|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
10-349 |
1.03e-128 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 372.50 E-value: 1.03e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 10 AIVVTILFVVCY-GSALIAQTPppvdnfvASAHYGSFKKRHGKAFGGDAEEGHRFNAFKQNMQTAYFLNTQNPHAHYDVS 88
Cdd:PTZ00203 12 AVVCVVLAAACApARAIYVGTP-------AAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHARFGIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 89 gKFADLTPQEFAKLYLN-PDYYA---RHLKNHKEDVHVDDSAPSGvmSVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEG 164
Cdd:PTZ00203 85 -KFFDLSEAEFAARYLNgAAYFAaakQHAGQHYRKARADLSAVPD--AVDWREKGAVTPVKNQGACGSCWAFSAVGNIES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 165 QWAASGHSLVSLSEQMLVSCDNIDEGCNGGLMDQAMNWIMQSHNGSVFTEASYPYTSGGGTRPPCHDEGEV--GAKITGF 242
Cdd:PTZ00203 162 QWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELapGARIDGY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 243 LSLPHDEERIAEWVEKRGPVAVAVDATTWQLYFGGVVSLCLAWSLNHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIR 322
Cdd:PTZ00203 242 VSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVR 321
|
330 340
....*....|....*....|....*..
gi 126021 323 LAMGSNQCMLKNYPVSATVESPHTPHV 349
Cdd:PTZ00203 322 VTMGVNACLLTGYPVSVHVSQSPTPYL 348
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
132-340 |
8.18e-96 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 283.66 E-value: 8.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 132 SVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVSLSEQMLVSCDNIDEGCNGGLMDQAMNWIMQshNGSV 211
Cdd:pfam00112 4 SFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKK--NGGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 212 FTEASYPYTSGGGTrppCH--DEGEVGAKITGFLSLPH-DEERIAEWVEKRGPVAVAVDAT--TWQLYFGGVVSL--CLA 284
Cdd:pfam00112 82 VTESDYPYTAKDGT---CKfkKSNSKVAKIKGYGDVPYnDEEALQAALAKNGPVSVAIDAYerDFQLYKSGVYKHteCGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126021 285 wSLNHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIRLAMGSN-QCMLKNYPVSAT 340
Cdd:pfam00112 159 -ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
132-339 |
1.77e-91 |
|
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: 272.58 E-value: 1.77e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 132 SVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVSLSEQMLVSCD-NIDEGCNGGLMDQAMNWImqsHNGS 210
Cdd:cd02248 3 SVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCStSGNNGCNGGNPDNAFEYV---KNGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 211 VFTEASYPYTSGGGTrppCH-DEGEVGAKITGFLSLPH-DEERIAEWVEKRGPVAVAVDAT-TWQLYFGGVVSL--CLAW 285
Cdd:cd02248 80 LASESDYPYTGKDGT---CKyNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASsSFQFYKGGIYSGpcCSNT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126021 286 SLNHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIRLAMGSNQCMLKNYPVSA 339
Cdd:cd02248 157 NLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
132-339 |
5.26e-72 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 221.69 E-value: 5.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 132 SVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVSLSEQMLVSCDN-IDEGCNGGLMDQAMNWIMQshNGS 210
Cdd:smart00645 4 SFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGgGNCGCNGGLPDNAFEYIKK--NGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 211 VFTEASYPYTSgggtrppchdegevgakitgflslphdeeriaewvekrgpvAVAVDATTWQLYFGGVV--SLCLAWSLN 288
