|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
1-332 |
0e+00 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 608.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 1 MATSRAALCAVAVVCVVLAAACAPARAIHVGTPAAALFEEFKRTYGRAYETLAEEQQRLANFERNLELMREHQARNPHAQ 80
Cdd:PTZ00203 1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 81 FGITKFFDLSEAEFAARYLNGAAYFAAAKRHAAQHYRKARADLSAVPDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIE 160
Cdd:PTZ00203 81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 161 GQWYLAGHELVSLSEQQLVSCDDMNDGCSGGLMLQAFDWLLQNTNGHLHTEDSYPYVSGNGYVPECSNSSELVVGAQIDG 240
Cdd:PTZ00203 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 241 HVLIGSSEKAMAAWLAKNGPIAIALDASSFMSYKSGVLTACIGKQLNHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYV 320
Cdd:PTZ00203 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
|
330
....*....|..
gi 401430387 321 RVVMGVNACLLS 332
Cdd:PTZ00203 321 RVTMGVNACLLT 332
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
126-327 |
1.67e-103 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 302.15 E-value: 1.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 126 VPDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVSCDDMNDGCSGGLMLQAFDWLLQntN 205
Cdd:pfam00112 1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKK--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 206 GHLHTEDSYPYVSGNGYvpeCSNSSELVVGAQIDGHVLI-GSSEKAMAAWLAKNGPIAIALDAS--SFMSYKSGVL--TA 280
Cdd:pfam00112 79 GGIVTESDYPYTAKDGT---CKFKKSNSKVAKIKGYGDVpYNDEEALQAALAKNGPVSVAIDAYerDFQLYKSGVYkhTE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 401430387 281 CiGKQLNHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYVRVVMGVN 327
Cdd:pfam00112 156 C-GGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVN 201
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
127-329 |
5.92e-96 |
|
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) similar to papain, including the mammalian CPs (cathepsins B, C, F, H, L, K, O, S, V, X and W). Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional carboxydipeptidyl activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds. Parasitic CPs act extracellularly to help invade tissues and cells, to hatch or to evade the host immune system. Mammalian CPs are primarily lysosomal enzymes with the exception of cathepsin W, which is retained in the endoplasmic reticulum. They are responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. In addition to its inhibitory role, the propeptide is required for proper folding of the newly synthesized enzyme and its stabilization in denaturing pH conditions. Residues within the propeptide region also play a role in the transport of the proenzyme to lysosomes or acidified vesicles. Also included in this subfamily are proteins classified as non-peptidase homologs, which lack peptidase activity or have missing active site residues.
Pssm-ID: 239068 [Multi-domain] Cd Length: 210 Bit Score: 282.98 E-value: 5.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 127 PDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVSCDDM-NDGCSGGLMLQAFDWLLQNTn 205
Cdd:cd02248 1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFEYVKNGG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 206 ghLHTEDSYPYVSGNGyvpECSNSSElVVGAQIDGHVLI-GSSEKAMAAWLAKNGPIAIALDAS-SFMSYKSGVLTA--C 281
Cdd:cd02248 80 --LASESDYPYTGKDG---TCKYNSS-KVGAKITGYSNVpPGDEEALKAALANYGPVSVAIDASsSFQFYKGGIYSGpcC 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 401430387 282 IGKQLNHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYVRVVMGVNAC 329
Cdd:cd02248 154 SNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLC 201
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
126-329 |
8.63e-77 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 232.86 E-value: 8.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 126 VPDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVSCDDMND-GCSGGLMLQAFDWLLQnt 204
Cdd:smart00645 1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNcGCNGGLPDNAFEYIKK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 205 NGHLHTEDSYPYVsgngyvpecsnsselvvgaqidghvligssekamaawlakngpIAIALDASSFMSYKSGVL--TACI 282
