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Conserved domains on  [gi|2118777167|gb|UDE22410|]
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cathepsin F1 [Mytilus galloprovincialis]

Protein Classification

C1 family peptidase( domain architecture ID 11276840)

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|14515150
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;
120-378 2.42e-76

Papain family cysteine protease;


:

Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 235.13  E-value: 2.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 120 LPDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDGFedvtrkNADCGvfGGWPYLAY 199
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTF------NNGCN--GGLPDNAF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 200 QYIMKTGGIESSRDYgycsgdtdtkhqennclpcpppgfnstlcgpavPYCNMSQSCVAKLDKSKFVKglkIADWKAI-D 278
Cdd:pfam00112  73 EYIKKNGGIVTESDY---------------------------------PYTAKDGTCKFKKSNSKVAK---IKGYGDVpY 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 279 KNETNIAEQLMKIGPLSIAMNA--DWLMFYRSGISSPYFCDPKsINHAVLLVGFGKEKtlfGEKlYWKVKNSWGPSWGEK 356
Cdd:pfam00112 117 NDEEALQAALAKNGPVSVAIDAyeRDFQLYKSGVYKHTECGGE-LNHAVLLVGYGTEN---GVP-YWIVKNSWGTDWGEN 191

                         250       260
                  ....*....|....*....|...
gi 2118777167 357 GYFRIKRN-AGTCGINTQVTTAI 378
Cdd:pfam00112 192 GYFRIARGvNNECGIASEASYPI 214
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 35-91 8.03e-16

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: 71.12  E-value: 8.03e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2118777167   35 FQTWKLENGKEYNGVNEEQKRFDVFYDNIKTINKYNKMYQPQTTFALNKFADMSPSE 91
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHSYKLGVNQFSDLTPEE 57
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
120-378 2.42e-76

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 235.13  E-value: 2.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 120 LPDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDGFedvtrkNADCGvfGGWPYLAY 199
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTF------NNGCN--GGLPDNAF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 200 QYIMKTGGIESSRDYgycsgdtdtkhqennclpcpppgfnstlcgpavPYCNMSQSCVAKLDKSKFVKglkIADWKAI-D 278
Cdd:pfam00112  73 EYIKKNGGIVTESDY---------------------------------PYTAKDGTCKFKKSNSKVAK---IKGYGDVpY 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 279 KNETNIAEQLMKIGPLSIAMNA--DWLMFYRSGISSPYFCDPKsINHAVLLVGFGKEKtlfGEKlYWKVKNSWGPSWGEK 356
Cdd:pfam00112 117 NDEEALQAALAKNGPVSVAIDAyeRDFQLYKSGVYKHTECGGE-LNHAVLLVGYGTEN---GVP-YWIVKNSWGTDWGEN 191

                         250       260
                  ....*....|....*....|...
gi 2118777167 357 GYFRIKRN-AGTCGINTQVTTAI 378
Cdd:pfam00112 192 GYFRIARGvNNECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 121-377 5.08e-76

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: 234.06  E-value: 5.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 121 PDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDgfedvTRKNADCGvfGGWPYLAYQ 200
Cdd:cd02248     1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCS-----TSGNNGCN--GGNPDNAFE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 201 YImKTGGIESSRDYgycsgdtdtkhqennclpcpppgfnstlcgpavPYCNMSQSCVAkldkSKFVKGLKIADWKAIDK- 279
Cdd:cd02248    74 YV-KNGGLASESDY---------------------------------PYTGKDGTCKY----NSSKVGAKITGYSNVPPg 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 280 NETNIAEQLMKIGPLSIAMNAD-WLMFYRSGISSPYFCDPKSINHAVLLVGFGKEKtlfGEKlYWKVKNSWGPSWGEKGY 358
Cdd:cd02248   116 DEEALKAALANYGPVSVAIDASsSFQFYKGGIYSGPCCSNTNLNHAVLLVGYGTEN---GVD-YWIVKNSWGTSWGEKGY 191