Cdd:smart00645 82 LETESCYPYTG-----------------------------------------SVAIDASDFQFYKSGIYdhPGCGSGTLD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126021 289 HGVLIVGFNKNA--KPPYWIVKNSWGSSWGEKGYIRLAMGS-NQCMLKNYPVSA 339
Cdd:smart00645 121 HAVLIVGYGTEVenGKDYWIVKNSWGTDWGENGYFRIARGKnNECGIEASVASY 174
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
124-323 |
5.12e-32 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 124.48 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 124 DSAPSgvmSVDWRdkGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVS---LSEQMLVSC----DNIDEGCNGGLM 196
Cdd:COG4870 2 AALPS---SVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNQarngDGTEGTDDGGSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 197 DQ-AMNWImqSHNGSVfTEASYPYTSGGGTRPPCHDEGEVGA--KITGFLSLP-----HDEERIAEWVEKRGPVAVAVDA 268
Cdd:COG4870 77 LRdALKLL--RWSGVV-PESDWPYDDSDFTSQPSAAAYADARnyKIQDYYRLPggggaTDLDAIKQALAEGGPVVFGFYV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126021 269 T-TWQLYFGGVV--SLCLAWSLNHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIRL 323
Cdd:COG4870 154 YeSFYNYTGGVYypTPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
10-349 |
1.03e-128 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 372.50 E-value: 1.03e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 10 AIVVTILFVVCY-GSALIAQTPppvdnfvASAHYGSFKKRHGKAFGGDAEEGHRFNAFKQNMQTAYFLNTQNPHAHYDVS 88
Cdd:PTZ00203 12 AVVCVVLAAACApARAIYVGTP-------AAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHARFGIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 89 gKFADLTPQEFAKLYLN-PDYYA---RHLKNHKEDVHVDDSAPSGvmSVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEG 164
Cdd:PTZ00203 85 -KFFDLSEAEFAARYLNgAAYFAaakQHAGQHYRKARADLSAVPD--AVDWREKGAVTPVKNQGACGSCWAFSAVGNIES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 165 QWAASGHSLVSLSEQMLVSCDNIDEGCNGGLMDQAMNWIMQSHNGSVFTEASYPYTSGGGTRPPCHDEGEV--GAKITGF 242
Cdd:PTZ00203 162 QWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELapGARIDGY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 243 LSLPHDEERIAEWVEKRGPVAVAVDATTWQLYFGGVVSLCLAWSLNHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIR 322
Cdd:PTZ00203 242 VSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVR 321
|
330 340
....*....|....*....|....*..
gi 126021 323 LAMGSNQCMLKNYPVSATVESPHTPHV 349
Cdd:PTZ00203 322 VTMGVNACLLTGYPVSVHVSQSPTPYL 348
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
132-340 |
8.18e-96 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 283.66 E-value: 8.18e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 132 SVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVSLSEQMLVSCDNIDEGCNGGLMDQAMNWIMQshNGSV 211
Cdd:pfam00112 4 SFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKK--NGGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 212 FTEASYPYTSGGGTrppCH--DEGEVGAKITGFLSLPH-DEERIAEWVEKRGPVAVAVDAT--TWQLYFGGVVSL--CLA 284
Cdd:pfam00112 82 VTESDYPYTAKDGT---CKfkKSNSKVAKIKGYGDVPYnDEEALQAALAKNGPVSVAIDAYerDFQLYKSGVYKHteCGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 126021 285 wSLNHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIRLAMGSN-QCMLKNYPVSAT 340
Cdd:pfam00112 159 -ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
132-339 |
1.77e-91 |
|
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: 272.58 E-value: 1.77e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 132 SVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVSLSEQMLVSCD-NIDEGCNGGLMDQAMNWImqsHNGS 210
Cdd:cd02248 3 SVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCStSGNNGCNGGNPDNAFEYV---KNGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 211 VFTEASYPYTSGGGTrppCH-DEGEVGAKITGFLSLPH-DEERIAEWVEKRGPVAVAVDAT-TWQLYFGGVVSL--CLAW 285
