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Conserved domains on  [gi|568983491|ref|XP_006517376|]
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cathepsin M isoform X4 [Mus musculus]

Protein Classification

C1 family peptidase( domain architecture ID 10656546)

C1 family peptidase (also called papain family protein) is a papain-like cysteine peptidase that catalyzes the hydrolysis of peptide bonds in substrates using a catalytic dyad of Cys and His residues

CATH:  3.90.70.10
EC:  3.4.22.-
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 cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
115-260 1.27e-64

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: 200.93  E-value: 1.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 115 PKFINWKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRPqGNWGCYLGNTYLALHYvMENG 194
Cdd:cd02248    1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEY-VKNG 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983491 195 GLESEATYPYEEKDGSCRYSPENSTANITGFEFVPK-NEDALMNAVASIGPISVAIDARHaSFLFYK 260
Cdd:cd02248   79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASS-SFQFYK 144
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
29-87 2.11e-19

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.


:

Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 79.21  E-value: 2.11e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491    29 WQKWKIKYGKAYSLEEEGQKR-AVWEDNMKKIKLHNGENglgKHGFTMEMNAFGDMTLEE 87
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRfAIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
 
Name Accession Description Interval E-value
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
115-260 1.27e-64

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: 200.93  E-value: 1.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 115 PKFINWKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRPqGNWGCYLGNTYLALHYvMENG 194
Cdd:cd02248    1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEY-VKNG 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983491 195 GLESEATYPYEEKDGSCRYSPENSTANITGFEFVPK-NEDALMNAVASIGPISVAIDARHaSFLFYK 260
Cdd:cd02248   79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASS-SFQFYK 144
Peptidase_C1 pfam00112
Papain family cysteine protease;
114-260 4.10e-62

Papain family cysteine protease;


Pssm-ID: 425470  Cd Length: 214  Bit Score: 194.68  E-value: 4.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491  114 LPKFINWKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRpqGNWGCYLGNTYLALHYVMEN 193
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDT--FNNGCNGGLPDNAFEYIKKN 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983491  194 GGLESEATYPYEEKDGSCRYSPENST-ANITGFEFVPKN-EDALMNAVASIGPISVAIDARHASFLFYK 260
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNSKvAKIKGYGDVPYNdEEALQAALAKNGPVSVAIDAYERDFQLYK 147
Pept_C1 smart00645
Papain family cysteine protease;
114-205 2.72e-42

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 142.72  E-value: 2.72e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491   114 LPKFINWKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRPQGNwGCYLGNTYLALHYVMEN 193
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNC-GCNGGLPDNAFEYIKKN 79
                           90
                   ....*....|..
gi 568983491   194 GGLESEATYPYE 205
Cdd:smart00645  80 GGLETESCYPYT 91
PTZ00021 PTZ00021
falcipain-2; Provisional
36-260 2.02e-40

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 145.68  E-value: 2.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491  36 YGKAYSLEEEGQKR-AVWEDNMKKIKLHNG-ENGLGKHGftmeMNAFGDMTLEEFRKVMIeipvpTVKKGKSvqKRLSVN 113
Cdd:PTZ00021 176 HGKKYQTPDEMQQRyLSFVENLAKINAHNNkENVLYKKG----MNRFGDLSFEEFKKKYL-----TLKSFDF--KSNGKK 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 114 LPKFIN---------------------WKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRP 172
Cdd:PTZ00021 245 SPRVINyddvikkykpkdatfdhakydWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSFK 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 173 qgNWGCYLGNTYLALHYVMENGGLESEATYPY-EEKDGSCRYSPENSTANITGFEFVPknEDALMNAVASIGPISVAIDA 251
Cdd:PTZ00021 325 --NNGCYGGLIPNAFEDMIELGGLCSEDDYPYvSDTPELCNIDRCKEKYKIKSYVSIP--EDKFKEAIRFLGPISVSIAV 400

                 ....*....
gi 568983491 252 RHaSFLFYK 260
Cdd:PTZ00021 401 SD-DFAFYK 408
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
29-87 2.11e-19

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.


Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 79.21  E-value: 2.11e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491    29 WQKWKIKYGKAYSLEEEGQKR-AVWEDNMKKIKLHNGENglgKHGFTMEMNAFGDMTLEE 87
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRfAIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
29-88 8.42e-17

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS.


