|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
62-302 |
6.42e-165 |
|
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: 457.65 E-value: 6.42e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 62 LPKSWDWRNVDGVNYASITRNQHIPQYCGSCWAHASTSAMADRINIKRKGAWPSTLLSVQNVIDCGNAGSCEGGNDLSVW 141
Cdd:cd02698 1 LPKSWDWRNVNGVNYVSPTRNQHIPQYCGSCWAHGSTSALADRINIARKGAWPSVYLSVQVVIDCAGGGSCHGGDPGGVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 142 DYAHQHGIPDETCNNYQAKDQECDKFNQCGTCNEFKECHAIRNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATER 221
Cdd:cd02698 81 EYAHKHGIPDETCNPYQAKDGECNPFNRCGTCNPFGECFAIKNYTLYFVSDYGSVSGRDKMMAEIYARGPISCGIMATEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 222 LANYTGGIYAEYQDTTYINHVVSVAGWGISD-GTEYWIVRNSWGEPWGERGWLRIVTSTYkdgKGARYNLAIEEHCTFGD 300
Cdd:cd02698 161 LENYTGGVYKEYVQDPLINHIISVAGWGVDEnGVEYWIVRNSWGEPWGERGWFRIVTSSY---KGARYNLAIEEDCAWAD 237
|
..
gi 22538442 301 PI 302
Cdd:cd02698 238 PI 239
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
62-281 |
1.33e-64 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 202.39 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 62 LPKSWDWRNVdgvNYASITRNQHipqYCGSCWAHASTSAMADRINIKRKgawPSTLLSVQNVIDC--GNAGsCEGGNDLS 139
Cdd:pfam00112 1 LPESFDWREK---GAVTPVKDQG---QCGSCWAFSAVGALEGRYCIKTG---KLVSLSEQQLVDCdtFNNG-CNGGLPDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 140 VWDYAHQ-HGIPDETCNNYQAKDQECdKFNQCgtcnefkechairNYTLWRVGDYGSLSGR--EKMMAEIYANGPISCGI 216
Cdd:pfam00112 71 AFEYIKKnGGIVTESDYPYTAKDGTC-KFKKS-------------NSKVAKIKGYGDVPYNdeEALQAALAKNGPVSVAI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22538442 217 MATER-LANYTGGIYAEYQDTTYINHVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIVTSTYK 281
Cdd:pfam00112 137 DAYERdFQLYKSGVYKHTECGGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNN 202
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
62-281 |
1.28e-38 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 134.25 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 62 LPKSWDWRNVDGVnyaSITRNQHipqYCGSCWAHASTSAMADRINIKRKGawpSTLLSVQNVIDCGNAGS--CEGGNDLS 139
Cdd:smart00645 1 LPESFDWRKKGAV---TPVKDQG---QCGSCWAFSATGALEGRYCIKTGK---LVSLSEQQLVDCSGGGNcgCNGGLPDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 140 VWDYAHQH-GIPDETCNNYQAkdqecdkfnqcgtcnefkechairnytlwrvgdygslsgrekmmaeiyangpiSCGIMA 218
Cdd:smart00645 72 AFEYIKKNgGLETESCYPYTG-----------------------------------------------------SVAIDA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22538442 219 TErLANYTGGIYAEYQDTT-YINHVVSVAGWG--ISDGTEYWIVRNSWGEPWGERGWLRIVTSTYK 281
Cdd:smart00645 99 SD-FQFYKSGIYDHPGCGSgTLDHAVLIVGYGteVENGKDYWIVKNSWGTDWGENGYFRIARGKNN 163
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
59-282 |