Cdd:cd02248 80 LASESDYPYTGKDGT---CKyNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASsSFQFYKGGIYSGpcCSNT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126021 286 SLNHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIRLAMGSNQCMLKNYPVSA 339
Cdd:cd02248 157 NLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
132-339 |
5.26e-72 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 221.69 E-value: 5.26e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 132 SVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVSLSEQMLVSCDN-IDEGCNGGLMDQAMNWIMQshNGS 210
Cdd:smart00645 4 SFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGgGNCGCNGGLPDNAFEYIKK--NGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 211 VFTEASYPYTSgggtrppchdegevgakitgflslphdeeriaewvekrgpvAVAVDATTWQLYFGGVV--SLCLAWSLN 288
Cdd:smart00645 82 LETESCYPYTG-----------------------------------------SVAIDASDFQFYKSGIYdhPGCGSGTLD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 126021 289 HGVLIVGFNKNA--KPPYWIVKNSWGSSWGEKGYIRLAMGS-NQCMLKNYPVSA 339
Cdd:smart00645 121 HAVLIVGYGTEVenGKDYWIVKNSWGTDWGENGYFRIARGKnNECGIEASVASY 174
|
|
| PTZ00021 |
PTZ00021 |
falcipain-2; Provisional |
45-323 |
4.00e-55 |
|
falcipain-2; Provisional
Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 187.67 E-value: 4.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 45 FKKRHGKAFGGDAEEGHRFNAFKQNMQTAYFLNTQNPHAHYDVSGKFADLTPQEFAKLYLN-------------PDY--Y 109
Cdd:PTZ00021 172 FIKEHGKKYQTPDEMQQRYLSFVENLAKINAHNNKENVLYKKGMNRFGDLSFEEFKKKYLTlksfdfksngkksPRVinY 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 110 ARHLKNHK-EDVHVDDSApsgvmsVDWRDKGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVSLSEQMLVSCDNID 188
Cdd:PTZ00021 252 DDVIKKYKpKDATFDHAK------YDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSFKN 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 189 EGCNGGLMDQAMNWIMQShnGSVFTEASYPYTsggGTRPP-CH-DEGEVGAKITGFLSLPhdEERIAEWVEKRGPVAVAV 266
Cdd:PTZ00021 326 NGCYGGLIPNAFEDMIEL--GGLCSEDDYPYV---SDTPElCNiDRCKEKYKIKSYVSIP--EDKFKEAIRFLGPISVSI 398
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 126021 267 DAT-TWQLYFGGVVSLCLAWSLNHGVLIVGF----------NKNAKPPYWIVKNSWGSSWGEKGYIRL 323
Cdd:PTZ00021 399 AVSdDFAFYKGGIFDGECGEEPNHAVILVGYgmeeiynsdtKKMEKRYYYIIKNSWGESWGEKGFIRI 466
|
|
| PTZ00200 |
PTZ00200 |
cysteine proteinase; Provisional |
44-330 |
1.20e-48 |
|
cysteine proteinase; Provisional
Pssm-ID: 240310 [Multi-domain] Cd Length: 448 Bit Score: 169.49 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 44 SFKKRHGKAFGGDAEEGHRFNAFKQNmqtaYF-LNTQNPHAHYdVSG--KFADLTPQEFAKLY-------------LNPD 107
Cdd:PTZ00200 128 EFNKKYNRKHATHAERLNRFLTFRNN----YLeVKSHKGDEPY-SKEinKFSDLTEEEFRKLFpvikvppksnstsHNND 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 108 YYARH------LKNHKEDVHVDDSA--PSGVMS--VDWRDKGAVTPVKNQGL-CGSCWAFSAIGNIEGQWAASGHSLVSL 176
Cdd:PTZ00200 203 FKARHvsnptyLKNLKKAKNTDEDVkdPSKITGegLDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRDKSVDL 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 177 SEQMLVSCDNIDEGCNGGLMDQAMNWImqsHNGSVFTEASYPYTsggGTRPPC--HDEGEVgaKITGFLSLPHDEeriae 254
Cdd:PTZ00200 283 SEQELVNCDTKSQGCSGGYPDTALEYV---KNKGLSSSSDVPYL---AKDGKCvvSSTKKV--YIDSYLVAKGKD----- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 255 wVEKR----GPVAVAVDAT-TWQLYFGGVVSLCLAWSLNHGVLIV--GFNKNAKPPYWIVKNSWGSSWGEKGYIRLA--- 324
Cdd:PTZ00200 350 -VLNKslviSPTVVYIAVSrELLKYKSGVYNGECGKSLNHAVLLVgeGYDEKTKKRYWIIKNSWGTDWGENGYMRLErtn 428
|
....*.
