|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
55-297 |
7.62e-133 |
|
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: 376.37 E-value: 7.62e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 55 IPDSFDWRDVNNTYFVSPVTNQFLPSPCGCCWAHAAVGALTDRMMIATQAKRSIVPLSPQVLLDCAdpDLGSCHGGSALG 134
Cdd:cd02698 1 LPKSWDWRNVNGVNYVSPTRNQHIPQYCGSCWAHGSTSALADRINIARKGAWPSVYLSVQVVIDCA--GGGSCHGGDPGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 135 AYKFIFKNGITDITCSPFMGvdsfywAEVPCNE-TMCRTCDRFGKCSFIK-GPTYFISEYGTVTGEDQMKAEVFARGPIA 212
Cdd:cd02698 79 VYEYAHKHGIPDETCNPYQA------KDGECNPfNRCGTCNPFGECFAIKnYTLYFVSDYGSVSGRDKMMAEIYARGPIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 213 CSVYAHSaAFEEYTGGVIHDPVQYNSTTHVVAVTGWGTDEKtGMKYWIGRNSFGTAWGEDGWFKLQRGV----NALDIEK 288
Cdd:cd02698 153 CGIMATE-ALENYTGGVYKEYVQDPLINHIISVAGWGVDEN-GVEYWIVRNSWGEPWGERGWFRIVTSSykgaRYNLAIE 230
|
....*....
gi 50657031 289 HTCAWAVPK 297
Cdd:cd02698 231 EDCAWADPI 239
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
55-282 |
3.61e-56 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 180.43 E-value: 3.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 55 IPDSFDWRDVNNtyfVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATqakRSIVPLSPQVLLDCADPDLGsCHGGSALG 134
Cdd:pfam00112 1 LPESFDWREKGA---VTPVKDQ---GQCGSCWAFSAVGALEGRYCIKT---GKLVSLSEQQLVDCDTFNNG-CNGGLPDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 135 AYKFIFKN-GITDITCSPFMGVDsfywaevpcnetmcRTCDRFGKcsfiKGPTYFISEYGTVTG--EDQMKAEVFARGPI 211
Cdd:pfam00112 71 AFEYIKKNgGIVTESDYPYTAKD--------------GTCKFKKS----NSKVAKIKGYGDVPYndEEALQAALAKNGPV 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50657031 212 ACSVYAHSAAFEEYTGGVIHDPVQYNSTTHVVAVTGWGTDEktGMKYWIGRNSFGTAWGEDGWFKLQRGVN 282
Cdd:pfam00112 133 SVAIDAYERDFQLYKSGVYKHTECGGELNHAVLLVGYGTEN--GVPYWIVKNSWGTDWGENGYFRIARGVN 201
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
55-282 |
3.52e-40 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 138.10 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 55 IPDSFDWRDVNNtyfVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATQAKrsiVPLSPQVLLDCADPDLGSCHGGSALG 134
Cdd:smart00645 1 LPESFDWRKKGA---VTPVKDQ---GQCGSCWAFSATGALEGRYCIKTGKL---VSLSEQQLVDCSGGGNCGCNGGLPDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 135 AYKFIFKN-GITDITCSPFMGvdsfywaevpcnetmcrtcdrfgkcsfikgptyfiseygtvtgedqmkaevfargpiac 213
Cdd:smart00645 72 AFEYIKKNgGLETESCYPYTG----------------------------------------------------------- 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 214 SVYAHSAAFEEYTGGVIHDP-VQYNSTTHVVAVTGWGTDEKTGMKYWIGRNSFGTAWGEDGWFKLQRGVN 282
Cdd:smart00645 93 SVAIDASDFQFYKSGIYDHPgCGSGTLDHAVLIVGYGTEVENGKDYWIVKNSWGTDWGENGYFRIARGKN 162
|
|
| PTZ00364 |
PTZ00364 |
dipeptidyl-peptidase I precursor; Provisional |
56-287 |
1.27e-29 |
|
dipeptidyl-peptidase I precursor; Provisional
Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 117.68 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 56 PDSFDWRDVNNTYFVSPVTNQFLPSPCGCCWAHAAVGALTDRMMIATQAKRSI---VPLSPQVLLDCADPDLGsCHGGSA 132
Cdd:PTZ00364 206 PAAWSWGDVGGASFLPAAPPASPGRGCNSSYVEAALAAMMARVMVASNRTDPLgqqTFLSARHVLDCSQYGQG-CAGGFP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 133 LGAYKFIFKNGItditcspfMGVDSFYWAEVP--CNETMCRTcDRFGKCSFIKGPTYFISEYGTVTGEDQMKAEVFARGP 210
Cdd:PTZ00364 285 EEVGKFAETFGI--------LTTDSYYIPYDSgdGVERACKT-RRPSRRYYFTNYGPLGGYYGAVTDPDEIIWEIYRHGP 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 211 IACSVYAHSAAF---EEYTGGVIHDPVQYNSTT---------------HVVAVTGWGTDEKTGmKYWIGRNSFGT--AWG 270
Cdd:PTZ00364 356 VPASVYANSDWYncdENSTEDVRYVSLDDYSTAsadrplrhyfasnvnHTVLIIGWGTDENGG-DYWLVLDPWGSrrSWC 434
|
250
....*....|....*..