1.05e-29 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 116.77 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 59 PADLPKSWDWRNvdgvnYASITRNQhipQYCGSCWAHASTSAMADRINIKRKGAWPSTLLSVQNVI-----DCGNAGSCE 133
Cdd:COG4870 1 AAALPSSVDLRG-----YVTPVKDQ---GSLGSCWAFATAAALESYLKKQAGAPGTSLDLSELFLYnqarnGDGTEGTDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 134 GGNDL-SVWDYAHQHGIPDETCNNYQAKDQECDKFNQCgtcnefkechaIRNYTLWRVGDYGSLSGR------EKMMAEI 206
Cdd:COG4870 73 GGSSLrDALKLLRWSGVVPESDWPYDDSDFTSQPSAAA-----------YADARNYKIQDYYRLPGGggatdlDAIKQAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22538442 207 YANGPISCGIMATERLANYTGGIYA-EYQDTTYINHVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIvtsTYKD 282
Cdd:COG4870 142 AEGGPVVFGFYVYESFYNYTGGVYYpTPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI---SYDD 215
|
|
| PTZ00049 |
PTZ00049 |
cathepsin C-like protein; Provisional |
53-301 |
1.27e-26 |
|
cathepsin C-like protein; Provisional
Pssm-ID: 240244 [Multi-domain] Cd Length: 693 Bit Score: 109.66 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 53 PHEYLSPADLPKSWDWrnvdGVNYASITRNQHIPQ--YCGSCWAHASTSAMADRINI-------KRKGAWPSTLLSVQNV 123
Cdd:PTZ00049 372 PHRELEIDELPKNFTW----GDPFNNNTREYDVTNqlLCGSCYIASQMYAFKRRIEIaltknldKKYLNNFDDLLSIQTV 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 124 IDCG--NAGsCEGGNDLSVWDYAHQHGIPDETCNNYQAKDQEC----DKF--------------------NQCGTCNEFK 177
Cdd:PTZ00049 448 LSCSfyDQG-CNGGFPYLVSKMAKLQGIPLDKVFPYTATEQTCpyqvDQSansmngsanlrqinavffssETQSDMHADF 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 178 ECHAIRNYTLWRVGDYGSL---------SGREKMMAEIYANGPISCGIMATERLANYTGGIY-AE--------------- 232
Cdd:PTZ00049 527 EAPISSEPARWYAKDYNYIggcygcnqcNGEKIMMNEIYRNGPIVASFEASPDFYDYADGVYyVEdfpharrctvdlpkh 606
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22538442 233 ---YQDT--TYINHVVSVAGWGIS--DGT--EYWIVRNSWGEPWGERGWLRIVtstykdgKGARYNlAIEEHCTFGDP 301
Cdd:PTZ00049 607 ngvYNITgwEKVNHAIVLVGWGEEeiNGKlyKYWIGRNSWGKNWGKEGYFKII-------RGKNFS-GIESQSLFIEP 676
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
62-302 |
6.42e-165 |
|
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: 457.65 E-value: 6.42e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 62 LPKSWDWRNVDGVNYASITRNQHIPQYCGSCWAHASTSAMADRINIKRKGAWPSTLLSVQNVIDCGNAGSCEGGNDLSVW 141
Cdd:cd02698 1 LPKSWDWRNVNGVNYVSPTRNQHIPQYCGSCWAHGSTSALADRINIARKGAWPSVYLSVQVVIDCAGGGSCHGGDPGGVY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 142 DYAHQHGIPDETCNNYQAKDQECDKFNQCGTCNEFKECHAIRNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATER 221
Cdd:cd02698 81 EYAHKHGIPDETCNPYQAKDGECNPFNRCGTCNPFGECFAIKNYTLYFVSDYGSVSGRDKMMAEIYARGPISCGIMATEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 222 LANYTGGIYAEYQDTTYINHVVSVAGWGISD-GTEYWIVRNSWGEPWGERGWLRIVTSTYkdgKGARYNLAIEEHCTFGD 300
Cdd:cd02698 161 LENYTGGVYKEYVQDPLINHIISVAGWGVDEnGVEYWIVRNSWGEPWGERGWFRIVTSSY---KGARYNLAIEEDCAWAD 237
|
..