gi 126021 325 MGSNQC 330
Cdd:PTZ00200 429 EGTDKC 434
|
|
| Peptidase_C1 |
cd02619 |
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
132-323 |
2.88e-33 |
|
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: 123.01 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 132 SVDWRDKGaVTPVKNQGLCGSCWAFSAIGNIEGQW--AASGHSLVSLSEQMLVSCDN-----IDEGCNGGLMDQAMNWIM 204
Cdd:cd02619 1 SVDLRPLR-LTPVKNQGSRGSCWAFASAYALESAYriKGGEDEYVDLSPQYLYICANdeclgINGSCDGGGPLSALLKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 205 QSHnGsVFTEASYPYTSG-GGTRPPCHDEGEVGA-KITGF-LSLPHDEERIAEWVEKRGPVAVAVDAT-TWQLYFGGVVS 280
Cdd:cd02619 80 ALK-G-IPPEEDYPYGAEsDGEEPKSEAALNAAKvKLKDYrRVLKNNIEDIKEALAKGGPVVAGFDVYsGFDRLKEGIIY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 126021 281 LCLAWSL-------NHGVLIVGFNKNAKP--PYWIVKNSWGSSWGEKGYIRL 323
Cdd:cd02619 158 EEIVYLLyedgdlgGHAVVIVGYDDNYVEgkGAFIVKNSWGTDWGDNGYGRI 209
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
124-323 |
5.12e-32 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 124.48 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 124 DSAPSgvmSVDWRdkGAVTPVKNQGLCGSCWAFSAIGNIEGQWAASGHSLVS---LSEQMLVSC----DNIDEGCNGGLM 196
Cdd:COG4870 2 AALPS---SVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNQarngDGTEGTDDGGSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 197 DQ-AMNWImqSHNGSVfTEASYPYTSGGGTRPPCHDEGEVGA--KITGFLSLP-----HDEERIAEWVEKRGPVAVAVDA 268
Cdd:COG4870 77 LRdALKLL--RWSGVV-PESDWPYDDSDFTSQPSAAAYADARnyKIQDYYRLPggggaTDLDAIKQALAEGGPVVFGFYV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 126021 269 T-TWQLYFGGVV--SLCLAWSLNHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIRL 323
Cdd:COG4870 154 YeSFYNYTGGVYypTPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| Peptidase_C1A_CathepsinB |
cd02620 |
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ... |
135-339 |
7.55e-32 |
|
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: 119.68 E-value: 7.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 135 WRDKGAVTPVKNQGLCGSCWAFSAIGniegqwAAS--------GHSLVSLSEQMLVSCD-NIDEGCNGGLMDQAMNWImq 205
Cdd:cd02620 10 WPNCISIGEIRDQGNCGSCWAFSAVE------AFSdrlciqsnGKENVLLSAQDLLSCCsGCGDGCNGGYPDAAWKYL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 206 sHNGSVFTEASYPYTSGGGTR---------------PPCHDEGEVG-----AKITGFLSLPHDEERIAEWVEKRGPVAVA 265
Cdd:cd02620 82 -TTTGVVTGGCQPYTIPPCGHhpegpppccgtpyctPKCQDGCEKTyeedkHKGKSAYSVPSDETDIMKEIMTNGPVQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 266 -------------VDATTWQLYFGGvvslclawslnHGVLIVGFNKNAKPPYWIVKNSWGSSWGEKGYIRLAMGSNQCML 332
Cdd:cd02620 161 ftvyedflyyksgVYQHTSGKQLGG-----------HAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNECGI 229
|
....*..
gi 126021 333 KNYPVSA 339
Cdd:cd02620 230 ESEVVAG 236
|
|
| Peptidase_C1A_CathepsinC |
cd02621 |
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ... |
134-340 |
1.04e-29 |
|
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: 114.02 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 134 DWRDKGA----VTPVKNQGLCGSCWAFSAIGNIEG--QWAASGHSLVS----LSEQMLVSCDNIDEGCNGG---LMDQAM 200
Cdd:cd02621 6 DWGDVNNgfnyVSPVRNQGGCGSCYAFASVYALEAriMIASNKTDPLGqqpiLSPQHVLSCSQYSQGCDGGfpfLVGKFA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 201 NWImqshngSVFTEASYPYTsgGGTRPPC--HDEGEVGAKITGFLSLPH-----DEERIAEWVEKRGPVAVAVDATT-WQ 272
Cdd:cd02621 86 EDF------GIVTEDYFPYT--ADDDRPCkaSPSECRRYYFSDYNYVGGcygctNEDEMKWEIYRNGPIVVAFEVYSdFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 273 LYFGGV-VSLCLAWS-------------LNHGVLIVGFNKNAKP--PYWIVKNSWGSSWGEKGYIRLAMGSNQCMLKNYP 336
Cdd:cd02621 158 FYKEGVyHHTDNDEVsdgdndnfnpfelTNHAVLLVGWGEDEIKgeKYWIVKNSWGSSWGEKGYFKIRRGTNECGIESQA 237
|
....