Cdd:smart00645 79 NGGLETESCYPYT-------------------------------------------GSVAIDASDFQFYKSGIYdhPGCG 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 401430387 283 GKQLNHGVLLVGYDMTGE--VPYWVIKNSWGGDWGEQGYVRVVMGV-NAC 329
Cdd:smart00645 116 SGTLDHAVLIVGYGTEVEngKDYWIVKNSWGTDWGENGYFRIARGKnNEC 165
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
123-322 |
2.81e-35 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 132.57 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 123 LSAVPDAVDWREKgaVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVS---LSEQQLVS-----CDDMNDGCSGGLML 194
Cdd:COG4870 1 AAALPSSVDLRGY--VTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNqarngDGTEGTDDGGSSLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 195 QAFDWLlqNTNGhLHTEDSYPYVSGNGYVPECSNSSELVVGAQIDGHVLIGSSE-----KAMAAWLAKNGPIAIALDA-S 268
Cdd:COG4870 79 DALKLL--RWSG-VVPESDWPYDDSDFTSQPSAAAYADARNYKIQDYYRLPGGGgatdlDAIKQALAEGGPVVFGFYVyE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 401430387 269 SFMSYKSGVLTACIGKQL--NHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYVRV 322
Cdd:COG4870 156 SFYNYTGGVYYPTPGDASlgGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
1-332 |
0e+00 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 608.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 1 MATSRAALCAVAVVCVVLAAACAPARAIHVGTPAAALFEEFKRTYGRAYETLAEEQQRLANFERNLELMREHQARNPHAQ 80
Cdd:PTZ00203 1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 81 FGITKFFDLSEAEFAARYLNGAAYFAAAKRHAAQHYRKARADLSAVPDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIE 160
Cdd:PTZ00203 81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 161 GQWYLAGHELVSLSEQQLVSCDDMNDGCSGGLMLQAFDWLLQNTNGHLHTEDSYPYVSGNGYVPECSNSSELVVGAQIDG 240
Cdd:PTZ00203 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 241 HVLIGSSEKAMAAWLAKNGPIAIALDASSFMSYKSGVLTACIGKQLNHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYV 320
Cdd:PTZ00203 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
|
330
....*....|..
gi 401430387 321 RVVMGVNACLLS 332
Cdd:PTZ00203 321 RVTMGVNACLLT 332
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
126-327 |
1.67e-103 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 302.15 E-value: 1.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 126 VPDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVSCDDMNDGCSGGLMLQAFDWLLQntN 205
Cdd:pfam00112 1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKK--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 206 GHLHTEDSYPYVSGNGYvpeCSNSSELVVGAQIDGHVLI-GSSEKAMAAWLAKNGPIAIALDAS--SFMSYKSGVL--TA 280
Cdd:pfam00112 79 GGIVTESDYPYTAKDGT---CKFKKSNSKVAKIKGYGDVpYNDEEALQAALAKNGPVSVAIDAYerDFQLYKSGVYkhTE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 401430387 281 CiGKQLNHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYVRVVMGVN 327
Cdd:pfam00112 156 C-GGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVN 201
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
127-329 |
5.92e-96 |
|
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) similar to papain, including the mammalian CPs (cathepsins B, C, F, H, L, K, O, S, V, X and W). Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional carboxydipeptidyl activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds. Parasitic CPs act extracellularly to help invade tissues and cells, to hatch or to evade the host immune system. Mammalian CPs are primarily lysosomal enzymes with the exception of cathepsin W, which is retained in the endoplasmic reticulum. They are responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. In addition to its inhibitory role, the propeptide is required for proper folding of the newly synthesized enzyme and its stabilization in denaturing pH conditions. Residues within the propeptide region also play a role in the transport of the proenzyme to lysosomes or acidified vesicles. Also included in this subfamily are proteins classified as non-peptidase homologs, which lack peptidase activity or have missing active site residues.