gi 22538442 301 PI 302
Cdd:cd02698 238 PI 239
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
62-281 |
1.33e-64 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 202.39 E-value: 1.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 62 LPKSWDWRNVdgvNYASITRNQHipqYCGSCWAHASTSAMADRINIKRKgawPSTLLSVQNVIDC--GNAGsCEGGNDLS 139
Cdd:pfam00112 1 LPESFDWREK---GAVTPVKDQG---QCGSCWAFSAVGALEGRYCIKTG---KLVSLSEQQLVDCdtFNNG-CNGGLPDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 140 VWDYAHQ-HGIPDETCNNYQAKDQECdKFNQCgtcnefkechairNYTLWRVGDYGSLSGR--EKMMAEIYANGPISCGI 216
Cdd:pfam00112 71 AFEYIKKnGGIVTESDYPYTAKDGTC-KFKKS-------------NSKVAKIKGYGDVPYNdeEALQAALAKNGPVSVAI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22538442 217 MATER-LANYTGGIYAEYQDTTYINHVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIVTSTYK 281
Cdd:pfam00112 137 DAYERdFQLYKSGVYKHTECGGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNN 202
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
63-277 |
1.30e-58 |
|
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: 186.68 E-value: 1.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 63 PKSWDWRNVDGVnyaSITRNQhipQYCGSCWAHASTSAMADRINIKRKgawPSTLLSVQNVIDCGNAGS--CEGGNDLSV 140
Cdd:cd02248 1 PESVDWREKGAV---TPVKDQ---GSCGSCWAFSTVGALEGAYAIKTG---KLVSLSEQQLVDCSTSGNngCNGGNPDNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 141 WDYAHQHGIPDETCNNYQAKDQECdkfnqcgtcnefkecHAIRNYTLWRVGDYGSLSGR--EKMMAEIYANGPISCGIMA 218
Cdd:cd02248 72 FEYVKNGGLASESDYPYTGKDGTC---------------KYNSSKVGAKITGYSNVPPGdeEALKAALANYGPVSVAIDA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 219 TERLANYTGGIYAEYQ-DTTYINHVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIVT 277
Cdd:cd02248 137 SSSFQFYKGGIYSGPCcSNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIAR 196
|
|
| Peptidase_C1A_CathepsinB |
cd02620 |
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ... |
81-276 |
3.27e-40 |
|
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: 140.10 E-value: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 81 RNQhipQYCGSCWAHASTSAMADRINIKRKGAWpSTLLSVQNVIDC--GNAGSCEGGNDLSVWDYAHQHGIPDETCNNYQ 158
Cdd:cd02620 20 RDQ---GNCGSCWAFSAVEAFSDRLCIQSNGKE-NVLLSAQDLLSCcsGCGDGCNGGYPDAAWKYLTTTGVVTGGCQPYT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 159 AKDQECdKFNQCGTCNEFKEC---------HAIRNYTLWRVGDYGSLSGREKMMAEIYANGPISCGIMATERLANYTGGI 229
Cdd:cd02620 96 IPPCGH-HPEGPPPCCGTPYCtpkcqdgceKTYEEDKHKGKSAYSVPSDETDIMKEIMTNGPVQAAFTVYEDFLYYKSGV 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 22538442 230 YaeyQDTTYIN---HVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIV 276
Cdd:cd02620 175 Y---QHTSGKQlggHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRIL 221
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
62-281 |