gi 50657031 271 EDGWFKLQRGVNALDIE 287
Cdd:PTZ00364 435 DGGTRKIARGVNAYNIE 451
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
52-277 |
2.48e-27 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 110.22 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 52 PSVIPDSFDWRDvnntyFVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATQAKRSIVPLSPQVLLDCA---DPDLGSCH 128
Cdd:COG4870 1 AAALPSSVDLRG-----YVTPVKDQ---GSLGSCWAFATAAALESYLKKQAGAPGTSLDLSELFLYNQArngDGTEGTDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 129 GGSAL-GAYKFIFKNGITDITCSPFmgvDSFYWAEVPcnetmcrtcdrfGKCSFIKGPTYFISEYGTVTGE------DQM 201
Cdd:COG4870 73 GGSSLrDALKLLRWSGVVPESDWPY---DDSDFTSQP------------SAAAYADARNYKIQDYYRLPGGggatdlDAI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50657031 202 KAEVFARGPIACSVYAHSAaFEEYTGGVIHDPVQYNSTT-HVVAVTGWgtDEKTGMKYWIGRNSFGTAWGEDGWFKL 277
Cdd:COG4870 138 KQALAEGGPVVFGFYVYES-FYNYTGGVYYPTPGDASLGgHAVAIVGY--DDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
55-297 |
7.62e-133 |
|
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: 376.37 E-value: 7.62e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 55 IPDSFDWRDVNNTYFVSPVTNQFLPSPCGCCWAHAAVGALTDRMMIATQAKRSIVPLSPQVLLDCAdpDLGSCHGGSALG 134
Cdd:cd02698 1 LPKSWDWRNVNGVNYVSPTRNQHIPQYCGSCWAHGSTSALADRINIARKGAWPSVYLSVQVVIDCA--GGGSCHGGDPGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 135 AYKFIFKNGITDITCSPFMGvdsfywAEVPCNE-TMCRTCDRFGKCSFIK-GPTYFISEYGTVTGEDQMKAEVFARGPIA 212
Cdd:cd02698 79 VYEYAHKHGIPDETCNPYQA------KDGECNPfNRCGTCNPFGECFAIKnYTLYFVSDYGSVSGRDKMMAEIYARGPIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 213 CSVYAHSaAFEEYTGGVIHDPVQYNSTTHVVAVTGWGTDEKtGMKYWIGRNSFGTAWGEDGWFKLQRGV----NALDIEK 288
Cdd:cd02698 153 CGIMATE-ALENYTGGVYKEYVQDPLINHIISVAGWGVDEN-GVEYWIVRNSWGEPWGERGWFRIVTSSykgaRYNLAIE 230
|
....*....
