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Conserved domains on  [gi|982742431|ref|NP_001306066|]
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pro-cathepsin H isoform c [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
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;
32-198 1.90e-77

Papain family cysteine protease;


:

Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 230.89  E-value: 1.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431   32 EQQLVDCaqDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKF-QPGKAIGFVKDVANITIYDEEAMVEAVA 110
Cdd:pfam00112  50 EQQLVDC--DTFNNGCNGGLPDNAFEYIKKNGGIVTESDYPYTAKDGTCKFkKSNSKVAKIKGYGDVPYNDEEALQAALA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  111 LYNPVSFAFEVTQ-DFMMYRTGIYSSTSCHKtpdKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKN-MC 188
Cdd:pfam00112 128 KNGPVSVAIDAYErDFQLYKSGVYKHTECGG---ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnEC 204
                         170
                  ....*....|
gi 982742431  189 GLAACASYPI 198
Cdd:pfam00112 205 GIASEASYPI 214
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
32-198 1.90e-77

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 230.89  E-value: 1.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431   32 EQQLVDCaqDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKF-QPGKAIGFVKDVANITIYDEEAMVEAVA 110
Cdd:pfam00112  50 EQQLVDC--DTFNNGCNGGLPDNAFEYIKKNGGIVTESDYPYTAKDGTCKFkKSNSKVAKIKGYGDVPYNDEEALQAALA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  111 LYNPVSFAFEVTQ-DFMMYRTGIYSSTSCHKtpdKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKN-MC 188
Cdd:pfam00112 128 KNGPVSVAIDAYErDFQLYKSGVYKHTECGG---ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnEC 204
                         170
                  ....*....|
gi 982742431  189 GLAACASYPI 198
Cdd:pfam00112 205 GIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
32-197 4.16e-77

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: 229.82  E-value: 4.16e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  32 EQQLVDCAQDFNNhGCQGGLPSQAFEYIlYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVAL 111
Cdd:cd02248   49 EQQLVDCSTSGNN-GCNGGNPDNAFEYV-KNGGLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALAN 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431 112 YNPVSFAFEVTQDFMMYRTGIYSSTSChkTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLA 191
Cdd:cd02248  127 YGPVSVAIDASSSFQFYKGGIYSGPCC--SNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIA 204

                 ....*.
gi 982742431 192 ACASYP 197
Cdd:cd02248  205 SYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
32-197 1.52e-49

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 158.51  E-value: 1.52e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431    32 EQQLVDCAQDFNNhGCQGGLPSQAFEYILYNKGIMGEDTYPYQGkdgyckfqpgkaigfvkdvanitiydeeamveaval 111
Cdd:smart00645  50 EQQLVDCSGGGNC-GCNGGLPDNAFEYIKKNGGLETESCYPYTG------------------------------------ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431   112 ynpvsFAFEVTQDFMMYRTGIYSSTSChkTPDKVNHAVLAVGYGEK--NGIPYWIVKNSWGPQWGMNGYFLIERGK-NMC 188
Cdd:smart00645  93 -----SVAIDASDFQFYKSGIYDHPGC--GSGTLDHAVLIVGYGTEveNGKDYWIVKNSWGTDWGENGYFRIARGKnNEC 165
                          170
                   ....*....|
gi 982742431   189 GL-AACASYP 197
Cdd:smart00645 166 GIeASVASYP 175
PTZ00200 PTZ00200
cysteine proteinase; Provisional
26-190 9.25e-39

