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Conserved domains on  [gi|22538442|ref|NP_001327|]
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cathepsin Z preproprotein [Homo sapiens]

Protein Classification

C1 family peptidase( domain architecture ID 10119592)

C1 family peptidase (also called papain family protein) may be an endopeptidase or an exopeptidase, and catalyzes the hydrolysis of peptide bonds in substrates using a catalytic dyad of Cys and His residues; similar to Homo sapiens cathepsin Z

CATH:  3.90.70.10
Gene Ontology:  GO:0008234|GO:0006508
MEROPS:  C1
PubMed:  12887050|11517925
SCOP:  4000859

Graphical summary

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List of domain hits

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
 
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
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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