELMLGGTDSKYYKGSLSYLN----------VTRKAYWQVHLDQVEVASGLT 284
Cdd:cd06096 150 LLFTKRPKLKKdkIFSICLSED-----GGELTIGGYDKDYTVRNSSIGNnkvskivwtpITRKYYYYVKLEGLSVYGTTS 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  285 LC--KEGCEAIVDTGTSLMVGPvdevRELQKAIgavpliqgeymipcekVSTLPAITLKLGGkGYKL--SPEDY-TLKVS 359
Cdd:cd06096 225 NSgnTKGLGMLVDSGSTLSHFP----EDLYNKI----------------NNFFPTITIIFEN-NLKIdwKPSSYlYKKES 283
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 4503143  360 QAGKTLCLSGFMGMdipppsgplwILGDVFIGRYYTVFDRDNNRVGFAEA 409
Cdd:cd06096 284 FWCKGGEKSVSNKP----------ILGASFFKNKQIIFDLDNNRIGFVES 323
pepsin_A_like_plant cd05476
Chroloplast Nucleoids DNA-binding Protease and Nucellin, pepsin-like aspartic proteases from ...
78-409 6.11e-19

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: 85.78  E-value: 6.11e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   78 QYYGEIGIGTPPQCFTVVFDTGSSNLWVPsihCklldiaCwihhkynsdksstyvkngtSFDIHYGSGSLS-GYLSQDTV 156
Cdd:cd05476   1 EYLVTLSIGTPPQPFSLIVDTGSDLTWTQ---C------C-------------------SYEYSYGDGSSTsGVLATETF 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  157 SVPcqsaSSASALGGVkverqVFGEATKQPGITFiaAKFDGILGMAYPRISvnnvlpvfdnLMQQKLVDQNIFSFYLSRD 236
Cdd:cd05476  53 TFG----DSSVSVPNV-----AFGCGTDNEGGSF--GGADGILGLGRGPLS----------LVSQLGSTGNKFSYCLVPH 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  237 PDAQPGGELMLGGtDSKYYKGSLSY----LNVTRKAYWQVHLDQVEVASGLTLCKEGCEA---------IVDTGTSL--M 301
Cdd:cd05476 112 DDTGGSSPLILGD-AADLGGSGVVYtplvKNPANPTYYYVNLEGISVGGKRLPIPPSVFAidsdgsggtIIDSGTTLtyL 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  302 VGPVdevrelqkaigavpliqgeymipcekvstLPAITLKLGGKGY-KLSPEDYTlkVSQAGKTLCLsGFMGMDipppSG 380
Cdd:cd05476 191 PDPA-----------------------------YPDLTLHFDGGADlELPPENYF--VDVGEGVVCL-AILSSS----SG 234
                       330       340
                ....*....|....*....|....*....
gi 4503143  381 PLWILGDVFIGRYYTVFDRDNNRVGFAEA 409
Cdd:cd05476 235 GVSILGNIQQQNFLVEYDLENSRLGFAPA 263
TAXi_N pfam14543
Xylanase inhibitor N-terminal; The N- and C-termini of the members of this family are jointly ...
79-249 1.58e-16

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: 76.93  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143     79 YYGEIGIGTPPQCFTVVFDTGSSNLWVPsihCKLLDIACwIHHKYNSDKSSTY--VKNGTS------------------- 137
Cdd:pfam14543   1 YLVTISIGTPPVPFFLVVDTGSDLTWVQ---CDPCCYSQ-PDPLFDPYKSSTYkpVPCSSPlcslialsspgpccsnntc 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143    138 -FDIHYGSGSLS-GYLSQDTVSVPcqsassaSALGGVKVERQVFGEATKQPGitFIAAKFDGILGMAYPRISvnnvlpvf 215
Cdd:pfam14543  77 dYEVSYGDGSSTsGVLATDTLTLN-------STGGSVSVPNFVFGCGYNLLG--GLPAGADGILGLGRGKLS-------- 139
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 4503143    216 dnlmqqkLVDQ--------NIFSFYLSRDPDAqpGGELMLGG 249
Cdd:pfam14543 140 -------LPSQlasqgifgNKFSYCLSSSSSG--SGVLFFGD 172
cnd41_like cd05472
Chloroplast Nucleoids DNA-binding Protease, catalyzes the degradation of ribulose-1, ...
78-410 8.34e-07