Pssm-ID: 239068 [Multi-domain] Cd Length: 210 Bit Score: 282.98 E-value: 5.92e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 127 PDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVSCDDM-NDGCSGGLMLQAFDWLLQNTn 205
Cdd:cd02248 1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFEYVKNGG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 206 ghLHTEDSYPYVSGNGyvpECSNSSElVVGAQIDGHVLI-GSSEKAMAAWLAKNGPIAIALDAS-SFMSYKSGVLTA--C 281
Cdd:cd02248 80 --LASESDYPYTGKDG---TCKYNSS-KVGAKITGYSNVpPGDEEALKAALANYGPVSVAIDASsSFQFYKGGIYSGpcC 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 401430387 282 IGKQLNHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYVRVVMGVNAC 329
Cdd:cd02248 154 SNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLC 201
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
126-329 |
8.63e-77 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 232.86 E-value: 8.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 126 VPDAVDWREKGAVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVSCDDMND-GCSGGLMLQAFDWLLQnt 204
Cdd:smart00645 1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNcGCNGGLPDNAFEYIKK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 205 NGHLHTEDSYPYVsgngyvpecsnsselvvgaqidghvligssekamaawlakngpIAIALDASSFMSYKSGVL--TACI 282
Cdd:smart00645 79 NGGLETESCYPYT-------------------------------------------GSVAIDASDFQFYKSGIYdhPGCG 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 401430387 283 GKQLNHGVLLVGYDMTGE--VPYWVIKNSWGGDWGEQGYVRVVMGV-NAC 329
Cdd:smart00645 116 SGTLDHAVLIVGYGTEVEngKDYWIVKNSWGTDWGENGYFRIARGKnNEC 165
|
|
| PTZ00200 |
PTZ00200 |
cysteine proteinase; Provisional |
38-329 |
3.94e-62 |
|
cysteine proteinase; Provisional
Pssm-ID: 240310 [Multi-domain] Cd Length: 448 Bit Score: 204.16 E-value: 3.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 38 FEEFKRTYGRAYETLAEEQQRLANFERNLELMREHQARNPHAQfGITKFFDLSEAEFAARY-----LNGAAYFAAAKRHA 112
Cdd:PTZ00200 126 FEEFNKKYNRKHATHAERLNRFLTFRNNYLEVKSHKGDEPYSK-EINKFSDLTEEEFRKLFpvikvPPKSNSTSHNNDFK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 113 AQHY---------RKAR------ADLSAV-PDAVDWREKGAVTPVKDQGA-CGSCWAFSAVGNIEGQWYLAGHELVSLSE 175
Cdd:PTZ00200 205 ARHVsnptylknlKKAKntdedvKDPSKItGEGLDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRDKSVDLSE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 176 QQLVSCDDMNDGCSGGLMLQAFDWLlqnTNGHLHTEDSYPYVSGNGyvpECSNSSELVVgaQIDG-HVLIGSS--EKAMA 252
Cdd:PTZ00200 285 QELVNCDTKSQGCSGGYPDTALEYV---KNKGLSSSSDVPYLAKDG---KCVVSSTKKV--YIDSyLVAKGKDvlNKSLV 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 253 AwlaknGPIAIALDAS-SFMSYKSGVLTACIGKQLNHGVLLV--GYDMTGEVPYWVIKNSWGGDWGEQGYVRVV---MGV 326
Cdd:PTZ00200 357 I-----SPTVVYIAVSrELLKYKSGVYNGECGKSLNHAVLLVgeGYDEKTKKRYWIIKNSWGTDWGENGYMRLErtnEGT 431
|
...
