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Conserved domains on  [gi|384081596|ref|NP_001244902|]
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procathepsin L isoform 2 [Homo sapiens]

Protein Classification

C1 family peptidase( domain architecture ID 11085187)

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

CATH:  3.90.70.10
EC:  3.4.-.-
Gene Ontology:  GO:0008234|GO:0006508
MEROPS:  C1
PubMed:  12887050|11517925|8439290|7845226
SCOP:  4000859

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
1-150 5.89e-72

Papain family cysteine protease;


:

Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 214.71  E-value: 5.89e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596    1 MDYAFQYVQDNGGLDSEESYPYEATEESCKYNP-KYSVANDTGFVDIPKQ-EKALMKAVATVGPISVAIDAGHESFLFYK 78
Cdd:pfam00112  68 PDNAFEYIKKNGGIVTESDYPYTAKDGTCKFKKsNSKVAKIKGYGDVPYNdEEALQAALAKNGPVSVAIDAYERDFQLYK 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384081596   79 EGIYFEPDCSSEdMDHGVLVVGYGFEstesDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPT 150
Cdd:pfam00112 148 SGVYKHTECGGE-LNHAVLLVGYGTE----NGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
1-150 5.89e-72

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 214.71  E-value: 5.89e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596    1 MDYAFQYVQDNGGLDSEESYPYEATEESCKYNP-KYSVANDTGFVDIPKQ-EKALMKAVATVGPISVAIDAGHESFLFYK 78
Cdd:pfam00112  68 PDNAFEYIKKNGGIVTESDYPYTAKDGTCKFKKsNSKVAKIKGYGDVPYNdEEALQAALAKNGPVSVAIDAYERDFQLYK 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384081596   79 EGIYFEPDCSSEdMDHGVLVVGYGFEstesDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPT 150
Cdd:pfam00112 148 SGVYKHTECGGE-LNHAVLLVGYGTE----NGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 1-149 3.06e-66

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: 200.16  E-value: 3.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   1 MDYAFQYVQdNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPK-QEKALMKAVATVGPISVAIDAGHeSFLFYKE 79
Cdd:cd02248   68 PDNAFEYVK-NGGLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASS-SFQFYKG 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  80 GIYFEPDCSSEDMDHGVLVVGYGFEstesDNNKYWLVKNSWGEEWGMGGYVKMAKDrRNHCGIASAASYP 149
Cdd:cd02248  146 GIYSGPCCSNTNLNHAVLLVGYGTE----NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
1-149 8.19e-45

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 144.65  E-value: 8.19e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596     1 MDYAFQYVQDNGGLDSEESYPYEAteesckynpkysvandtgfvdipkqekalmkavatvgpiSVAIDAGHesFLFYKEG 80
Cdd:smart00645  69 PDNAFEYIKKNGGLETESCYPYTG---------------------------------------SVAIDASD--FQFYKSG 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596    81 IYFEPDCSSEDMDHGVLVVGYGFESteSDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGI-ASAASYP 149
Cdd:smart00645 108 IYDHPGCGSGTLDHAVLIVGYGTEV--ENGKDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
PTZ00021 PTZ00021
falcipain-2; Provisional
 4-151 3.24e-24

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 96.76  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   4 AFQYVQDNGGLDSEESYPYEA-TEESCKY---NPKYSVANdtgFVDIPkqEKALMKAVATVGPISVAIdAGHESFLFYKE 79
Cdd:PTZ00021 336 AFEDMIELGGLCSEDDYPYVSdTPELCNIdrcKEKYKIKS---YVSIP--EDKFKEAIRFLGPISVSI-AVSDDFAFYKG 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  80 GIyFEPDCSsEDMDHGVLVVGYGFEST-ESDNNK-----YWLVKNSWGEEWGMGGYVKMAKDR---RNHCGIASAASYPT 150
Cdd:PTZ00021 410 GI-FDGECG-EEPNHAVILVGYGMEEIyNSDTKKmekryYYIIKNSWGESWGEKGFIRIETDEnglMKTCSLGTEAYVPL 487