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: 50.35  E-value: 8.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   78 QYYGEIGIGTPPQCFTVVFDTGSSNLWVpsiHCKlldiACWIhhkynsdksstyvkngtsFDIHYGSGSLS-GYLSQDTV 156
Cdd:cd05472   1 EYVVTVGLGTPARDQTVIVDTGSDLTWV---QCQ----PCCL------------------YQVSYGDGSYTtGDLATDTL 55
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  157 SVpcqsaSSASALGGVkverqVFGEATKQPGiTFIAAkfDGILGMAYPRIS-VNNVLPVFDnlmqqklvdqNIFSFYL-S 234
Cdd:cd05472  56 TL-----GSSDVVPGF-----AFGCGHDNEG-LFGGA--AGLLGLGRGKLSlPSQTASSYG----------GVFSYCLpD 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  235 RDPDAqpGGELMLGGTDSKyyKGSLSYLNVTRKA----YWQVHLDQVEVASG-LTLCKEGCEA---IVDTGTSLMVGPVD 306
Cdd:cd05472 113 RSSSS--SGYLSFGAAASV--PAGASFTPMLSNPrvptFYYVGLTGISVGGRrLPIPPASFGAggvIIDSGTVITRLPPS 188
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  307 EVRELQKAI----------GAVPLIQGEYMIPCEKVSTLPAITLKL-GGKGYKLSPEDYTLKVSQAGkTLCLsGFMGMDi 375
Cdd:cd05472 189 AYAALRDAFraamaaypraPGFSILDTCYDLSGFRSVSVPTVSLHFqGGADVELDASGVLYPVDDSS-QVCL-AFAGTS- 265
                       330       340       350
                ....*....|....*....|....*....|....*
gi 4503143  376 ppPSGPLWILGDVFIGRYYTVFDRDNNRVGFAEAA 410
Cdd:cd05472 266 --DDGGLSIIGNVQQQTFRVVYDVAGGRIGFAPGG 298
A1_Propeptide pfam07966
A1 Propeptide; Most eukaryotic endopeptidases (Merops Family A1) are synthesized with signal ...
23-49 2.97e-05

A1 Propeptide; Most eukaryotic endopeptidases (Merops Family A1) are synthesized with signal and propeptides. The animal pepsin-like endopeptidase propeptides form a distinct family of propeptides, which contain a conserved motif approximately 30 residues long. In pepsinogen A, the first 11 residues of the mature pepsin sequence are displaced by residues of the propeptide. The propeptide contains two helices that block the active site cleft, in particular the conserved Asp11 residue, in pepsin, hydrogen bonds to a conserved Arg residues in the propeptide. This hydrogen bond stabilizes the propeptide conformation and is probably responsible for triggering the conversion of pepsinogen to pepsin under acidic conditions.


Pssm-ID: 462326  Cd Length: 27  Bit Score: 40.40  E-value: 2.97e-05
                          10        20
                  ....*....|....*....|....*..
gi 4503143     23 RIPLHKFTSIRRTMSEvGGSVEDLIAK 49
Cdd:pfam07966   1 RIPLKKGKSIRETLRE-KGLLEEFLKE 26
nucellin_like cd05475
Nucellins, plant aspartic proteases specifically expressed in nucellar cells during ...
78-405 2.58e-03

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: 39.28  E-value: 2.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143   78 QYYGEIGIGTPPQCFTVVFDTGSSNLWvpsIHCKLLDIACWIHhkynsdksstyvkngtsFDIHYGSGSLS-GYLSQDTV 156
Cdd:cd05475   2 YYYVTINIGNPPKPYFLDIDTGSDLTW---LQCDAPCTGCQCD-----------------YEIEYADGGSSmGVLVTDIF 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  157 SVPCQSASSASAlggvkveRQVFGEATKQPGITFIA-AKFDGILGMAYPRISvnnvLPvfDNLMQQKLVdQNIFSFYLSR 235
Cdd:cd05475  62 SLKLTNGSRAKP-------RIAFGCGYDQQGPLLNPpPPTDGILGLGRGKIS----LP--SQLASQGII-KNVIGHCLSS 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  236 dpdaQPGGELMLGgtDSKYYKGSLSYLNVTRKA---YWQVHLDQVEVASGLTLCKeGCEAIVDTGTSLMVGPvdevrelQ 312
Cdd:cd05475 128 ----NGGGFLFFG--DDLVPSSGVTWTPMRRESqkkHYSPGPASLLFNGQPTGGK-GLEVVFDSGSSYTYFN-------A 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503143  313 KAigavpliqgeYMIPcekvstlpaITLKLGGKGYK----LSPEDYtLKVSQAGKTlCLSGFMGMDIppPSGPLWILGDV 388
Cdd:cd05475 194 QA----------YFKP---------LTLKFGKGWRTrlleIPPENY-LIISEKGNV-CLGILNGSEI--GLGNTNIIGDI 250
                       330
                ....*....|....*..
gi 4503143  389 FIGRYYTVFDRDNNRVG 405
Cdd:cd05475 251 SMQGLMVIYDNEKQQIG 267
TAXi_C pfam14541
Xylanase inhibitor C-terminal; The N- and C-termini of the members of this family are jointly ...
335-407 3.53e-03

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: 38.03  E-value: 3.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503143    335 LPAITLKL-GGKGYKLSPEDYTLKVSqaGKTLCLsGFMGMDIPPPSGPlwILGDVFIGRYYTVFDRDNNRVGFA 407
Cdd:pfam14541  92 VPPITLVFeGGADWTIFGANSMVQVD--GGVACL-GFVDGGVPPASAS--VIGGHQQEDNLLEFDLEKSRLGFS 160
 
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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