gi 401430387 327 NAC 329
Cdd:PTZ00200 432 DKC 434
|
|
| PTZ00021 |
PTZ00021 |
falcipain-2; Provisional |
37-322 |
3.08e-60 |
|
falcipain-2; Provisional
Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 200.38 E-value: 3.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 37 LFEEFKRTYGRAYETLAEEQQRLANFERNLELMREHQAR-NPHAQFGITKFFDLSEAEFAARYL---------NG----- 101
Cdd:PTZ00021 168 SFYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAHNNKeNVLYKKGMNRFGDLSFEEFKKKYLtlksfdfksNGkkspr 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 102 -AAYFAAAKRhaaqhYRKARADLSAVpdAVDWREKGAVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVS 180
Cdd:PTZ00021 248 vINYDDVIKK-----YKPKDATFDHA--KYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 181 CDDMNDGCSGGLMLQAFDWLLQntNGHLHTEDSYPYVsgnGYVPECSNSSELVVGAQIDGHVLIGSSE-KAMAAWLaknG 259
Cdd:PTZ00021 321 CSFKNNGCYGGLIPNAFEDMIE--LGGLCSEDDYPYV---SDTPELCNIDRCKEKYKIKSYVSIPEDKfKEAIRFL---G 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 401430387 260 PIAIALDAS-SFMSYKSGVLTACIGKQLNHGVLLVGYDM---------TGEVPYW-VIKNSWGGDWGEQGYVRV 322
Cdd:PTZ00021 393 PISVSIAVSdDFAFYKGGIFDGECGEEPNHAVILVGYGMeeiynsdtkKMEKRYYyIIKNSWGESWGEKGFIRI 466
|
|
| Peptidase_C1A_CathepsinB |
cd02620 |
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ... |
127-329 |
2.72e-43 |
|
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.
Pssm-ID: 239111 [Multi-domain] Cd Length: 236 Bit Score: 148.96 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 127 PDAVDWREK----GAVTPVKDQGACGSCWAFSAVGNIEGQWYLA--GHELVSLSEQQLVSCD-DMNDGCSGGLMLQAFDW 199
Cdd:cd02620 1 PESFDAREKwpncISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQsnGKENVLLSAQDLLSCCsGCGDGCNGGYPDAAWKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 200 LlqNTNGhLHTEDSYPYVSGNGYV---------------PECSNSSELVVGAQI---DGHVLIGSSEKAMAAWLAKNGPI 261
Cdd:cd02620 81 L--TTTG-VVTGGCQPYTIPPCGHhpegpppccgtpyctPKCQDGCEKTYEEDKhkgKSAYSVPSDETDIMKEIMTNGPV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 262 AIALD-ASSFMSYKSGVLTACIGKQLN-HGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYVRVVMGVNAC 329
Cdd:cd02620 158 QAAFTvYEDFLYYKSGVYQHTSGKQLGgHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNEC 227
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
123-322 |
2.81e-35 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 132.57 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 123 LSAVPDAVDWREKgaVTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVS---LSEQQLVS-----CDDMNDGCSGGLML 194
Cdd:COG4870 1 AAALPSSVDLRGY--VTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNqarngDGTEGTDDGGSSLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 195 QAFDWLlqNTNGhLHTEDSYPYVSGNGYVPECSNSSELVVGAQIDGHVLIGSSE-----KAMAAWLAKNGPIAIALDA-S 268
Cdd:COG4870 79 DALKLL--RWSG-VVPESDWPYDDSDFTSQPSAAAYADARNYKIQDYYRLPGGGgatdlDAIKQALAEGGPVVFGFYVyE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 401430387 269 SFMSYKSGVLTACIGKQL--NHGVLLVGYDMTGEVPYWVIKNSWGGDWGEQGYVRV 322
Cdd:COG4870 156 SFYNYTGGVYYPTPGDASlgGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| Peptidase_C1 |
cd02619 |
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
130-322 |
7.96e-35 |
|
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; composed of two subfamilies of cysteine peptidases (CPs), C1A (papain) and C1B (bleomycin hydrolase). Papain-like enzymes are mostly endopeptidases with some exceptions like cathepsins B, C, H and X, which are exopeptidases. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds while mammalian CPs are primarily lysosomal enzymes responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. Bleomycin hydrolase (BH) is a CP that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. It forms a hexameric ring barrel structure with the active sites imbedded in the central channel. Some members of the C1 family are proteins classified as non-peptidase homologs which lack peptidase activity or have missing active site residues.