                         250
                  ....*....|....*....
gi 2118777167 359 FRIKRNAGTCGINTQVTTA 377
Cdd:cd02248   192 IRIARGSNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
120-378 1.73e-63

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 200.50  E-value: 1.73e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  120 LPDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDGfedvtrkNADCGVFGGWPYLAY 199
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSG-------GGNCGCNGGLPDNAF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  200 QYIMKTGGIESSRDYgycsgdtdtkhqennclpcpppgfnstlcgpavPYcnmsqscvakldkskfvkglkiadwkaidk 279
Cdd:smart00645  74 EYIKKNGGLETESCY---------------------------------PY------------------------------ 90

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  280 netniaeqlmkigPLSIAMNADWLMFYRSGISSPYFCDPKSINHAVLLVGFGKEKTlfGEKLYWKVKNSWGPSWGEKGYF 359
Cdd:smart00645  91 -------------TGSVAIDASDFQFYKSGIYDHPGCGSGTLDHAVLIVGYGTEVE--NGKDYWIVKNSWGTDWGENGYF 155

                          250       260
                   ....*....|....*....|
gi 2118777167  360 RIKRN-AGTCGINTQVTTAI 378
Cdd:smart00645 156 RIARGkNNECGIEASVASYP 175
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 31-368 1.69e-61

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 201.47  E-value: 1.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  31 AKQLFQTWKLENGKEYNGVNEEQKRFDVFYDNIKTINKYnKMYQPQTTFALNKFADMSPSEFHRKILMSDR---KPPTFE 107
Cdd:PTZ00203   34 AAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREH-QARNPHARFGITKFFDLSEAEFAARYLNGAAyfaAAKQHA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 108 NDRYIKGEKGFY-LPDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDgfedvtrkNA 186
Cdd:PTZ00203  113 GQHYRKARADLSaVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCD--------HV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 187 DCGVFGGWPYLAYQYIMK--TGGIESSRDYGYCSGDTDtkhqennclpcpppgfnstlcgpaVPYCnmsqscvakLDKSK 264
Cdd:PTZ00203  185 DNGCGGGLMLQAFEWVLRnmNGTVFTEKSYPYVSGNGD------------------------VPEC---------SNSSE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 265 FVKGLKIADWKAIDKNETNIAEQLMKIGPLSIAMNADWLMFYRSGISSPyfCDPKSINHAVLLVGFGKEktlfGEKLYWK 344
Cdd:PTZ00203  232 LAPGARIDGYVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTS--CIGEQLNHGVLLVGYNMT----GEVPYWV 305

                         330       340
                  ....*....|....*....|....
gi 2118777167 345 VKNSWGPSWGEKGYFRIKRNAGTC 368
Cdd:PTZ00203  306 IKNSWGEDWGEKGYVRVTMGVNAC 329
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
120-362 3.64e-25

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 105.99  E-value: 3.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 120 LPDSFDWvpKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPL---VNLSVEQVVDCDGFEDVTRkNADCGvfGGWPY 196
Cdd:COG4870     4 LPSSVDL--RGYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQARNGDGTE-GTDDG--GSSLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 197 LAYqYIMKTGGIESSRDYGYcsgdtdtkhQENNCLPCPPPGFNSTlcgpAVPYcnmsqscvakldkskfvkglKIADWKA 276
Cdd:COG4870    79 DAL-KLLRWSGVVPESDWPY---------DDSDFTSQPSAAAYAD----ARNY--------------------KIQDYYR 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 277 IDKNETN-----IAEQLMKIGPLSIAMNA--DWlMFYRSGISSPYFCDPKSINHAVLLVGFGKEKtlfgEKLYWKVKNSW 349
Cdd:COG4870   125 LPGGGGAtdldaIKQALAEGGPVVFGFYVyeSF-YNYTGGVYYPTPGDASLGGHAVAIVGYDDNY----SDGAFIIKNSW 199

                         250
                  ....*....|...
gi 2118777167 350 GPSWGEKGYFRIK 362
Cdd:COG4870   200 GTGWGDNGYFWIS 212
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 35-91 8.03e-16

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: 71.12  E-value: 8.03e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2118777167   35 FQTWKLENGKEYNGVNEEQKRFDVFYDNIKTINKYNKMYQPQTTFALNKFADMSPSE 91
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 35-92 5.16e-15

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 Swiss:Q70SU8. This family is classified as I29 by MEROPS.