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 137.90  E-value: 9.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  26 VSFFQAEQQLVDCaqDFNNHGCQGGLPSQAFEYIlYNKGIMGEDTYPYQGKDGYC-------KFQPGKAIGFVKDVANIT 98
Cdd:PTZ00200 278 KSVDLSEQELVNC--DTKSQGCSGGYPDTALEYV-KNKGLSSSSDVPYLAKDGKCvvsstkkVYIDSYLVAKGKDVLNKS 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  99 IydeeamveavaLYNPVSFAFEVTQDFMMYRTGIYSStSCHKTPdkvNHAVLAVG--YGEKNGIPYWIVKNSWGPQWGMN 176
Cdd:PTZ00200 355 L-----------VISPTVVYIAVSRELLKYKSGVYNG-ECGKSL---NHAVLLVGegYDEKTKKRYWIIKNSWGTDWGEN 419
                        170
                 ....*....|....*..
gi 982742431 177 GYFLIER---GKNMCGL 190
Cdd:PTZ00200 420 GYMRLERtneGTDKCGI 436
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
47-181 2.74e-22

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 92.89  E-value: 2.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  47 CQGGLPSQAFeYILYNKGIMGEDTYPYQGKDGYCK---FQPGKAIGF-VKDVANIT----IYDEEAMVEAVALYNPVSFA 118
Cdd:COG4870   72 DGGSSLRDAL-KLLRWSGVVPESDWPYDDSDFTSQpsaAAYADARNYkIQDYYRLPggggATDLDAIKQALAEGGPVVFG 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982742431 119 FEVTQDFMMYRTGIYSSTSchKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLI 181
Cdd:COG4870  151 FYVYESFYNYTGGVYYPTP--GDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
32-198 1.90e-77

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 230.89  E-value: 1.90e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431   32 EQQLVDCaqDFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKF-QPGKAIGFVKDVANITIYDEEAMVEAVA 110
Cdd:pfam00112  50 EQQLVDC--DTFNNGCNGGLPDNAFEYIKKNGGIVTESDYPYTAKDGTCKFkKSNSKVAKIKGYGDVPYNDEEALQAALA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  111 LYNPVSFAFEVTQ-DFMMYRTGIYSSTSCHKtpdKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKN-MC 188
Cdd:pfam00112 128 KNGPVSVAIDAYErDFQLYKSGVYKHTECGG---ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnEC 204
                         170
                  ....*....|
gi 982742431  189 GLAACASYPI 198
Cdd:pfam00112 205 GIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
32-197 4.16e-77

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: 229.82  E-value: 4.16e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  32 EQQLVDCAQDFNNhGCQGGLPSQAFEYIlYNKGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVAL 111
Cdd:cd02248   49 EQQLVDCSTSGNN-GCNGGNPDNAFEYV-KNGGLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALAN 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431 112 YNPVSFAFEVTQDFMMYRTGIYSSTSChkTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLA 191
Cdd:cd02248  127 YGPVSVAIDASSSFQFYKGGIYSGPCC--SNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIA 204

                 ....*.
gi 982742431 192 ACASYP 197
Cdd:cd02248  205 SYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
32-197 1.52e-49

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 158.51  E-value: 1.52e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431    32 EQQLVDCAQDFNNhGCQGGLPSQAFEYILYNKGIMGEDTYPYQGkdgyckfqpgkaigfvkdvanitiydeeamveaval 111
Cdd:smart00645  50 EQQLVDCSGGGNC-GCNGGLPDNAFEYIKKNGGLETESCYPYTG------------------------------------ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431   112 ynpvsFAFEVTQDFMMYRTGIYSSTSChkTPDKVNHAVLAVGYGEK--NGIPYWIVKNSWGPQWGMNGYFLIERGK-NMC 188
Cdd:smart00645  93 -----SVAIDASDFQFYKSGIYDHPGC--GSGTLDHAVLIVGYGTEveNGKDYWIVKNSWGTDWGENGYFRIARGKnNEC 165
                          170
                   ....*....|
gi 982742431   189 GL-AACASYP 197
Cdd:smart00645 166 GIeASVASYP 175
PTZ00200 PTZ00200
cysteine proteinase; Provisional
26-190 9.25e-39