Pssm-ID: 239110 [Multi-domain] Cd Length: 223 Bit Score: 126.48 E-value: 7.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 130 VDWREKGaVTPVKDQGACGSCWAFSAVGNIEGqWYLAGH---ELVSLSEQQLVSCDDM-----NDGCSGGLMLQAFDWLL 201
Cdd:cd02619 2 VDLRPLR-LTPVKNQGSRGSCWAFASAYALES-AYRIKGgedEYVDLSPQYLYICANDeclgiNGSCDGGGPLSALLKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 202 QNtNGhLHTEDSYPYVSGNGYVPECSNSSELVVGAQIDGHVLI-GSSEKAMAAWLAKNGPIAIALDASS-FMSYKSGVLT 279
Cdd:cd02619 80 AL-KG-IPPEEDYPYGAESDGEEPKSEAALNAAKVKLKDYRRVlKNNIEDIKEALAKGGPVVAGFDVYSgFDRLKEGIIY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 401430387 280 ACIGKQL-------NHGVLLVGYDM--TGEVPYWVIKNSWGGDWGEQGYVRV 322
Cdd:cd02619 158 EEIVYLLyedgdlgGHAVVIVGYDDnyVEGKGAFIVKNSWGTDWGDNGYGRI 209
|
|
| Peptidase_C1A_CathepsinC |
cd02621 |
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ... |
127-329 |
5.13e-34 |
|
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine peptidase with chloride dependency and dipeptidyl aminopeptidase activity, resulting from its tetrameric structure which limits substrate access. Each subunit of the tetramer is composed of three peptides: the heavy and light chains, which together adopts the papain fold and forms the catalytic domain; and the residual propeptide region, which forms a beta barrel and points towards the substrate's N-terminus. The subunit composition is the result of the unique characteristic of procathepsin C maturation involving the cleavage of the catalytic domain and the non-autocatalytic excision of an activation peptide within its propeptide region. By removing N-terminal dipeptide extensions, cathepsin C activates granule serine peptidases (granzymes) involved in cell-mediated apoptosis, inflammation and tissue remodelling. Loss-of-function mutations in cathepsin C are associated with Papillon-Lefevre and Haim-Munk syndromes, rare diseases characterized by hyperkeratosis and early-onset periodontitis. Cathepsin C is widely expressed in many tissues with high levels in lung, kidney and placenta. It is also highly expressed in cytotoxic lymphocytes and mature myeloid cells.
Pssm-ID: 239112 [Multi-domain] Cd Length: 243 Bit Score: 125.19 E-value: 5.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 127 PDAVDWREKGA----VTPVKDQGACGSCWAFSAVGNIEGQWYLAGHELVS------LSEQQLVSCDDMNDGCSGGlmlqa 196
Cdd:cd02621 2 PKSFDWGDVNNgfnyVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPlgqqpiLSPQHVLSCSQYSQGCDGG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 197 FDWL---LQNTNGhLHTEDSYPYVSGNgyVPECS-NSSELVVGAQIDGHVLIG----SSEKAMAAWLAKNGPIAIALDA- 267
Cdd:cd02621 77 FPFLvgkFAEDFG-IVTEDYFPYTADD--DRPCKaSPSECRRYYFSDYNYVGGcygcTNEDEMKWEIYRNGPIVVAFEVy 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 401430387 268 SSFMSYKSGV------LTACIG--------KQLNHGVLLVGY--DMTGEVPYWVIKNSWGGDWGEQGYVRVVMGVNAC 329
Cdd:cd02621 154 SDFDFYKEGVyhhtdnDEVSDGdndnfnpfELTNHAVLLVGWgeDEIKGEKYWIVKNSWGSSWGEKGYFKIRRGTNEC 231
|
|
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
126-326 |
3.73e-26 |
|
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response.