                 .
gi 384081596 151 V 151
Cdd:PTZ00021 488 I 488
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
13-132 1.45e-15

Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 72.47  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  13 GLDSEESYPYEATEESCKYNPK-YSVAND---TGFVDIPKQE-----KALMKAVATVGPISVAIdAGHESFLFYKEGIYF 83
Cdd:COG4870   88 GVVPESDWPYDDSDFTSQPSAAaYADARNykiQDYYRLPGGGgatdlDAIKQALAEGGPVVFGF-YVYESFYNYTGGVYY 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 384081596  84 EPDCSSEDMDHGVLVVGYgfesTESDNNKYWLVKNSWGEEWGMGGYVKM 132
Cdd:COG4870  167 PTPGDASLGGHAVAIVGY----DDNYSDGAFIIKNSWGTGWGDNGYFWI 211
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
1-150 5.89e-72

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 214.71  E-value: 5.89e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596    1 MDYAFQYVQDNGGLDSEESYPYEATEESCKYNP-KYSVANDTGFVDIPKQ-EKALMKAVATVGPISVAIDAGHESFLFYK 78
Cdd:pfam00112  68 PDNAFEYIKKNGGIVTESDYPYTAKDGTCKFKKsNSKVAKIKGYGDVPYNdEEALQAALAKNGPVSVAIDAYERDFQLYK 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384081596   79 EGIYFEPDCSSEdMDHGVLVVGYGFEstesDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGIASAASYPT 150
Cdd:pfam00112 148 SGVYKHTECGGE-LNHAVLLVGYGTE----NGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 1-149 3.06e-66

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: 200.16  E-value: 3.06e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   1 MDYAFQYVQdNGGLDSEESYPYEATEESCKYNPKYSVANDTGFVDIPK-QEKALMKAVATVGPISVAIDAGHeSFLFYKE 79
Cdd:cd02248   68 PDNAFEYVK-NGGLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASS-SFQFYKG 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  80 GIYFEPDCSSEDMDHGVLVVGYGFEstesDNNKYWLVKNSWGEEWGMGGYVKMAKDrRNHCGIASAASYP 149
Cdd:cd02248  146 GIYSGPCCSNTNLNHAVLLVGYGTE----NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
1-149 8.19e-45

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 144.65  E-value: 8.19e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596     1 MDYAFQYVQDNGGLDSEESYPYEAteesckynpkysvandtgfvdipkqekalmkavatvgpiSVAIDAGHesFLFYKEG 80
Cdd:smart00645  69 PDNAFEYIKKNGGLETESCYPYTG---------------------------------------SVAIDASD--FQFYKSG 107

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596    81 IYFEPDCSSEDMDHGVLVVGYGFESteSDNNKYWLVKNSWGEEWGMGGYVKMAKDRRNHCGI-ASAASYP 149
Cdd:smart00645 108 IYDHPGCGSGTLDHAVLIVGYGTEV--ENGKDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
PTZ00021 PTZ00021
falcipain-2; Provisional
 4-151 3.24e-24

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 96.76  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   4 AFQYVQDNGGLDSEESYPYEA-TEESCKY---NPKYSVANdtgFVDIPkqEKALMKAVATVGPISVAIdAGHESFLFYKE 79
Cdd:PTZ00021 336 AFEDMIELGGLCSEDDYPYVSdTPELCNIdrcKEKYKIKS---YVSIP--EDKFKEAIRFLGPISVSI-AVSDDFAFYKG 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  80 GIyFEPDCSsEDMDHGVLVVGYGFEST-ESDNNK-----YWLVKNSWGEEWGMGGYVKMAKDR---RNHCGIASAASYPT 150
Cdd:PTZ00021 410 GI-FDGECG-EEPNHAVILVGYGMEEIyNSDTKKmekryYYIIKNSWGESWGEKGFIRIETDEnglMKTCSLGTEAYVPL 487


                 .
gi 384081596 151 V 151
Cdd:PTZ00021 488 I 488
PTZ00200 PTZ00200
cysteine proteinase; Provisional
 2-144 8.35e-23