gi 126021 337 VSAT 340
Cdd:cd02621 238 VFAY 241
|
|
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
132-327 |
2.51e-23 |
|
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: 96.71 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 132 SVDWRDKGAV---TPVKNQGL---CGSCWAF---SAIG---NI--EGQWAAsghslVSLSEQMLVSCDNIDEgCNGGLMD 197
Cdd:cd02698 4 SWDWRNVNGVnyvSPTRNQHIpqyCGSCWAHgstSALAdriNIarKGAWPS-----VYLSVQVVIDCAGGGS-CHGGDPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 198 QAMNWImqsHNGSVFTEASYPYTsggGTRPPCHDEGEVG----------------AKITGFLSLPHDEERIAEwVEKRGP 261
Cdd:cd02698 78 GVYEYA---HKHGIPDETCNPYQ---AKDGECNPFNRCGtcnpfgecfaiknytlYFVSDYGSVSGRDKMMAE-IYARGP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126021 262 VAVAVDATTWQL-YFGGVVSLCLAWSL-NHGVLIVGFNK-NAKPPYWIVKNSWGSSWGEKGYIRLAMGS 327
Cdd:cd02698 151 ISCGIMATEALEnYTGGVYKEYVQDPLiNHIISVAGWGVdENGVEYWIVRNSWGEPWGERGWFRIVTSS 219
|
|
| PTZ00364 |
PTZ00364 |
dipeptidyl-peptidase I precursor; Provisional |
119-339 |
4.10e-14 |
|
dipeptidyl-peptidase I precursor; Provisional
Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 73.39 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 119 DVHVDDSAPSgvmSVDWRDKG------AVTPVKNQGLCGSCWAFSAIgniegqWAASGHSLVS------------LSEQM 180
Cdd:PTZ00364 198 SHQLGDPPPA---AWSWGDVGgasflpAAPPASPGRGCNSSYVEAAL------AAMMARVMVAsnrtdplgqqtfLSARH 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 181 LVSCDNIDEGCNGGLMDQAMNWimqSHNGSVFTEASY--PYTSGGGTRPPCH-DEGEV------GAKITGFLSLPHDEER 251
Cdd:PTZ00364 269 VLDCSQYGQGCAGGFPEEVGKF---AETFGILTTDSYyiPYDSGDGVERACKtRRPSRryyftnYGPLGGYYGAVTDPDE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 252 IAEWVEKRGPVAVAVDATTwQLYF-----GGVVSLCLAWS-----------------LNHGVLIVGFNKNA-KPPYWIVK 308
Cdd:PTZ00364 346 IIWEIYRHGPVPASVYANS-DWYNcdensTEDVRYVSLDDystasadrplrhyfasnVNHTVLIIGWGTDEnGGDYWLVL 424
|
250 260 270
....*....|....*....|....*....|...
gi 126021 309 NSWGS--SWGEKGYIRLAMGSNQCMLKNYPVSA 339
Cdd:PTZ00364 425 DPWGSrrSWCDGGTRKIARGVNAYNIESEVVVM 457
|
|
| PTZ00049 |
PTZ00049 |
cathepsin C-like protein; Provisional |
144-328 |
2.03e-12 |
|
cathepsin C-like protein; Provisional
Pssm-ID: 240244 [Multi-domain] Cd Length: 693 Bit Score: 68.06 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 144 VKNQGLCGSCWAFSAIGNIEGQW--AAS---GHSLVS-----LSEQMLVSCDNIDEGCNGGL------------------ 195
Cdd:PTZ00049 400 VTNQLLCGSCYIASQMYAFKRRIeiALTknlDKKYLNnfddlLSIQTVLSCSFYDQGCNGGFpylvskmaklqgipldkv 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 196 -------------MDQAMNWIMQSH-----NGSVFTEASYPYTSGGGTRPPCHDEGEVGAKITGFLSLPHD------EER 251
Cdd:PTZ00049 480 fpytateqtcpyqVDQSANSMNGSAnlrqiNAVFFSSETQSDMHADFEAPISSEPARWYAKDYNYIGGCYGcnqcngEKI 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 252 IAEWVEKRGPVAVAVDAT-TWQLYFGGV---------------------VSLCLAWS-LNHGVLIVGFNK---NAKP-PY 304
Cdd:PTZ00049 560 MMNEIYRNGPIVASFEASpDFYDYADGVyyvedfpharrctvdlpkhngVYNITGWEkVNHAIVLVGWGEeeiNGKLyKY 639
|
250 260
....*....|....*....|....