gi 50657031 289 HTCAWAVPK 297
Cdd:cd02698 231 EDCAWADPI 239
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
55-282 |
3.61e-56 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 180.43 E-value: 3.61e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 55 IPDSFDWRDVNNtyfVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATqakRSIVPLSPQVLLDCADPDLGsCHGGSALG 134
Cdd:pfam00112 1 LPESFDWREKGA---VTPVKDQ---GQCGSCWAFSAVGALEGRYCIKT---GKLVSLSEQQLVDCDTFNNG-CNGGLPDN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 135 AYKFIFKN-GITDITCSPFMGVDsfywaevpcnetmcRTCDRFGKcsfiKGPTYFISEYGTVTG--EDQMKAEVFARGPI 211
Cdd:pfam00112 71 AFEYIKKNgGIVTESDYPYTAKD--------------GTCKFKKS----NSKVAKIKGYGDVPYndEEALQAALAKNGPV 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50657031 212 ACSVYAHSAAFEEYTGGVIHDPVQYNSTTHVVAVTGWGTDEktGMKYWIGRNSFGTAWGEDGWFKLQRGVN 282
Cdd:pfam00112 133 SVAIDAYERDFQLYKSGVYKHTECGGELNHAVLLVGYGTEN--GVPYWIVKNSWGTDWGENGYFRIARGVN 201
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
56-289 |
1.46e-54 |
|
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: 176.28 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 56 PDSFDWRDVNntyFVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATqakRSIVPLSPQVLLDCADPDLGSCHGGSALGA 135
Cdd:cd02248 1 PESVDWREKG---AVTPVKDQ---GSCGSCWAFSTVGALEGAYAIKT---GKLVSLSEQQLVDCSTSGNNGCNGGNPDNA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 136 YKFIFKNGITDITCSPFMGVDsfywaevpcnetmcrtcdrfGKCSF-IKGPTYFISEYGTVTG--EDQMKAEVFARGPIA 212
Cdd:cd02248 72 FEYVKNGGLASESDYPYTGKD--------------------GTCKYnSSKVGAKITGYSNVPPgdEEALKAALANYGPVS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50657031 213 CSVYAhSAAFEEYTGGVIHDPVQ-YNSTTHVVAVTGWGTDEktGMKYWIGRNSFGTAWGEDGWFKLQRGVNALDIEKH 289
Cdd:cd02248 132 VAIDA-SSSFQFYKGGIYSGPCCsNTNLNHAVLLVGYGTEN--GVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASY 206
|
|
| Peptidase_C1A_CathepsinC |
cd02621 |
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ... |
56-287 |
2.06e-47 |
|
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: 159.09 E-value: 2.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 56 PDSFDWRDVNNTY-FVSPVTNQFLpspCGCCWAHAAVGALTDRMMIATQAKRSIVP---LSPQVLLDCADPDLGsCHGGS 131
Cdd:cd02621 2 PKSFDWGDVNNGFnYVSPVRNQGG---CGSCYAFASVYALEARIMIASNKTDPLGQqpiLSPQHVLSCSQYSQG-CDGGF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 132 ALGAYKFIFKNGITDITCSPFMGVDsfywaEVPCNETMcRTCDRfgkcsfikgptYFISEYGTV------TGEDQMKAEV 205
Cdd:cd02621 78 PFLVGKFAEDFGIVTEDYFPYTADD-----DRPCKASP-SECRR-----------YYFSDYNYVggcygcTNEDEMKWEI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 206 FARGPIACSVYAHSAaFEEYTGGVIH-----DPVQ--------YNSTTHVVAVTGWGTDEKTGMKYWIGRNSFGTAWGED 272
Cdd:cd02621 141 YRNGPIVVAFEVYSD-FDFYKEGVYHhtdndEVSDgdndnfnpFELTNHAVLLVGWGEDEIKGEKYWIVKNSWGSSWGEK 219
|
250
....*....|....*
gi 50657031 273 GWFKLQRGVNALDIE 287
Cdd:cd02621 220 GYFKIRRGTNECGIE 234
|
|
| Peptidase_C1A_CathepsinB |
cd02620 |
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ... |
56-288 |
3.62e-42 |
|
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: 145.11 E-value: 3.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 56 PDSFDWRDV-NNTYFVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATQAKRSiVPLSPQVLLDCADPDLGSCHGGSALG 134
Cdd:cd02620 1 PESFDAREKwPNCISIGEIRDQ---GNCGSCWAFSAVEAFSDRLCIQSNGKEN-VLLSAQDLLSCCSGCGDGCNGGYPDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 135 AYKFIFKNGITDITCSPfmgvdsfYWAEvPCNETMCRTCDRFG------KCSFIKGPTYFI------SEYGTVTGEDQMK 202
Cdd:cd02620 77 AWKYLTTTGVVTGGCQP-------YTIP-PCGHHPEGPPPCCGtpyctpKCQDGCEKTYEEdkhkgkSAYSVPSDETDIM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 203 AEVFARGPI--ACSVYAHsaaFEEYTGGVihdpvqYNSTT------HVVAVTGWGTDEKTgmKYWIGRNSFGTAWGEDGW 274
Cdd:cd02620 149 KEIMTNGPVqaAFTVYED---FLYYKSGV------YQHTSgkqlggHAVKIIGWGVENGV--PYWLAANSWGTDWGENGY 217
|
250
....*....|....