Pssm-ID: 462410 [Multi-domain]  Cd Length: 58  Bit Score: 68.83  E-value: 5.16e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118777167  35 FQTWKLENGKEYNGVNEEQKRFDVFYDNIKTINKYNKMYQPQTTFALNKFADMSPSEF 92
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGNVTYKLGLNKFADLTDEEF 58
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
120-378 2.42e-76

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 235.13  E-value: 2.42e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 120 LPDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDGFedvtrkNADCGvfGGWPYLAY 199
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTF------NNGCN--GGLPDNAF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 200 QYIMKTGGIESSRDYgycsgdtdtkhqennclpcpppgfnstlcgpavPYCNMSQSCVAKLDKSKFVKglkIADWKAI-D 278
Cdd:pfam00112  73 EYIKKNGGIVTESDY---------------------------------PYTAKDGTCKFKKSNSKVAK---IKGYGDVpY 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 279 KNETNIAEQLMKIGPLSIAMNA--DWLMFYRSGISSPYFCDPKsINHAVLLVGFGKEKtlfGEKlYWKVKNSWGPSWGEK 356
Cdd:pfam00112 117 NDEEALQAALAKNGPVSVAIDAyeRDFQLYKSGVYKHTECGGE-LNHAVLLVGYGTEN---GVP-YWIVKNSWGTDWGEN 191

                         250       260
                  ....*....|....*....|...
gi 2118777167 357 GYFRIKRN-AGTCGINTQVTTAI 378
Cdd:pfam00112 192 GYFRIARGvNNECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 121-377 5.08e-76

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: 234.06  E-value: 5.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 121 PDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDgfedvTRKNADCGvfGGWPYLAYQ 200
Cdd:cd02248     1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCS-----TSGNNGCN--GGNPDNAFE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 201 YImKTGGIESSRDYgycsgdtdtkhqennclpcpppgfnstlcgpavPYCNMSQSCVAkldkSKFVKGLKIADWKAIDK- 279
Cdd:cd02248    74 YV-KNGGLASESDY---------------------------------PYTGKDGTCKY----NSSKVGAKITGYSNVPPg 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 280 NETNIAEQLMKIGPLSIAMNAD-WLMFYRSGISSPYFCDPKSINHAVLLVGFGKEKtlfGEKlYWKVKNSWGPSWGEKGY 358
Cdd:cd02248   116 DEEALKAALANYGPVSVAIDASsSFQFYKGGIYSGPCCSNTNLNHAVLLVGYGTEN---GVD-YWIVKNSWGTSWGEKGY 191

                         250
                  ....*....|....*....
gi 2118777167 359 FRIKRNAGTCGINTQVTTA 377
Cdd:cd02248   192 IRIARGSNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
120-378 1.73e-63

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 200.50  E-value: 1.73e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  120 LPDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDGfedvtrkNADCGVFGGWPYLAY 199
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSG-------GGNCGCNGGLPDNAF 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  200 QYIMKTGGIESSRDYgycsgdtdtkhqennclpcpppgfnstlcgpavPYcnmsqscvakldkskfvkglkiadwkaidk 279
Cdd:smart00645  74 EYIKKNGGLETESCY---------------------------------PY------------------------------ 90

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  280 netniaeqlmkigPLSIAMNADWLMFYRSGISSPYFCDPKSINHAVLLVGFGKEKTlfGEKLYWKVKNSWGPSWGEKGYF 359
Cdd:smart00645  91 -------------TGSVAIDASDFQFYKSGIYDHPGCGSGTLDHAVLIVGYGTEVE--NGKDYWIVKNSWGTDWGENGYF 155