gi 126021 305 WIVKNSWGSSWGEKGYIRLAMGSN 328
Cdd:PTZ00049 640 WIGRNSWGKNWGKEGYFKIIRGKN 663
|
|
| Inhibitor_I29 |
pfam08246 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
42-99 |
2.04e-12 |
|
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: 61.51 E-value: 2.04e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 126021 42 YGSFKKRHGKAFGGDAEEGHRFNAFKQNMQTAYFLNtQNPHAHYDVS-GKFADLTPQEF 99
Cdd:pfam08246 1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHN-SNGNVTYKLGlNKFADLTDEEF 58
|
|
| Inhibitor_I29 |
smart00848 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
42-98 |
1.09e-11 |
|
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: 59.18 E-value: 1.09e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 126021 42 YGSFKKRHGKAFGGDAEEGHRFNAFKQNMQTAYFLNTQNPHAHYDVSGKFADLTPQE 98
Cdd:smart00848 1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHSYKLGVNQFSDLTPEE 57
|
|
| PTZ00462 |
PTZ00462 |
Serine-repeat antigen protein; Provisional |
144-330 |
3.38e-08 |
|
Serine-repeat antigen protein; Provisional
Pssm-ID: 185641 [Multi-domain] Cd Length: 1004 Bit Score: 55.45 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 144 VKNQGLCGSCWAFSAIGNIEGQWAASGHSLVSLSEQMLVSC------DNIDEGCN----------GGLM----------- 196
Cdd:PTZ00462 547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCskgehkDRCDEGSNpleflqiiedNGFLpadsnylynyt 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 197 -------DQAMNWIMQSHNGSVFTEASYPYTSGGGTRPPCHDEGEVGAKITGFLSLPHDEeriaewVEKRGPVAVAVDAT 269
Cdd:PTZ00462 627 kvgedcpDEEDHWMNLLDHGKILNHNKKEPNSLDGKAYRAYESEHFHDKMDAFIKIIKDE------IMNKGSVIAYIKAE 700
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126021 270 TWQLY-FGG--VVSLCLAWSLNHGVLIVGF-----NKNAKPPYWIVKNSWGSSWGEKGYIRLAM-GSNQC 330
Cdd:PTZ00462 701 NVLGYeFNGkkVQNLCGDDTADHAVNIVGYgnyinDEDEKKSYWIVRNSWGKYWGDEGYFKVDMyGPSHC 770
|
|
| PepC |
COG3579 |
Aminopeptidase C [Amino acid transport and metabolism]; |
287-320 |
1.16e-07 |
|
Aminopeptidase C [Amino acid transport and metabolism];
Pssm-ID: 442798 [Multi-domain] Cd Length: 440 Bit Score: 52.95 E-value: 1.16e-07
10 20 30
....*....|....*....|....*....|....*.
gi 126021 287 LNHGVLIVGFNK--NAKPPYWIVKNSWGSSWGEKGY 320
Cdd:COG3579 361 DTHAMVITGVDLdqNGKPTRWKVENSWGDDNGYKGY 396
|
|
| Peptidase_C1_2 |
pfam03051 |
Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, ... |
287-320 |
3.59e-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: 38.86 E-value: 3.59e-03
10 20 30
....*....|....*....|....*....|....*.
gi 126021 287 LNHGVLIVGFN--KNAKPPYWIVKNSWGSSWGEKGY 320
Cdd:pfam03051 359 MTHAMVLTGVDedDDGKPTKWKVENSWGEDSGEKGY 394
|
|
| Peptidase_C1B |
cd00585 |
Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin ... |
286-320 |
5.86e-03 |
|
Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin hydrolases (BH) and bacterial aminopeptidases C (pepC). The proteins of this subfamily contain a large insert relative to the C1A peptidase (papain) subfamily. BH is a cysteine peptidase 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. Bleomycin, a glycopeptide derived from the fungus Streptomyces verticullus, is an effective anticancer drug due to its ability to induce DNA strand breaks. Human BH is the major cause of tumor cell resistance to bleomycin chemotherapy, and is also genetically linked to Alzheimer's disease. In addition to its peptidase activity, the yeast BH (Gal6) binds DNA and acts as a repressor in the Gal4 regulatory system. BH forms a hexameric ring barrel structure with the active sites imbedded in the central channel. The bacterial homolog of BH, called pepC, is a cysteine aminopeptidase possessing broad specificity. Although its crystal structure has not been solved, biochemical analysis shows that pepC also forms a hexamer.
Pssm-ID: 238328 [Multi-domain] Cd Length: 437 Bit Score: 38.34 E-value: 5.86e-03
10 20 30
....*....|....*....|....*....|....*..
gi 126021 286 SLNHGVLIVGFN--KNAKPPYWIVKNSWGSSWGEKGY 320
Cdd:cd00585 357 LMTHAMVLTGVDldEDGKPVKWKVENSWGEKVGKKGY 393
|
|
| |