gi 50657031 275 FKLQRGVNALDIEK 288
Cdd:cd02620 218 FRILRGSNECGIES 231
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
55-282 |
3.52e-40 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 138.10 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 55 IPDSFDWRDVNNtyfVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATQAKrsiVPLSPQVLLDCADPDLGSCHGGSALG 134
Cdd:smart00645 1 LPESFDWRKKGA---VTPVKDQ---GQCGSCWAFSATGALEGRYCIKTGKL---VSLSEQQLVDCSGGGNCGCNGGLPDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 135 AYKFIFKN-GITDITCSPFMGvdsfywaevpcnetmcrtcdrfgkcsfikgptyfiseygtvtgedqmkaevfargpiac 213
Cdd:smart00645 72 AFEYIKKNgGLETESCYPYTG----------------------------------------------------------- 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 214 SVYAHSAAFEEYTGGVIHDP-VQYNSTTHVVAVTGWGTDEKTGMKYWIGRNSFGTAWGEDGWFKLQRGVN 282
Cdd:smart00645 93 SVAIDASDFQFYKSGIYDHPgCGSGTLDHAVLIVGYGTEVENGKDYWIVKNSWGTDWGENGYFRIARGKN 162
|
|
| PTZ00364 |
PTZ00364 |
dipeptidyl-peptidase I precursor; Provisional |
56-287 |
1.27e-29 |
|
dipeptidyl-peptidase I precursor; Provisional
Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 117.68 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 56 PDSFDWRDVNNTYFVSPVTNQFLPSPCGCCWAHAAVGALTDRMMIATQAKRSI---VPLSPQVLLDCADPDLGsCHGGSA 132
Cdd:PTZ00364 206 PAAWSWGDVGGASFLPAAPPASPGRGCNSSYVEAALAAMMARVMVASNRTDPLgqqTFLSARHVLDCSQYGQG-CAGGFP 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 133 LGAYKFIFKNGItditcspfMGVDSFYWAEVP--CNETMCRTcDRFGKCSFIKGPTYFISEYGTVTGEDQMKAEVFARGP 210
Cdd:PTZ00364 285 EEVGKFAETFGI--------LTTDSYYIPYDSgdGVERACKT-RRPSRRYYFTNYGPLGGYYGAVTDPDEIIWEIYRHGP 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 211 IACSVYAHSAAF---EEYTGGVIHDPVQYNSTT---------------HVVAVTGWGTDEKTGmKYWIGRNSFGT--AWG 270
Cdd:PTZ00364 356 VPASVYANSDWYncdENSTEDVRYVSLDDYSTAsadrplrhyfasnvnHTVLIIGWGTDENGG-DYWLVLDPWGSrrSWC 434
|
250
....*....|....*..