                          250       260
                   ....*....|....*....|
gi 2118777167  360 RIKRN-AGTCGINTQVTTAI 378
Cdd:smart00645 156 RIARGkNNECGIEASVASYP 175
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 31-368 1.69e-61

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 201.47  E-value: 1.69e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  31 AKQLFQTWKLENGKEYNGVNEEQKRFDVFYDNIKTINKYnKMYQPQTTFALNKFADMSPSEFHRKILMSDR---KPPTFE 107
Cdd:PTZ00203   34 AAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREH-QARNPHARFGITKFFDLSEAEFAARYLNGAAyfaAAKQHA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 108 NDRYIKGEKGFY-LPDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCDgfedvtrkNA 186
Cdd:PTZ00203  113 GQHYRKARADLSaVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCD--------HV 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 187 DCGVFGGWPYLAYQYIMK--TGGIESSRDYGYCSGDTDtkhqennclpcpppgfnstlcgpaVPYCnmsqscvakLDKSK 264
Cdd:PTZ00203  185 DNGCGGGLMLQAFEWVLRnmNGTVFTEKSYPYVSGNGD------------------------VPEC---------SNSSE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 265 FVKGLKIADWKAIDKNETNIAEQLMKIGPLSIAMNADWLMFYRSGISSPyfCDPKSINHAVLLVGFGKEktlfGEKLYWK 344
Cdd:PTZ00203  232 LAPGARIDGYVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTS--CIGEQLNHGVLLVGYNMT----GEVPYWV 305

                         330       340
                  ....*....|....*....|....
gi 2118777167 345 VKNSWGPSWGEKGYFRIKRNAGTC 368
Cdd:PTZ00203  306 IKNSWGEDWGEKGYVRVTMGVNAC 329
PTZ00021 PTZ00021
falcipain-2; Provisional
 41-379 2.91e-44

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 159.55  E-value: 2.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  41 ENGKEYNGVNEEQKRFDVFYDNIKTINKYNKMYQPQTTFALNKFADMSPSEFHRKIL-------MSDRKPPTFEND---- 109
Cdd:PTZ00021  175 EHGKKYQTPDEMQQRYLSFVENLAKINAHNNKENVLYKKGMNRFGDLSFEEFKKKYLtlksfdfKSNGKKSPRVINyddv 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 110 --RYiKGEKGFYLPDSFDWVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPLVNLSVEQVVDCdgfedvTRKNAD 187
Cdd:PTZ00021  255 ikKY-KPKDATFDHAKYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDC------SFKNNG 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 188 CgvFGGWPYLAYQYIMKTGGIESSRDYGYCsgdtdtkhqennclpcpppGFNSTLCgpavpycnmsqscvaKLDKSKfvK 267
Cdd:PTZ00021  328 C--YGGLIPNAFEDMIELGGLCSEDDYPYV-------------------SDTPELC---------------NIDRCK--E 369

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 268 GLKIADWKAIDKNEtnIAEQLMKIGPLSIAMNA-DWLMFYRSGISSPYFCDpkSINHAVLLVGFGKEK-----TLFGEKL 341
Cdd:PTZ00021  370 KYKIKSYVSIPEDK--FKEAIRFLGPISVSIAVsDDFAFYKGGIFDGECGE--EPNHAVILVGYGMEEiynsdTKKMEKR 445

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 2118777167 342 YWK-VKNSWGPSWGEKGYFRIKRNAG----TCGINTQVTTAIL 379
Cdd:PTZ00021  446 YYYiIKNSWGESWGEKGFIRIETDENglmkTCSLGTEAYVPLI 488
PTZ00200 PTZ00200
cysteine proteinase; Provisional
 35-381 1.64e-42