1.28e-38 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 134.25 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 62 LPKSWDWRNVDGVnyaSITRNQHipqYCGSCWAHASTSAMADRINIKRKGawpSTLLSVQNVIDCGNAGS--CEGGNDLS 139
Cdd:smart00645 1 LPESFDWRKKGAV---TPVKDQG---QCGSCWAFSATGALEGRYCIKTGK---LVSLSEQQLVDCSGGGNcgCNGGLPDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 140 VWDYAHQH-GIPDETCNNYQAkdqecdkfnqcgtcnefkechairnytlwrvgdygslsgrekmmaeiyangpiSCGIMA 218
Cdd:smart00645 72 AFEYIKKNgGLETESCYPYTG-----------------------------------------------------SVAIDA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22538442 219 TErLANYTGGIYAEYQDTT-YINHVVSVAGWG--ISDGTEYWIVRNSWGEPWGERGWLRIVTSTYK 281
Cdd:smart00645 99 SD-FQFYKSGIYDHPGCGSgTLDHAVLIVGYGteVENGKDYWIVKNSWGTDWGENGYFRIARGKNN 163
|
|
| Peptidase_C1 |
cd02619 |
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
65-282 |
1.76e-38 |
|
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: 135.33 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 65 SWDWRNVdgvnYASITRNQhipQYCGSCWAHASTSAMADRINIKrKGAWPSTLLSVQNVIDC------GNAGSCEGGNDL 138
Cdd:cd02619 1 SVDLRPL----RLTPVKNQ---GSRGSCWAFASAYALESAYRIK-GGEDEYVDLSPQYLYICandeclGINGSCDGGGPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 139 SVWDYA-HQHGIPDETCNNYQAKDQECDKfnqcgtcnefkECHAIRNYTLWRVGDYGSLSGR--EKMMAEIYANGPISCG 215
Cdd:cd02619 73 SALLKLvALKGIPPEEDYPYGAESDGEEP-----------KSEAALNAAKVKLKDYRRVLKNniEDIKEALAKGGPVVAG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22538442 216 IMATERLANYTGGIYAE------YQDTTYINHVVSVAGWGIS--DGTEYWIVRNSWGEPWGERGWLRIvtsTYKD 282
Cdd:cd02619 142 FDVYSGFDRLKEGIIYEeivyllYEDGDLGGHAVVIVGYDDNyvEGKGAFIVKNSWGTDWGDNGYGRI---SYED 213
|
|
| Peptidase_C1A_CathepsinC |
cd02621 |
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ... |
62-275 |
1.07e-37 |
|
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: 134.05 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 62 LPKSWDWRNV-DGVNYASITRNQHIpqyCGSCWAHASTSAMADRINIKRKGAWP---STLLSVQNVIDCGNAGS-CEGGN 136
Cdd:cd02621 1 LPKSFDWGDVnNGFNYVSPVRNQGG---CGSCYAFASVYALEARIMIASNKTDPlgqQPILSPQHVLSCSQYSQgCDGGF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 137 DLSVWDYAHQHGIPDETCNNYQAKDQecdkfnqcGTCNeFKECHAIRNYT--LWRVGDYGSLSGREKMMAEIYANGPISC 214
Cdd:cd02621 78 PFLVGKFAEDFGIVTEDYFPYTADDD--------RPCK-ASPSECRRYYFsdYNYVGGCYGCTNEDEMKWEIYRNGPIVV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22538442 215 GIMATERLANYTGGIY-----AEYQDT--------TYINHVVSVAGWG--ISDGTEYWIVRNSWGEPWGERGWLRI 275
Cdd:cd02621 149 AFEVYSDFDFYKEGVYhhtdnDEVSDGdndnfnpfELTNHAVLLVGWGedEIKGEKYWIVKNSWGSSWGEKGYFKI 224
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
59-282 |
1.05e-29 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 116.77 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 59 PADLPKSWDWRNvdgvnYASITRNQhipQYCGSCWAHASTSAMADRINIKRKGAWPSTLLSVQNVI-----DCGNAGSCE 133