gi 50657031 271 EDGWFKLQRGVNALDIE 287
Cdd:PTZ00364 435 DGGTRKIARGVNAYNIE 451
|
|
| PTZ00200 |
PTZ00200 |
cysteine proteinase; Provisional |
54-279 |
2.40e-29 |
|
cysteine proteinase; Provisional
Pssm-ID: 240310 [Multi-domain] Cd Length: 448 Bit Score: 115.95 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 54 VIPDSFDWRDVNNtyfVSPVTNQFLPspCGCCWAHAAVGALTDRMMIAtqaKRSIVPLSPQVLLDCadpDLGS--CHGGS 131
Cdd:PTZ00200 233 ITGEGLDWRRADA---VTKVKDQGLN--CGSCWAFSSVGSVESLYKIY---RDKSVDLSEQELVNC---DTKSqgCSGGY 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 132 ALGAYKFIFKNGITDITCSPFMGVDsfywaevpcnetmcrtcdrfGKCSFIKGPTYFISEYGTVTGEDQM-KAEVFarGP 210
Cdd:PTZ00200 302 PDTALEYVKNKGLSSSSDVPYLAKD--------------------GKCVVSSTKKVYIDSYLVAKGKDVLnKSLVI--SP 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50657031 211 iaCSVY-AHSAAFEEYTGGVihdpvqYN-----STTHVVAVTGWGTDEKTGMKYWIGRNSFGTAWGEDGWFKLQR 279
Cdd:PTZ00200 360 --TVVYiAVSRELLKYKSGV------YNgecgkSLNHAVLLVGEGYDEKTKKRYWIIKNSWGTDWGENGYMRLER 426
|
|
| Peptidase_C1 |
cd02619 |
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
58-277 |
1.69e-28 |
|
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: 109.14 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 58 SFDWRDVNNTyfvsPVTNQFlpsPCGCCWAHAAVGALTDRMMIATqAKRSIVPLSPQVLLDCADP----DLGSCHGGSAL 133
Cdd:cd02619 1 SVDLRPLRLT----PVKNQG---SRGSCWAFASAYALESAYRIKG-GEDEYVDLSPQYLYICANDeclgINGSCDGGGPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 134 GAY-KFIFKNGITDITCSPFmgvdsfywaevPCNETMCRTCdrfgkCSFIKGPTYF-ISEYGTVTG--EDQMKAEVFARG 209
Cdd:cd02619 73 SALlKLVALKGIPPEEDYPY-----------GAESDGEEPK-----SEAALNAAKVkLKDYRRVLKnnIEDIKEALAKGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50657031 210 PIACSVYAHSAaFEEYTGGVIHDPVQYNST------THVVAVTGWGTDEKTGMKYWIGRNSFGTAWGEDGWFKL 277
Cdd:cd02619 137 PVVAGFDVYSG-FDRLKEGIIYEEIVYLLYedgdlgGHAVVIVGYDDNYVEGKGAFIVKNSWGTDWGDNGYGRI 209
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
52-277 |
2.48e-27 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 110.22 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 52 PSVIPDSFDWRDvnntyFVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATQAKRSIVPLSPQVLLDCA---DPDLGSCH 128
Cdd:COG4870 1 AAALPSSVDLRG-----YVTPVKDQ---GSLGSCWAFATAAALESYLKKQAGAPGTSLDLSELFLYNQArngDGTEGTDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 129 GGSAL-GAYKFIFKNGITDITCSPFmgvDSFYWAEVPcnetmcrtcdrfGKCSFIKGPTYFISEYGTVTGE------DQM 201
Cdd:COG4870 73 GGSSLrDALKLLRWSGVVPESDWPY---DDSDFTSQP------------SAAAYADARNYKIQDYYRLPGGggatdlDAI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50657031 202 KAEVFARGPIACSVYAHSAaFEEYTGGVIHDPVQYNSTT-HVVAVTGWgtDEKTGMKYWIGRNSFGTAWGEDGWFKL 277
Cdd:COG4870 138 KQALAEGGPVVFGFYVYES-FYNYTGGVYYPTPGDASLGgHAVAIVGY--DDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
53-297 |
1.71e-26 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 106.71 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 53 SVIPDSFDWRDVNNtyfVSPVTNQflpSPCGCCWAHAAVGALTDRMMIATQakrSIVPLSPQVLLDCADPDLGsCHGGSA 132
Cdd:PTZ00203 124 SAVPDAVDWREKGA---VTPVKNQ---GACGSCWAFSAVGNIESQWAVAGH---KLVRLSEQQLVSCDHVDNG-CGGGLM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 133 LGAYKFIFKN--GITDITCS-PFMGVDsfywAEVPcnetMCRTCDRFGKCSFIKGptYFISEygtvTGEDQMKAEVFARG 209
Cdd:PTZ00203 194 LQAFEWVLRNmnGTVFTEKSyPYVSGN----GDVP----ECSNSSELAPGARIDG--YVSME----SSERVMAAWLAKNG 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 210 PIACSVYAhsAAFEEYTGGVIHDPVQYNSTTHVVAVtgwGTDEKTGMKYWIGRNSFGTAWGEDGWFKLQRGVNALDIEKH 289
Cdd:PTZ00203 260 PISIAVDA--SSFMSYHSGVLTSCIGEQLNHGVLLV---GYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGY 334
|
....*...