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 154.08  E-value: 1.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  35 FQTWKLENGKEYNGVNEEQKRFDVF---YDNIKTiNKYNKMYqpqtTFALNKFADMSPSEFHR---KILMSDRKPPTFEN 108
Cdd:PTZ00200  126 FEEFNKKYNRKHATHAERLNRFLTFrnnYLEVKS-HKGDEPY----SKEINKFSDLTEEEFRKlfpVIKVPPKSNSTSHN 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 109 DRYI-------------KGEKGFYLP---------DSFDWVPKNVVTSVKNQGA-AGSCWAFSTIENIEGQWALSGQPLV 165
Cdd:PTZ00200  201 NDFKarhvsnptylknlKKAKNTDEDvkdpskitgEGLDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRDKSV 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 166 NLSVEQVVDCDGFEDvtrknadcGVFGGWPYLAYQYImKTGGIESSRDygycsgdtdtkhqennclpcpppgfnstlcgp 245
Cdd:PTZ00200  281 DLSEQELVNCDTKSQ--------GCSGGYPDTALEYV-KNKGLSSSSD-------------------------------- 319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 246 aVPYCNMSQSCVAKLDKSKFVKGLKIAdwKAIDknetnIAEQLMKIGPLSIAMNA-DWLMFYRSGIsspyFCDP--KSIN 322
Cdd:PTZ00200  320 -VPYLAKDGKCVVSSTKKVYIDSYLVA--KGKD-----VLNKSLVISPTVVYIAVsRELLKYKSGV----YNGEcgKSLN 387

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2118777167 323 HAVLLVGFGKEKTLfgEKLYWKVKNSWGPSWGEKGYFRIKR-NAGT--CGINTQVTTAILMK 381
Cdd:PTZ00200  388 HAVLLVGEGYDEKT--KKRYWIIKNSWGTDWGENGYMRLERtNEGTdkCGILTVGLTPVFYS 447
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
 121-377 4.64e-38

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: 136.63  E-value: 4.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 121 PDSFD----WVPKNVVTSVKNQGAAGSCWAFSTIENIEGQWALS--GQPLVNLSVEQVVDCDGFedvtrknADCGVFGGW 194
Cdd:cd02620     1 PESFDarekWPNCISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQsnGKENVLLSAQDLLSCCSG-------CGDGCNGGY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 195 PYLAYQYIMKTGGIessrdYGYC---SGDTDTKHQENNClPCPPPGFNSTLCgpavpycnmSQSCVAKLDKSKFvkglKI 271
Cdd:cd02620    74 PDAAWKYLTTTGVV-----TGGCqpyTIPPCGHHPEGPP-PCCGTPYCTPKC---------QDGCEKTYEEDKH----KG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 272 ADWKAIDKNETNIAEQLMKIGPLSIAM--NADWLMfYRSGISSPYfcdpKSIN---HAVLLVGFGKEKtlfGEKlYWKVK 346
Cdd:cd02620   135 KSAYSVPSDETDIMKEIMTNGPVQAAFtvYEDFLY-YKSGVYQHT----SGKQlggHAVKIIGWGVEN---GVP-YWLAA 205

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2118777167 347 NSWGPSWGEKGYFRIKRNAGTCGINTQVTTA 377
Cdd:cd02620   206 NSWGTDWGENGYFRILRGSNECGIESEVVAG 236
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
 120-377 9.06e-30

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: 114.79  E-value: 9.06e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 120 LPDSFDW----VPKNVVTSVKNQGAAGSCWAFSTIENIEGQ--------WALSGQPLvnLSVEQVVDCDGFedvtrknaD 187
Cdd:cd02621     1 LPKSFDWgdvnNGFNYVSPVRNQGGCGSCYAFASVYALEARimiasnktDPLGQQPI--LSPQHVLSCSQY--------S 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 188 CGVFGGWPYLAYQYiMKTGGIESSRDYGYCSGDTDtkhqennclPCPPPGFNSTlcgpavpycnmsqscvakldKSKFVK 267
Cdd:cd02621    71 QGCDGGFPFLVGKF-AEDFGIVTEDYFPYTADDDR---------PCKASPSECR--------------------RYYFSD 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 268 GLKIADWKAIdKNETNIAEQLMKIGPLSIAMNADW-LMFYRSGI----SSPYFCDP--------KSINHAVLLVGFGKEK 334
Cdd:cd02621   121 YNYVGGCYGC-TNEDEMKWEIYRNGPIVVAFEVYSdFDFYKEGVyhhtDNDEVSDGdndnfnpfELTNHAVLLVGWGEDE 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2118777167 335 tLFGEKlYWKVKNSWGPSWGEKGYFRIKRNAGTCGINTQVTTA 377
Cdd:cd02621   200 -IKGEK-YWIVKNSWGSSWGEKGYFKIRRGTNECGIESQAVFA 240
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 123-361 2.83e-29