Cdd:COG4870 1 AAALPSSVDLRG-----YVTPVKDQ---GSLGSCWAFATAAALESYLKKQAGAPGTSLDLSELFLYnqarnGDGTEGTDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 134 GGNDL-SVWDYAHQHGIPDETCNNYQAKDQECDKFNQCgtcnefkechaIRNYTLWRVGDYGSLSGR------EKMMAEI 206
Cdd:COG4870 73 GGSSLrDALKLLRWSGVVPESDWPYDDSDFTSQPSAAA-----------YADARNYKIQDYYRLPGGggatdlDAIKQAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22538442 207 YANGPISCGIMATERLANYTGGIYA-EYQDTTYINHVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIvtsTYKD 282
Cdd:COG4870 142 AEGGPVVFGFYVYESFYNYTGGVYYpTPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI---SYDD 215
|
|
| PTZ00049 |
PTZ00049 |
cathepsin C-like protein; Provisional |
53-301 |
1.27e-26 |
|
cathepsin C-like protein; Provisional
Pssm-ID: 240244 [Multi-domain] Cd Length: 693 Bit Score: 109.66 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 53 PHEYLSPADLPKSWDWrnvdGVNYASITRNQHIPQ--YCGSCWAHASTSAMADRINI-------KRKGAWPSTLLSVQNV 123
Cdd:PTZ00049 372 PHRELEIDELPKNFTW----GDPFNNNTREYDVTNqlLCGSCYIASQMYAFKRRIEIaltknldKKYLNNFDDLLSIQTV 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 124 IDCG--NAGsCEGGNDLSVWDYAHQHGIPDETCNNYQAKDQEC----DKF--------------------NQCGTCNEFK 177
Cdd:PTZ00049 448 LSCSfyDQG-CNGGFPYLVSKMAKLQGIPLDKVFPYTATEQTCpyqvDQSansmngsanlrqinavffssETQSDMHADF 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 178 ECHAIRNYTLWRVGDYGSL---------SGREKMMAEIYANGPISCGIMATERLANYTGGIY-AE--------------- 232
Cdd:PTZ00049 527 EAPISSEPARWYAKDYNYIggcygcnqcNGEKIMMNEIYRNGPIVASFEASPDFYDYADGVYyVEdfpharrctvdlpkh 606
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22538442 233 ---YQDT--TYINHVVSVAGWGIS--DGT--EYWIVRNSWGEPWGERGWLRIVtstykdgKGARYNlAIEEHCTFGDP 301
Cdd:PTZ00049 607 ngvYNITgwEKVNHAIVLVGWGEEeiNGKlyKYWIGRNSWGKNWGKEGYFKII-------RGKNFS-GIESQSLFIEP 676
|
|
| PTZ00200 |
PTZ00200 |
cysteine proteinase; Provisional |
67-284 |
4.67e-24 |
|
cysteine proteinase; Provisional
Pssm-ID: 240310 [Multi-domain] Cd Length: 448 Bit Score: 101.31 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 67 DWRNVDGVNYasiTRNQHIpqYCGSCWAHASTSAMADRINIKRKgawPSTLLSVQNVIDCGN-AGSCEGGNDLSVWDYAH 145
Cdd:PTZ00200 239 DWRRADAVTK---VKDQGL--NCGSCWAFSSVGSVESLYKIYRD---KSVDLSEQELVNCDTkSQGCSGGYPDTALEYVK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 146 QHGIPDETCNNYQAKDqecdkfnqcGTCNEFKechairnYTLWRVGDYGSLSGREkMMAEIYANGPISCGIMATERLANY 225
Cdd:PTZ00200 311 NKGLSSSSDVPYLAKD---------GKCVVSS-------TKKVYIDSYLVAKGKD-VLNKSLVISPTVVYIAVSRELLKY 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22538442 226 TGGIY-AEYQDttYINHVVSVAGWGISDGTE--YWIVRNSWGEPWGERGWLRIVTSTYKDGK 284
Cdd:PTZ00200 374 KSGVYnGECGK--SLNHAVLLVGEGYDEKTKkrYWIIKNSWGTDWGENGYMRLERTNEGTDK 433
|
|
| PTZ00364 |
PTZ00364 |
dipeptidyl-peptidase I precursor; Provisional |
62-275 |
5.77e-22 |
|
dipeptidyl-peptidase I precursor; Provisional
Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 95.73 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 62 LPKSWDWRNVDGVNYASITRNQHIPQYCGSCWAHASTSAMADRINIKRKGAWP---STLLSVQNVIDCGNAGS-CEGGND 137