Pssm-ID: 429886 [Multi-domain]  Cd Length: 58  Bit Score: 72.29  E-value: 8.42e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568983491   29 WQKWKIKYGKAY-SLEEEGQKRAVWEDNMKKIKLHNGEnglGKHGFTMEMNAFGDMTLEEF 88
Cdd:pfam08246   1 FDDWMKKYGKSYrSTEEELYRFQIFKENLKRIEEHNSN---GNVTYKLGLNKFADLTDEEF 58
 
Name Accession Description Interval E-value
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
115-260 1.27e-64

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: 200.93  E-value: 1.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 115 PKFINWKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRPqGNWGCYLGNTYLALHYvMENG 194
Cdd:cd02248    1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEY-VKNG 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568983491 195 GLESEATYPYEEKDGSCRYSPENSTANITGFEFVPK-NEDALMNAVASIGPISVAIDARHaSFLFYK 260
Cdd:cd02248   79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPgDEEALKAALANYGPVSVAIDASS-SFQFYK 144
Peptidase_C1 pfam00112
Papain family cysteine protease;
114-260 4.10e-62

Papain family cysteine protease;


Pssm-ID: 425470  Cd Length: 214  Bit Score: 194.68  E-value: 4.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491  114 LPKFINWKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRpqGNWGCYLGNTYLALHYVMEN 193
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDT--FNNGCNGGLPDNAFEYIKKN 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568983491  194 GGLESEATYPYEEKDGSCRYSPENST-ANITGFEFVPKN-EDALMNAVASIGPISVAIDARHASFLFYK 260
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNSKvAKIKGYGDVPYNdEEALQAALAKNGPVSVAIDAYERDFQLYK 147
Pept_C1 smart00645
Papain family cysteine protease;
114-205 2.72e-42

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 142.72  E-value: 2.72e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491   114 LPKFINWKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRPQGNwGCYLGNTYLALHYVMEN 193
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNC-GCNGGLPDNAFEYIKKN 79
                           90
                   ....*....|..
gi 568983491   194 GGLESEATYPYE 205
Cdd:smart00645  80 GGLETESCYPYT 91
PTZ00021 PTZ00021
falcipain-2; Provisional
36-260 2.02e-40

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 145.68  E-value: 2.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491  36 YGKAYSLEEEGQKR-AVWEDNMKKIKLHNG-ENGLGKHGftmeMNAFGDMTLEEFRKVMIeipvpTVKKGKSvqKRLSVN 113
Cdd:PTZ00021 176 HGKKYQTPDEMQQRyLSFVENLAKINAHNNkENVLYKKG----MNRFGDLSFEEFKKKYL-----TLKSFDF--KSNGKK 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 114 LPKFIN---------------------WKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRP 172
Cdd:PTZ00021 245 SPRVINyddvikkykpkdatfdhakydWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSFK 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 173 qgNWGCYLGNTYLALHYVMENGGLESEATYPY-EEKDGSCRYSPENSTANITGFEFVPknEDALMNAVASIGPISVAIDA 251
Cdd:PTZ00021 325 --NNGCYGGLIPNAFEDMIELGGLCSEDDYPYvSDTPELCNIDRCKEKYKIKSYVSIP--EDKFKEAIRFLGPISVSIAV 400

                 ....*....
gi 568983491 252 RHaSFLFYK 260
Cdd:PTZ00021 401 SD-DFAFYK 408
PTZ00203 PTZ00203
cathepsin L protease; Provisional
29-259 7.44e-35

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 128.28  E-value: 7.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491  29 WQKWKIKYGKAY-SLEEEGQKRAVWEDNMKKIKLHNGENGLGKHGFTmemnAFGDMTLEEF--RKVMIEIPVPTVKKGKS 105
Cdd:PTZ00203  38 FEEFKRTYQRAYgTLTEEQQRLANFERNLELMREHQARNPHARFGIT----KFFDLSEAEFaaRYLNGAAYFAAAKQHAG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 106 VQKR-----LSVnLPKFINWKKRGYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLIPLSVQNLVDCSRPQGnwGCYL 180
Cdd:PTZ00203 114 QHYRkaradLSA-VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDN--GCGG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 181 GNTYLALHYVMEN--GGLESEATYPYEEKDGSCRYSPENST----ANITGFEFVPKNEDALMNAVASIGPISVAIDArhA 254
Cdd:PTZ00203 191 GLMLQAFEWVLRNmnGTVFTEKSYPYVSGNGDVPECSNSSElapgARIDGYVSMESSERVMAAWLAKNGPISIAVDA--S 268

                 ....*
gi 568983491 255 SFLFY 259
Cdd:PTZ00203 269 SFMSY 273
PTZ00200 PTZ00200
cysteine proteinase; Provisional
27-267 4.08e-30

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 117.10  E-value: 4.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491  27 VEWQKWKIKYGKAYSLEEEGQKRAV-WEDNMKKIKLHNGenglgKHGFTMEMNAFGDMTLEEFRKVMIEIPVPTVKKGKS 105
Cdd:PTZ00200 124 LEFEEFNKKYNRKHATHAERLNRFLtFRNNYLEVKSHKG-----DEPYSKEINKFSDLTEEEFRKLFPVIKVPPKSNSTS 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 106 VQKRL---SVNLPKFI------------------------NWKKRGYVTPVQTQGR-CNSCWAFSVTGAIEG--QMFRKT 155
Cdd:PTZ00200 199 HNNDFkarHVSNPTYLknlkkakntdedvkdpskitgeglDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESlyKIYRDK 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 156 GqlIPLSVQNLVDCSRpqGNWGCYLGNTYLALHYVmENGGLESEATYPYEEKDGSCRYsPENSTANITGFeFVPKNEDaL 235
Cdd:PTZ00200 279 S--VDLSEQELVNCDT--KSQGCSGGYPDTALEYV-KNKGLSSSSDVPYLAKDGKCVV-SSTKKVYIDSY-LVAKGKD-V 350
                        250       260       270
                 ....*....|....*....|....*....|..
gi 568983491 236 MNAVASIGPISVAIdARHASFLFYKrAWVHNG 267
Cdd:PTZ00200 351 LNKSLVISPTVVYI-AVSRELLKYK-SGVYNG 380
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
119-269 9.34e-20