gi 50657031 290 TCAWAVPK 297
Cdd:PTZ00203 335 PVSVHVSQ 342
|
|
| PTZ00049 |
PTZ00049 |
cathepsin C-like protein; Provisional |
42-290 |
6.65e-25 |
|
cathepsin C-like protein; Provisional
Pssm-ID: 240244 [Multi-domain] Cd Length: 693 Bit Score: 104.26 E-value: 6.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 42 VTKPPHQKLNPSVIPDSFDWRD-VNNTYFVSPVTNQFLpspCGCCWAHAAVGALTDRMMIATQAK--RSIVP-----LSP 113
Cdd:PTZ00049 368 TEKAPHRELEIDELPKNFTWGDpFNNNTREYDVTNQLL---CGSCYIASQMYAFKRRIEIALTKNldKKYLNnfddlLSI 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 114 QVLLDCADPDLGsCHGGSALGAYKFIFKNGITDITCSPFMG--------VDSFYWAEVPCNETMCRTCDRFGK------- 178
Cdd:PTZ00049 445 QTVLSCSFYDQG-CNGGFPYLVSKMAKLQGIPLDKVFPYTAteqtcpyqVDQSANSMNGSANLRQINAVFFSSetqsdmh 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 179 -------CS-----FIKGPTYFISEYGT--VTGEDQMKAEVFARGPIACSVYAhSAAFEEYTGGV--------------- 229
Cdd:PTZ00049 524 adfeapiSSeparwYAKDYNYIGGCYGCnqCNGEKIMMNEIYRNGPIVASFEA-SPDFYDYADGVyyvedfpharrctvd 602
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50657031 230 ------IHDPVQYNSTTHVVAVTGWGTDEKTG--MKYWIGRNSFGTAWGEDGWFKLQRGVNALDIEKHT 290
Cdd:PTZ00049 603 lpkhngVYNITGWEKVNHAIVLVGWGEEEINGklYKYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQS 671
|
|
| PTZ00021 |
PTZ00021 |
falcipain-2; Provisional |
58-291 |
1.46e-20 |
|
falcipain-2; Provisional
Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 91.37 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 58 SFDWRDVNNtyfVSPVTNQFLpspCGCCWAHAAVGALTDRMMIAtqaKRSIVPLSPQVLLDCADPDLGsCHGGSALGAYK 137
Cdd:PTZ00021 269 KYDWRLHNG---VTPVKDQKN---CGSCWAFSTVGVVESQYAIR---KNELVSLSEQELVDCSFKNNG-CYGGLIPNAFE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 138 -FIFKNGItditCSpfmGVDSFYWAEVP--CNETMCRtcDRFGKCSFIKGPtyfiseygtvtgEDQMKAEVFARGPIACS 214
Cdd:PTZ00021 339 dMIELGGL----CS---EDDYPYVSDTPelCNIDRCK--EKYKIKSYVSIP------------EDKFKEAIRFLGPISVS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 215 VyAHSAAFEEYTGGvIHDPVQYNSTTHVVAVTGWGTDE------KTGMK--YWIGRNSFGTAWGEDGWFKLQRGVNALdi 286
Cdd:PTZ00021 398 I-AVSDDFAFYKGG-IFDGECGEEPNHAVILVGYGMEEiynsdtKKMEKryYYIIKNSWGESWGEKGFIRIETDENGL-- 473
|
....*
gi 50657031 287 eKHTC 291
Cdd:PTZ00021 474 -MKTC 477
|
|
| PTZ00462 |
PTZ00462 |
Serine-repeat antigen protein; Provisional |
201-277 |
3.32e-07 |
|
Serine-repeat antigen protein; Provisional
Pssm-ID: 185641 [Multi-domain] Cd Length: 1004 Bit Score: 51.60 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50657031 201 MKAEVFARGPIACSVYAHSAAFEEYTGGVIHDPVQYNSTTHVVAVTGWGT---DEKTGMKYWIGRNSFGTAWGEDGWFKL 277
Cdd:PTZ00462 683 IKDEIMNKGSVIAYIKAENVLGYEFNGKKVQNLCGDDTADHAVNIVGYGNyinDEDEKKSYWIVRNSWGKYWGDEGYFKV 762
|
|
| |