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: 112.99  E-value: 2.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 123 SFDWVPKNVvTSVKNQGAAGSCWAFSTIENIEGQW--ALSGQPLVNLSVEQVVDCDGFEDVTRKNADCGvfgGWPYLAYQ 200
Cdd:cd02619     1 SVDLRPLRL-TPVKNQGSRGSCWAFASAYALESAYriKGGEDEYVDLSPQYLYICANDECLGINGSCDG---GGPLSALL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 201 YIMKTGGIESSRDYGYcsGDTDTKHQEnnclpcpppgfnstlcgpavpycnmsqSCVAKLDKSKFvkglKIADWKAIDKN 280
Cdd:cd02619    77 KLVALKGIPPEEDYPY--GAESDGEEP---------------------------KSEAALNAAKV----KLKDYRRVLKN 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 281 ETN-IAEQLMKIGPLSIAMNA--DWLMFYRSGISSPYF----CDPKSINHAVLLVGFGKEKTlfGEKLYWKVKNSWGPSW 353
Cdd:cd02619   124 NIEdIKEALAKGGPVVAGFDVysGFDRLKEGIIYEEIVyllyEDGDLGGHAVVIVGYDDNYV--EGKGAFIVKNSWGTDW 201


                  ....*...
gi 2118777167 354 GEKGYFRI 361
Cdd:cd02619   202 GDNGYGRI 209
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
120-362 3.64e-25

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 105.99  E-value: 3.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 120 LPDSFDWvpKNVVTSVKNQGAAGSCWAFSTIENIEGQWALSGQPL---VNLSVEQVVDCDGFEDVTRkNADCGvfGGWPY 196
Cdd:COG4870     4 LPSSVDL--RGYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQARNGDGTE-GTDDG--GSSLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 197 LAYqYIMKTGGIESSRDYGYcsgdtdtkhQENNCLPCPPPGFNSTlcgpAVPYcnmsqscvakldkskfvkglKIADWKA 276
Cdd:COG4870    79 DAL-KLLRWSGVVPESDWPY---------DDSDFTSQPSAAAYAD----ARNY--------------------KIQDYYR 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 277 IDKNETN-----IAEQLMKIGPLSIAMNA--DWlMFYRSGISSPYFCDPKSINHAVLLVGFGKEKtlfgEKLYWKVKNSW 349
Cdd:COG4870   125 LPGGGGAtdldaIKQALAEGGPVVFGFYVyeSF-YNYTGGVYYPTPGDASLGGHAVAIVGYDDNY----SDGAFIIKNSW 199

                         250
                  ....*....|...
gi 2118777167 350 GPSWGEKGYFRIK 362
Cdd:COG4870   200 GTGWGDNGYFWIS 212
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
 120-365 6.32e-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: 99.03  E-value: 6.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 120 LPDSFDWvpKNV-----VTSVKNQ---GAAGSCWAFSTIENI--------EGQWalsgqPLVNLSVEQVVDCDGfedvtr 183
Cdd:cd02698     1 LPKSWDW--RNVngvnyVSPTRNQhipQYCGSCWAHGSTSALadriniarKGAW-----PSVYLSVQVVIDCAG------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 184 knADCgVFGGWPYLAYQYIMKTGgI--ESSRDYgycsgdtdtKHQENNCLPcpppgfnSTLCGPavpyCNMSQSCVAKLD 261
Cdd:cd02698    68 --GGS-CHGGDPGGVYEYAHKHG-IpdETCNPY---------QAKDGECNP-------FNRCGT----CNPFGECFAIKN 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 262 KSKFvkglKIADWKAIDKNETNIAEqLMKIGPLSIAMNA-DWLMFYRSGISSPYFCDPkSINHAVLLVGFGKEKTlfGEK 340
Cdd:cd02698   124 YTLY----FVSDYGSVSGRDKMMAE-IYARGPISCGIMAtEALENYTGGVYKEYVQDP-LINHIISVAGWGVDEN--GVE 195