Cdd:PTZ00364 205 PPAAWSWGDVGGASFLPAAPPASPGRGCNSSYVEAALAAMMARVMVASNRTDPlgqQTFLSARHVLDCSQYGQgCAGGFP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 138 LSVWDYAHQHGIpdETCNNYQAKDQECDKFNQCGTCNEFKECHAIRNYtLWRVGDYGSLSGREKMMAEIYANGPISCGIM 217
Cdd:PTZ00364 285 EEVGKFAETFGI--LTTDSYYIPYDSGDGVERACKTRRPSRRYYFTNY-GPLGGYYGAVTDPDEIIWEIYRHGPVPASVY 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 218 ATERL----ANYTGGIYAEYQDT---------------TYINHVVSVAGWGISD-GTEYWIVRNSWGEP--WGERGWLRI 275
Cdd:PTZ00364 362 ANSDWyncdENSTEDVRYVSLDDystasadrplrhyfaSNVNHTVLIIGWGTDEnGGDYWLVLDPWGSRrsWCDGGTRKI 441
|
|
| PTZ00021 |
PTZ00021 |
falcipain-2; Provisional |
65-277 |
1.00e-18 |
|
falcipain-2; Provisional
Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 85.98 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 65 SWDWRNVDGVnyaSITRNQhipQYCGSCWAHASTSAMADRINIKRKGAwpsTLLSVQNVIDCG--NAGsCEGGN------ 136
Cdd:PTZ00021 269 KYDWRLHNGV---TPVKDQ---KNCGSCWAFSTVGVVESQYAIRKNEL---VSLSEQELVDCSfkNNG-CYGGLipnafe 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 137 ---DL----SVWDYAHQHGIPdETCNnyqakdqecdkFNQCgtcnefKECHAIRNYTlwRVGDygslsgrEKMMAEIYAN 209
Cdd:PTZ00021 339 dmiELgglcSEDDYPYVSDTP-ELCN-----------IDRC------KEKYKIKSYV--SIPE-------DKFKEAIRFL 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22538442 210 GPISCGIMATERLANYTGGIY-AEYQDTTyiNHVVSVAGWGISDGTE----------YWIVRNSWGEPWGERGWLRIVT 277
Cdd:PTZ00021 392 GPISVSIAVSDDFAFYKGGIFdGECGEEP--NHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGFIRIET 468
|
|
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
60-279 |
1.50e-16 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 78.97 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 60 ADL---PKSWDWRNVDGVnyaSITRNQHIpqyCGSCWAHASTSamadriNIKRKGAWPS---TLLSVQNVIDCGNAGS-C 132
Cdd:PTZ00203 121 ADLsavPDAVDWREKGAV---TPVKNQGA---CGSCWAFSAVG------NIESQWAVAGhklVRLSEQQLVSCDHVDNgC 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 133 EGGNDLSVWDYA--HQHGIP-DETCNNYQAKDQECDkfnQCGTCNEFKECHAIRNYTLWRvgdygslSGREKMMAEIYAN 209
Cdd:PTZ00203 189 GGGLMLQAFEWVlrNMNGTVfTEKSYPYVSGNGDVP---ECSNSSELAPGARIDGYVSME-------SSERVMAAWLAKN 258
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22538442 210 GPISCGIMATERLAnYTGGIYAEYqDTTYINHVVSVAGWGISDGTEYWIVRNSWGEPWGERGWLRIVTST 279
Cdd:PTZ00203 259 GPISIAVDASSFMS-YHSGVLTSC-IGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGV 326
|
|
| PTZ00462 |
PTZ00462 |
Serine-repeat antigen protein; Provisional |
240-275 |
5.68e-06 |
|
Serine-repeat antigen protein; Provisional
Pssm-ID: 185641 [Multi-domain] Cd Length: 1004 Bit Score: 47.75 E-value: 5.68e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 22538442 240 NHVVSVAGWG--ISDGTE---YWIVRNSWGEPWGERGWLRI 275
Cdd:PTZ00462 722 DHAVNIVGYGnyINDEDEkksYWIVRNSWGKYWGDEGYFKV 762
|
|
| |