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 137.90  E-value: 9.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  26 VSFFQAEQQLVDCaqDFNNHGCQGGLPSQAFEYIlYNKGIMGEDTYPYQGKDGYC-------KFQPGKAIGFVKDVANIT 98
Cdd:PTZ00200 278 KSVDLSEQELVNC--DTKSQGCSGGYPDTALEYV-KNKGLSSSSDVPYLAKDGKCvvsstkkVYIDSYLVAKGKDVLNKS 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  99 IydeeamveavaLYNPVSFAFEVTQDFMMYRTGIYSStSCHKTPdkvNHAVLAVG--YGEKNGIPYWIVKNSWGPQWGMN 176
Cdd:PTZ00200 355 L-----------VISPTVVYIAVSRELLKYKSGVYNG-ECGKSL---NHAVLLVGegYDEKTKKRYWIIKNSWGTDWGEN 419
                        170
                 ....*....|....*..
gi 982742431 177 GYFLIER---GKNMCGL 190
Cdd:PTZ00200 420 GYMRLERtneGTDKCGI 436
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
33-190 7.11e-37

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: 128.16  E-value: 7.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  33 QQLVDCAqDFNNHGCQGGLPSQAFEYiLYNKGIMGEDTYPYQ--------------GKDGYC--KFQPGKAIGFVKDVA- 95
Cdd:cd02620   56 QDLLSCC-SGCGDGCNGGYPDAAWKY-LTTTGVVTGGCQPYTippcghhpegpppcCGTPYCtpKCQDGCEKTYEEDKHk 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  96 NITIY----DEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSstscHKTPDKVN-HAVLAVGYGEKNGIPYWIVKNSWG 170
Cdd:cd02620  134 GKSAYsvpsDETDIMKEIMTNGPVQAAFTVYEDFLYYKSGVYQ----HTSGKQLGgHAVKIIGWGVENGVPYWLAANSWG 209
                        170       180
                 ....*....|....*....|
gi 982742431 171 PQWGMNGYFLIERGKNMCGL 190
Cdd:cd02620  210 TDWGENGYFRILRGSNECGI 229
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
33-198 1.92e-34

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: 122.11  E-value: 1.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  33 QQLVDCAQdfNNHGCQGGLPSQAFEYIlYNKGIMGEDTYPYQG-KDGYCKFQP-GKAIGFVKDVANITIY----DEEAMV 106
Cdd:cd02621   61 QHVLSCSQ--YSQGCDGGFPFLVGKFA-EDFGIVTEDYFPYTAdDDRPCKASPsECRRYYFSDYNYVGGCygctNEDEMK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431 107 EAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPD----------KVNHAVLAVGYGE--KNGIPYWIVKNSWGPQWG 174
Cdd:cd02621  138 WEIYRNGPIVVAFEVYSDFDFYKEGVYHHTDNDEVSDgdndnfnpfeLTNHAVLLVGWGEdeIKGEKYWIVKNSWGSSWG 217
                        170       180
                 ....*....|....*....|....*.
gi 982742431 175 MNGYFLIERGKNMCGL--AACASYPI 198
Cdd:cd02621  218 EKGYFKIRRGTNECGIesQAVFAYPI 243
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
12-196 4.23e-33

C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; composed of two subfamilies of cysteine peptidases (CPs), C1A (papain) and C1B (bleomycin hydrolase). Papain-like enzymes are mostly endopeptidases with some exceptions like cathepsins B, C, H and X, which are exopeptidases. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds while mammalian CPs are primarily lysosomal enzymes responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. Bleomycin hydrolase (BH) is a CP that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. It forms a hexameric ring barrel structure with the active sites imbedded in the central channel. Some members of the C1 family are proteins classified as non-peptidase homologs which lack peptidase activity or have missing active site residues.