                         250       260
                  ....*....|....*....|....*
gi 2118777167 341 lYWKVKNSWGPSWGEKGYFRIKRNA 365
Cdd:cd02698   196 -YWIVRNSWGEPWGERGWFRIVTSS 219
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
 120-375 3.56e-16

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 80.00  E-value: 3.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 120 LPDSFDWV-PKNVVT---SVKNQGAAGSCWAFSTIENIEGQW--ALS---GQPLVN-----LSVEQVVDCDGFedvtrkn 185
Cdd:PTZ00049  381 LPKNFTWGdPFNNNTreyDVTNQLLCGSCYIASQMYAFKRRIeiALTknlDKKYLNnfddlLSIQTVLSCSFY------- 453

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 186 aDCGVFGGWPYLAYQyIMKTGGIESSRDYGYcSGDTDTKHQENNCLPCPPPGFNSTLCGPAVPYCNMSQSCVAKLDKSKF 265
Cdd:PTZ00049  454 -DQGCNGGFPYLVSK-MAKLQGIPLDKVFPY-TATEQTCPYQVDQSANSMNGSANLRQINAVFFSSETQSDMHADFEAPI 530

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 266 VKglKIADWKAIDKN-------------ETNIAEQLMKIGPLSIAMNADWLMF-YRSGI----SSPY--FCD---PKS-- 320
Cdd:PTZ00049  531 SS--EPARWYAKDYNyiggcygcnqcngEKIMMNEIYRNGPIVASFEASPDFYdYADGVyyveDFPHarRCTvdlPKHng 608

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2118777167 321 ---------INHAVLLVGFGKEKTLFGEKLYWKVKNSWGPSWGEKGYFRIKRNAGTCGINTQVT 375
Cdd:PTZ00049  609 vynitgwekVNHAIVLVGWGEEEINGKLYKYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQSL 672
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 35-91 8.03e-16

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: 71.12  E-value: 8.03e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2118777167   35 FQTWKLENGKEYNGVNEEQKRFDVFYDNIKTINKYNKMYQPQTTFALNKFADMSPSE 91
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 35-92 5.16e-15

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 Swiss:Q70SU8. This family is classified as I29 by MEROPS.


Pssm-ID: 462410 [Multi-domain]  Cd Length: 58  Bit Score: 68.83  E-value: 5.16e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2118777167  35 FQTWKLENGKEYNGVNEEQKRFDVFYDNIKTINKYNKMYQPQTTFALNKFADMSPSEF 92
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGNVTYKLGLNKFADLTDEEF 58
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
 284-361 1.62e-09

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 59.69  E-value: 1.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  284 IAEQLMKIGPLSIAMNADWLMFYR-SGISSPYFCDPKSINHAVLLVGFGKEKTLFGEKL-YWKVKNSWGPSWGEKGYFRI 361
Cdd:PTZ00462   683 IKDEIMNKGSVIAYIKAENVLGYEfNGKKVQNLCGDDTADHAVNIVGYGNYINDEDEKKsYWIVRNSWGKYWGDEGYFKV 762
PepC COG3579
Aminopeptidase C [Amino acid transport and metabolism];
322-359 1.86e-06

Aminopeptidase C [Amino acid transport and metabolism];