Pssm-ID: 239149 Cd Length: 239 Bit Score: 104.03 E-value: 3.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 126 VPDAVDWREKGAV---TPVKDQ---GACGSCWAFSAVG------NI--EGQWylaghELVSLSEQQLVSCDDMNDgCSGG 191
Cdd:cd02698 1 LPKSWDWRNVNGVnyvSPTRNQhipQYCGSCWAHGSTSaladriNIarKGAW-----PSVYLSVQVVIDCAGGGS-CHGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 192 LMLQAFDWLLQNTnghLHTEDSYPYVSGNG---YVPECSNSSELVVGAQIDGHVLIG-------SSEKAMAAWLAKNGPI 261
Cdd:cd02698 75 DPGGVYEYAHKHG---IPDETCNPYQAKDGecnPFNRCGTCNPFGECFAIKNYTLYFvsdygsvSGRDKMMAEIYARGPI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 401430387 262 AIALDASSFM-SYKSGVLTACIGKQL-NHGVLLVGY--DMTGeVPYWVIKNSWGGDWGEQGYVRVVMGV 326
Cdd:cd02698 152 SCGIMATEALeNYTGGVYKEYVQDPLiNHIISVAGWgvDENG-VEYWIVRNSWGEPWGERGWFRIVTSS 219
|
|
| Inhibitor_I29 |
smart00848 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
38-93 |
1.56e-15 |
|
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.
Pssm-ID: 214853 [Multi-domain] Cd Length: 57 Bit Score: 69.96 E-value: 1.56e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 401430387 38 FEEFKRTYGRAYETLAEEQQRLANFERNLELMREHQARNPH-AQFGITKFFDLSEAE 93
Cdd:smart00848 1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHsYKLGVNQFSDLTPEE 57
|
|
| Inhibitor_I29 |
pfam08246 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
38-94 |
1.68e-15 |
|
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin Swiss:Q70SU8. This family is classified as I29 by MEROPS.
Pssm-ID: 462410 [Multi-domain] Cd Length: 58 Bit Score: 69.98 E-value: 1.68e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 401430387 38 FEEFKRTYGRAYETLAEEQQRLANFERNLELMREHQARNPH-AQFGITKFFDLSEAEF 94
Cdd:pfam08246 1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGNVtYKLGLNKFADLTDEEF 58
|
|
| PTZ00049 |
PTZ00049 |
cathepsin C-like protein; Provisional |
141-327 |
3.24e-14 |
|
cathepsin C-like protein; Provisional
Pssm-ID: 240244 [Multi-domain] Cd Length: 693 Bit Score: 73.45 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 141 VKDQGACGSCWAFSAV----GNIE-------GQWYLAGHElVSLSEQQLVSCDDMNDGCSGGlmlqaFDWL--------- 200
Cdd:PTZ00049 400 VTNQLLCGSCYIASQMyafkRRIEialtknlDKKYLNNFD-DLLSIQTVLSCSFYDQGCNGG-----FPYLvskmaklqg 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 201 --LQNTNGHLHTEDSYPY---VSGNGYVPEC----------SNSSELVVGAQIDGHVL-------------IG------- 245
Cdd:PTZ00049 474 ipLDKVFPYTATEQTCPYqvdQSANSMNGSAnlrqinavffSSETQSDMHADFEAPISseparwyakdynyIGgcygcnq 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 246 -SSEKAMAAWLAKNGPIAIALDAS-SFMSYKSGVLTA--------CIG--------------KQLNHGVLLVGY---DMT 298
Cdd:PTZ00049 554 cNGEKIMMNEIYRNGPIVASFEASpDFYDYADGVYYVedfpharrCTVdlpkhngvynitgwEKVNHAIVLVGWgeeEIN 633