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 92.84  E-value: 8.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   2 DYAFQYVQdNGGLDSEESYPYEATEESCKY--NPKYSVANDTGFVDIPKQEKALmkavaTVGPISVAIdAGHESFLFYKE 79
Cdd:PTZ00200 303 DTALEYVK-NKGLSSSSDVPYLAKDGKCVVssTKKVYIDSYLVAKGKDVLNKSL-----VISPTVVYI-AVSRELLKYKS 375

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384081596  80 GIYfEPDCSSEdMDHGVLVVGYGFEstESDNNKYWLVKNSWGEEWGMGGYVKMA--KDRRNHCGIAS 144
Cdd:PTZ00200 376 GVY-NGECGKS-LNHAVLLVGEGYD--EKTKKRYWIIKNSWGTDWGENGYMRLErtNEGTDKCGILT 438
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 1-134 1.43e-22

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 91.30  E-value: 1.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   1 MDYAFQYVQDN--GGLDSEESYPYEATEES---CKYNPKYSV-ANDTGFVDIPKQEKALMKAVATVGPISVAIDAghESF 74
Cdd:PTZ00203 193 MLQAFEWVLRNmnGTVFTEKSYPYVSGNGDvpeCSNSSELAPgARIDGYVSMESSERVMAAWLAKNGPISIAVDA--SSF 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  75 LFYKEGIYfePDCSSEDMDHGVLVVGYgfesTESDNNKYWLVKNSWGEEWGMGGYVKMAK 134
Cdd:PTZ00203 271 MSYHSGVL--TSCIGEQLNHGVLLVGY----NMTGEVPYWVIKNSWGEDWGEKGYVRVTM 324
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
 4-142 4.26e-20

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: 82.70  E-value: 4.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   4 AFQYVQDNGgLDSEESYPYEA--------------TEESC------KYNPKYSvaNDTGFVD----IPKQEKALMKAVAT 59
Cdd:cd02620   77 AWKYLTTTG-VVTGGCQPYTIppcghhpegpppccGTPYCtpkcqdGCEKTYE--EDKHKGKsaysVPSDETDIMKEIMT 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  60 VGPISVAIDAgHESFLFYKEGIYFEpdcSSEDMD--HGVLVVGYGFESTEsdnnKYWLVKNSWGEEWGMGGYVKMAKDrR 137
Cdd:cd02620  154 NGPVQAAFTV-YEDFLYYKSGVYQH---TSGKQLggHAVKIIGWGVENGV----PYWLAANSWGTDWGENGYFRILRG-S 224


                 ....*
gi 384081596 138 NHCGI 142
Cdd:cd02620  225 NECGI 229
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
 7-146 1.56e-19

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: 81.28  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   7 YVQDNGgLDSEESYPYEA-TEESCKYNPKYSV---ANDTGFVDI---PKQEKALMKAVATVGPISVAIDAgHESFLFYKE 79
Cdd:cd02621   84 FAEDFG-IVTEDYFPYTAdDDRPCKASPSECRryyFSDYNYVGGcygCTNEDEMKWEIYRNGPIVVAFEV-YSDFDFYKE 161

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384081596  80 GIYF-EPDCSSEDMD-----------HGVLVVGYGFEstESDNNKYWLVKNSWGEEWGMGGYVKMAKDrRNHCGIASAA 146
Cdd:cd02621  162 GVYHhTDNDEVSDGDndnfnpfeltnHAVLLVGWGED--EIKGEKYWIVKNSWGSSWGEKGYFKIRRG-TNECGIESQA 237
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 13-132 7.07e-18

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: 76.78  E-value: 7.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  13 GLDSEESYPYEATEESCKYNP----KYSVANDTGFVDI-PKQEKALMKAVATVGPISVAIDAgHESFLFYKEGIY----- 82
Cdd:cd02619   83 GIPPEEDYPYGAESDGEEPKSeaalNAAKVKLKDYRRVlKNNIEDIKEALAKGGPVVAGFDV-YSGFDRLKEGIIyeeiv 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 384081596  83 FEPDCSSEDMDHGVLVVGYGFEstESDNNKYWLVKNSWGEEWGMGGYVKM 132
Cdd:cd02619  162 YLLYEDGDLGGHAVVIVGYDDN--YVEGKGAFIVKNSWGTDWGDNGYGRI 209
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
 4-133 7.04e-17