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  Cd Length: 223  Bit Score: 84.87  E-value: 9.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 119 NWKKRgYVTPVQTQGRCNSCWAFSVTGAIEGQMFRKTG--QLIPLSVQNLVDCSRPQ---GNWGCYLGNTYLALHYVMEN 193
Cdd:cd02619    3 DLRPL-RLTPVKNQGSRGSCWAFASAYALESAYRIKGGedEYVDLSPQYLYICANDEclgINGSCDGGGPLSALLKLVAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 194 GGLESEATYPYEEKDGSCRYSPENSTA----NITGFE-FVPKNEDALMNAVASIGPISVAIDArHASFLFYKRAWVHNGA 268
Cdd:cd02619   82 KGIPPEEDYPYGAESDGEEPKSEAALNaakvKLKDYRrVLKNNIEDIKEALAKGGPVVAGFDV-YSGFDRLKEGIIYEEI 160

                 .
gi 568983491 269 I 269
Cdd:cd02619  161 V 161
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
29-87 2.11e-19

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.


Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 79.21  E-value: 2.11e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491    29 WQKWKIKYGKAYSLEEEGQKR-AVWEDNMKKIKLHNGENglgKHGFTMEMNAFGDMTLEE 87
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRfAIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
29-88 8.42e-17

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS.


Pssm-ID: 429886 [Multi-domain]  Cd Length: 58  Bit Score: 72.29  E-value: 8.42e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568983491   29 WQKWKIKYGKAY-SLEEEGQKRAVWEDNMKKIKLHNGEnglGKHGFTMEMNAFGDMTLEEF 88
Cdd:pfam08246   1 FDDWMKKYGKSYrSTEEELYRFQIFKENLKRIEEHNSN---GNVTYKLGLNKFADLTDEEF 58
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
114-251 8.64e-15

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: 71.68  E-value: 8.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 114 LPKFINWKK---RGYVTPVQTQ---GRCNSCWAFSVTGAIEGQMF--RK-TGQLIPLSVQNLVDCsrpqGNWGCYLGNTY 184
Cdd:cd02698    1 LPKSWDWRNvngVNYVSPTRNQhipQYCGSCWAHGSTSALADRINiaRKgAWPSVYLSVQVVIDC----AGGGSCHGGDP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 185 LALHYVMENGGLESEATYPYEEKDGSCRYSPENSTANITGFEFVPKN--------------EDALMNAVASIGPISVAID 250
Cdd:cd02698   77 GGVYEYAHKHGIPDETCNPYQAKDGECNPFNRCGTCNPFGECFAIKNytlyfvsdygsvsgRDKMMAEIYARGPISCGIM 156

                 .
gi 568983491 251 A 251
Cdd:cd02698  157 A 157
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
128-260 3.79e-12

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: 64.21  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 128 PVQTQGRCNSCWAFSVTGAIEGQMFRKTGQLI--PLSVQNLVDCSRPQGNwGCYLGNTYLALHYvMENGGLESEATYPYe 205
Cdd:cd02620   18 EIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKEnvLLSAQDLLSCCSGCGD-GCNGGYPDAAWKY-LTTTGVVTGGCQPY- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 206 eKDGSCRYSPENSTaNITGFEF-------------------------VPKNEDALMNAVASIGPISVAIDArHASFLFYK 260
Cdd:cd02620   95 -TIPPCGHHPEGPP-PCCGTPYctpkcqdgcektyeedkhkgksaysVPSDETDIMKEIMTNGPVQAAFTV-YEDFLYYK 171
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
114-216 2.80e-03

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 38.72  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568983491 114 LPKFINWKKRGYVT-----PVQTQGR-CNSCWAFsvtGAIEGQMFR---------KTGQLIPLSVQNLVDCSrpQGNWGC 178
Cdd:PTZ00364 205 PPAAWSWGDVGGASflpaaPPASPGRgCNSSYVE---AALAAMMARvmvasnrtdPLGQQTFLSARHVLDCS--QYGQGC 279
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 568983491 179 YLGNTYLALHYVMENGGLESEATY-PYEEKDG---SCRYSPE 216
Cdd:PTZ00364 280 AGGFPEEVGKFAETFGILTTDSYYiPYDSGDGverACKTRRP 321
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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