Pssm-ID: 239110 [Multi-domain]  Cd Length: 223  Bit Score: 118.00  E-value: 4.23e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  12 AKALTASQLAGHWVVSFFQ-AEQQLVDCAQDF---NNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQGKDGYCKFQPGKA 87
Cdd:cd02619   27 AYALESAYRIKGGEDEYVDlSPQYLYICANDEclgINGSCDGGGPLSALLKLVALKGIPPEEDYPYGAESDGEEPKSEAA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  88 --IGFVKDVAN--ITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPDKV---NHAVLAVGYG--EKN 158
Cdd:cd02619  107 lnAAKVKLKDYrrVLKNNIEDIKEALAKGGPVVAGFDVYSGFDRLKEGIIYEEIVYLLYEDGdlgGHAVVIVGYDdnYVE 186
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 982742431 159 GIPYWIVKNSWGPQWGMNGYFLIERgKNMCGLAACASY 196
Cdd:cd02619  187 GKGAFIVKNSWGTDWGDNGYGRISY-EDVYEMTFGANV 223
PTZ00203 PTZ00203
cathepsin L protease; Provisional
20-198 1.43e-31

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 117.11  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  20 LAGHWVVSFfqAEQQLVDCaqDFNNHGCQGGLPSQAFEYILYNKG--IMGEDTYPYQGKDG-------YCKFQPGKAI-G 89
Cdd:PTZ00203 165 VAGHKLVRL--SEQQLVSC--DHVDNGCGGGLMLQAFEWVLRNMNgtVFTEKSYPYVSGNGdvpecsnSSELAPGARIdG 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  90 FVKDVANitiydEEAMVEAVALYNPVSFAFEVTQdFMMYRTGIYssTSChkTPDKVNHAVLAVGYGEKNGIPYWIVKNSW 169
Cdd:PTZ00203 241 YVSMESS-----ERVMAAWLAKNGPISIAVDASS-FMSYHSGVL--TSC--IGEQLNHGVLLVGYNMTGEVPYWVIKNSW 310
                        170       180
                 ....*....|....*....|....*....
gi 982742431 170 GPQWGMNGYFLIERGKNMCGLaacASYPI 198
Cdd:PTZ00203 311 GEDWGEKGYVRVTMGVNACLL---TGYPV 336
PTZ00021 PTZ00021
falcipain-2; Provisional
31-201 9.95e-29

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 111.40  E-value: 9.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  31 AEQQLVDCAqdFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQG-KDGYCKFQPGKAIGFVKDVANITiydEEAMVEAV 109
Cdd:PTZ00021 314 SEQELVDCS--FKNNGCYGGLIPNAFEDMIELGGLCSEDDYPYVSdTPELCNIDRCKEKYKIKSYVSIP---EDKFKEAI 388
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431 110 ALYNPVSFAFEVTQDFMMYRTGIYSStSCHKTPdkvNHAVLAVGYGEKNGIP----------YWIVKNSWGPQWGMNGYF 179
Cdd:PTZ00021 389 RFLGPISVSIAVSDDFAFYKGGIFDG-ECGEEP---NHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGFI 464
                        170       180
                 ....*....|....*....|....*.
gi 982742431 180 LIERGKN----MCGLAACASypIPLV 201
Cdd:PTZ00021 465 RIETDENglmkTCSLGTEAY--VPLI 488
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
33-185 2.82e-24

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: 95.56  E-value: 2.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  33 QQLVDCAQDFNnhgCQGGLPSQAFEYILyNKGIMGEDTYPYQGKDGYCK---------------FQPGKAIGFVKDVAni 97
Cdd:cd02698   60 QVVIDCAGGGS---CHGGDPGGVYEYAH-KHGIPDETCNPYQAKDGECNpfnrcgtcnpfgecfAIKNYTLYFVSDYG-- 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  98 TIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSCHKTPdkvNHAVLAVGYG-EKNGIPYWIVKNSWGPQWGMN 176
Cdd:cd02698  134 SVSGRDKMMAEIYARGPISCGIMATEALENYTGGVYKEYVQDPLI---NHIISVAGWGvDENGVEYWIVRNSWGEPWGER 210

                 ....*....
gi 982742431 177 GYFLIERGK 185
Cdd:cd02698  211 GWFRIVTSS 219
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
47-181 2.74e-22