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: 74.37  E-value: 7.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   4 AFQYVQDNGGLDsEESYPYEATEESC-KYN-----------------PKYSVAnDTGFVdipKQEKALMKAVATVGPISV 65
Cdd:cd02698   79 VYEYAHKHGIPD-ETCNPYQAKDGECnPFNrcgtcnpfgecfaiknyTLYFVS-DYGSV---SGRDKMMAEIYARGPISC 153

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384081596  66 AIDAgHESFLFYKEGIYFEPDcSSEDMDHGVLVVGYGfesTESDNNKYWLVKNSWGEEWGMGGYVKMA 133
Cdd:cd02698  154 GIMA-TEALENYTGGVYKEYV-QDPLINHIISVAGWG---VDENGVEYWIVRNSWGEPWGERGWFRIV 216
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
13-132 1.45e-15

Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 72.47  E-value: 1.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  13 GLDSEESYPYEATEESCKYNPK-YSVAND---TGFVDIPKQE-----KALMKAVATVGPISVAIdAGHESFLFYKEGIYF 83
Cdd:COG4870   88 GVVPESDWPYDDSDFTSQPSAAaYADARNykiQDYYRLPGGGgatdlDAIKQALAEGGPVVFGF-YVYESFYNYTGGVYY 166

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 384081596  84 EPDCSSEDMDHGVLVVGYgfesTESDNNKYWLVKNSWGEEWGMGGYVKM 132
Cdd:COG4870  167 PTPGDASLGGHAVAIVGY----DDNYSDGAFIIKNSWGTGWGDNGYFWI 211
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
 50-148 1.85e-14

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 69.21  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596  50 EKALMKAVATVGPISVAIDAGhESFLFYKEGIYFEPD------CSSED--------------MDHGVLVVGYGFESTESD 109
Cdd:PTZ00049 557 EKIMMNEIYRNGPIVASFEAS-PDFYDYADGVYYVEDfpharrCTVDLpkhngvynitgwekVNHAIVLVGWGEEEINGK 635

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 384081596 110 NNKYWLVKNSWGEEWGMGGYVKMAKDrRNHCGIASAASY 148
Cdd:PTZ00049 636 LYKYWIGRNSWGKNWGKEGYFKIIRG-KNFSGIESQSLF 673
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
 5-140 8.30e-10

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 55.84  E-value: 8.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596    5 FQYVQDNGGLDSEESYPYEATE--ESC-----------------KYNPKYSVANDT----------------GFVDIPKQ 49
Cdd:PTZ00462  606 LQIIEDNGFLPADSNYLYNYTKvgEDCpdeedhwmnlldhgkilNHNKKEPNSLDGkayrayesehfhdkmdAFIKIIKD 685

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384081596   50 EkalmkaVATVGPISVAIDAghESFLFYK-EGIYFEPDCSSEDMDHGVLVVGYG-FESTESDNNKYWLVKNSWGEEWGMG 127
Cdd:PTZ00462  686 E------IMNKGSVIAYIKA--ENVLGYEfNGKKVQNLCGDDTADHAVNIVGYGnYINDEDEKKSYWIVRNSWGKYWGDE 757

                         170
                  ....*....|...
gi 384081596  128 GYVKMAKDRRNHC 140
Cdd:PTZ00462  758 GYFKVDMYGPSHC 770
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 90-145 5.05e-06

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 44.88  E-value: 5.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384081596  90 EDMDHGVLVVGYGfesTESDNNKYWLVKNSWGEE--WGMGGYVKMAKDrRNHCGIASA 145
Cdd:PTZ00364 400 SNVNHTVLIIGWG---TDENGGDYWLVLDPWGSRrsWCDGGTRKIARG-VNAYNIESE 453
 
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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