|
250 260 270
....*....|....*....|....*....|
gi 401430387 299 GEV-PYWVIKNSWGGDWGEQGYVRVVMGVN 327
Cdd:PTZ00049 634 GKLyKYWIGRNSWGKNWGKEGYFKIIRGKN 663
|
|
| PTZ00364 |
PTZ00364 |
dipeptidyl-peptidase I precursor; Provisional |
127-328 |
3.30e-13 |
|
dipeptidyl-peptidase I precursor; Provisional
Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 70.30 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 127 PDAVDWREKGAVT---PVKDQGA---CGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVS------CDDMNDGCSGGLML 194
Cdd:PTZ00364 206 PAAWSWGDVGGASflpAAPPASPgrgCNSSYVEAALAAMMARVMVASNRTDPLGQQTFLSarhvldCSQYGQGCAGGFPE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 195 QAFdwLLQNTNGHLhTEDSY--PYVSGNGYVPECSNSSE-----LVVGAQIDGHVLIGSSEKAMAAWLAKNGPIAIALDA 267
Cdd:PTZ00364 286 EVG--KFAETFGIL-TTDSYyiPYDSGDGVERACKTRRPsrryyFTNYGPLGGYYGAVTDPDEIIWEIYRHGPVPASVYA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 268 -------------SSFMSYKSGVLTACIGK--------QLNHGVLLVGY--DMTGeVPYWVIKNSWG--GDWGEQGYVRV 322
Cdd:PTZ00364 363 nsdwyncdensteDVRYVSLDDYSTASADRplrhyfasNVNHTVLIIGWgtDENG-GDYWLVLDPWGsrRSWCDGGTRKI 441
|
....*.
gi 401430387 323 VMGVNA 328
Cdd:PTZ00364 442 ARGVNA 447
|
|
| PTZ00462 |
PTZ00462 |
Serine-repeat antigen protein; Provisional |
141-329 |
4.54e-10 |
|
Serine-repeat antigen protein; Provisional
Pssm-ID: 185641 [Multi-domain] Cd Length: 1004 Bit Score: 60.85 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 141 VKDQGACGSCWAFSAVGNIEGQWYLAGHELVSLSEQQLVSC------DDMNDGCSGGLMLQAFDwllqnTNGHLHTEDSY 214
Cdd:PTZ00462 547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCskgehkDRCDEGSNPLEFLQIIE-----DNGFLPADSNY 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 401430387 215 PYvsgnGYVP---ECSNSSELVVGAQIDGHVLIGS-------SEKAMAAW-------------------LAKNGPIAIAL 265
Cdd:PTZ00462 622 LY----NYTKvgeDCPDEEDHWMNLLDHGKILNHNkkepnslDGKAYRAYesehfhdkmdafikiikdeIMNKGSVIAYI 697
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 401430387 266 DASSFMSYK-SG--VLTACIGKQLNHGVLLVGY-----DMTGEVPYWVIKNSWGGDWGEQGYVRVVM-GVNAC 329
Cdd:PTZ00462 698 KAENVLGYEfNGkkVQNLCGDDTADHAVNIVGYgnyinDEDEKKSYWIVRNSWGKYWGDEGYFKVDMyGPSHC 770
|
|
| Peptidase_C1_2 |
pfam03051 |
Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, ... |
286-319 |
7.33e-03 |
|
Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, containing several prokaryotic and eukaryotic aminopeptidases and bleomycin hydrolases.
Pssm-ID: 397262 Cd Length: 438 Bit Score: 38.09 E-value: 7.33e-03
10 20 30
....*....|....*....|....*....|....*.
gi 401430387 286 LNHGVLLVGYDM--TGEVPYWVIKNSWGGDWGEQGY 319
Cdd:pfam03051 359 MTHAMVLTGVDEddDGKPTKWKVENSWGEDSGEKGY 394
|
|
| |