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 92.89  E-value: 2.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  47 CQGGLPSQAFeYILYNKGIMGEDTYPYQGKDGYCK---FQPGKAIGF-VKDVANIT----IYDEEAMVEAVALYNPVSFA 118
Cdd:COG4870   72 DGGSSLRDAL-KLLRWSGVVPESDWPYDDSDFTSQpsaAAYADARNYkIQDYYRLPggggATDLDAIKQALAEGGPVVFG 150
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 982742431 119 FEVTQDFMMYRTGIYSSTSchKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLI 181
Cdd:COG4870  151 FYVYESFYNYTGGVYYPTP--GDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
33-199 8.00e-21

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 89.63  E-value: 8.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  33 QQLVDCAqdFNNHGCQGGLPsqafeYILYN----KGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANIT---------- 98
Cdd:PTZ00049 445 QTVLSCS--FYDQGCNGGFP-----YLVSKmaklQGIPLDKVFPYTATEQTCPYQVDQSANSMNGSANLRqinavffsse 517
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  99 ------------IYDEEA-------------------------MVEavaLYN--PVSFAFEVTQDFMMYRTGIYSSTS-- 137
Cdd:PTZ00049 518 tqsdmhadfeapISSEPArwyakdynyiggcygcnqcngekimMNE---IYRngPIVASFEASPDFYDYADGVYYVEDfp 594
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431 138 ----C-----HKTP-------DKVNHAVLAVGYGEK--NGIP--YWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYP 197
Cdd:PTZ00049 595 harrCtvdlpKHNGvynitgwEKVNHAIVLVGWGEEeiNGKLykYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQSLFI 674

                 ..
gi 982742431 198 IP 199
Cdd:PTZ00049 675 EP 676
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
140-193 1.88e-09

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 56.61  E-value: 1.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 982742431  140 KTPDkvnHAVLAVGYG-----EKNGIPYWIVKNSWGPQWGMNGYFLIErgknMCGLAAC 193
Cdd:PTZ00462  719 DTAD---HAVNIVGYGnyindEDEKKSYWIVRNSWGKYWGDEGYFKVD----MYGPSHC 770
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
29-200 7.81e-08

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 51.43  E-value: 7.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  29 FQAEQQLVDCAQdfNNHGCQGGLPsqaFEYILYNK--GIMGEDTY--PYQGKDGY---CKFQP-------------GKAI 88
Cdd:PTZ00364 263 FLSARHVLDCSQ--YGQGCAGGFP---EEVGKFAEtfGILTTDSYyiPYDSGDGVeraCKTRRpsrryyftnygplGGYY 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 982742431  89 GFVKDVANIT--IYDEEAMVEAVALYNPVSFAFE-VTQDFMMYRTGIYSSTSC-----HKTPDKVNHAVLAVGYGE-KNG 159
Cdd:PTZ00364 338 GAVTDPDEIIweIYRHGPVPASVYANSDWYNCDEnSTEDVRYVSLDDYSTASAdrplrHYFASNVNHTVLIIGWGTdENG 417
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 982742431 160 IPYWIVKNSWGPQ--WGMNGYFLIERGKNMCGLaacASYPIPL 200
Cdd:PTZ00364 418 GDYWLVLDPWGSRrsWCDGGTRKIARGVNAYNI---ESEVVVM 457
PepC COG3579
Aminopeptidase C [Amino acid transport and metabolism];
146-179 1.13e-03

Aminopeptidase C [Amino acid transport and metabolism];


Pssm-ID: 442798 [Multi-domain]  Cd Length: 440  Bit Score: 39.09  E-value: 1.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 982742431 146 NHAVLAVGYG-EKNGIP-YWIVKNSWGPQWGMNGYF 179
Cdd:COG3579  362 THAMVITGVDlDQNGKPtRWKVENSWGDDNGYKGYF 397
 
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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