Pssm-ID: 442798 [Multi-domain]  Cd Length: 440  Bit Score: 49.49  E-value: 1.86e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2118777167 322 NHAVLLVGFGKEKTlfGEKLYWKVKNSWGPSWGEKGYF 359
Cdd:COG3579   362 THAMVITGVDLDQN--GKPTRWKVENSWGDDNGYKGYF 397
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 89-377 2.51e-05

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 46.04  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167  89 PSEFHRKILMSDRKPPT--FENDRYIKGEKGFYLPDSFDWVP---KNVVTSVKNQGAA---GSCWAFSTIeniegqWALS 160
Cdd:PTZ00364  172 PTGDPYSKSRSARKAKTasFGFRQSFSHQLGDPPPAAWSWGDvggASFLPAAPPASPGrgcNSSYVEAAL------AAMM 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 161 GQPLVN------------LSVEQVVDCDGFEDvtrknadcGVFGGWPYLAYQYiMKTGGIESSRDY--GYCSGDTDTKhq 226
Cdd:PTZ00364  246 ARVMVAsnrtdplgqqtfLSARHVLDCSQYGQ--------GCAGGFPEEVGKF-AETFGILTTDSYyiPYDSGDGVER-- 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 227 enNCLPCPPPgfnstlcgpavpycnmsqscvaklDKSKFVKGLKIADWKAIDKNETNIAEQLMKIGPL--SIAMNADWlm 304
Cdd:PTZ00364  315 --ACKTRRPS------------------------RRYYFTNYGPLGGYYGAVTDPDEIIWEIYRHGPVpaSVYANSDW-- 366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2118777167 305 FYRSGISSPYFC-------------DPK------SINHAVLLVGFGKEKTlfGEKlYWKVKNSWG--PSWGEKGYFRIKR 363
Cdd:PTZ00364  367 YNCDENSTEDVRyvslddystasadRPLrhyfasNVNHTVLIIGWGTDEN--GGD-YWLVLDPWGsrRSWCDGGTRKIAR 443

                         330
                  ....*....|....
gi 2118777167 364 NAGTCGINTQVTTA 377
Cdd:PTZ00364  444 GVNAYNIESEVVVM 457
Peptidase_C1_2 pfam03051
Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, ...
 322-359 1.22e-04

Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, containing several prokaryotic and eukaryotic aminopeptidases and bleomycin hydrolases.


Pssm-ID: 397262  Cd Length: 438  Bit Score: 43.87  E-value: 1.22e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2118777167 322 NHAVLLVGFGKEKTlfGEKLYWKVKNSWGPSWGEKGYF 359
Cdd:pfam03051 360 THAMVLTGVDEDDD--GKPTKWKVENSWGEDSGEKGYF 395
Peptidase_C1B cd00585
Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin ...
 320-359 1.42e-03

Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin hydrolases (BH) and bacterial aminopeptidases C (pepC). The proteins of this subfamily contain a large insert relative to the C1A peptidase (papain) subfamily. BH is a cysteine peptidase 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. Bleomycin, a glycopeptide derived from the fungus Streptomyces verticullus, is an effective anticancer drug due to its ability to induce DNA strand breaks. Human BH is the major cause of tumor cell resistance to bleomycin chemotherapy, and is also genetically linked to Alzheimer's disease. In addition to its peptidase activity, the yeast BH (Gal6) binds DNA and acts as a repressor in the Gal4 regulatory system. BH forms a hexameric ring barrel structure with the active sites imbedded in the central channel. The bacterial homolog of BH, called pepC, is a cysteine aminopeptidase possessing broad specificity. Although its crystal structure has not been solved, biochemical analysis shows that pepC also forms a hexamer.


Pssm-ID: 238328 [Multi-domain]  Cd Length: 437  Bit Score: 40.65  E-value: 1.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2118777167 320 SINHAVLLVGFGKEKTlfGEKLYWKVKNSWGPSWGEKGYF 359
Cdd:cd00585   357 LMTHAMVLTGVDLDED--GKPVKWKVENSWGEKVGKKGYF 394
 
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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