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Conserved domains on  [gi|18424347|ref|NP_568921|]
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aleurain-like protease [Arabidopsis thaliana]

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;
141-356 2.16e-116

Papain family cysteine protease;


:

Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 336.05  E-value: 2.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   141 LPETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGafNNYGCNGGLPSQAFEYIKSN 220
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDT--FNNGCNGGLPDNAFEYIKKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   221 GGLDTEKAYPYTGKDETCKFSAENVG-VQVLNSVNITLGAEDELKHAVGLVRPVSIAFEVIH-SFRLYKSGVYTDSHCGS 298
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNSKvAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18424347   299 TpmdVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKMEMGKN-MCGIATCASYPV 356
Cdd:pfam00112 159 E---LNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 59-114 2.08e-18

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: 78.05  E-value: 2.08e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18424347     59 FARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRSTNKKG-LSYKLGVNQFADLTWQE 114
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYeHSYKLGVNQFSDLTPEE 57
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
141-356 2.16e-116

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 336.05  E-value: 2.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   141 LPETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGafNNYGCNGGLPSQAFEYIKSN 220
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDT--FNNGCNGGLPDNAFEYIKKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   221 GGLDTEKAYPYTGKDETCKFSAENVG-VQVLNSVNITLGAEDELKHAVGLVRPVSIAFEVIH-SFRLYKSGVYTDSHCGS 298
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNSKvAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18424347   299 TpmdVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKMEMGKN-MCGIATCASYPV 356
Cdd:pfam00112 159 E---LNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 142-355 2.26e-115

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: 333.44  E-value: 2.26e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 142 PETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGAFNNyGCNGGLPSQAFEYIKsNG 221
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNN-GCNGGNPDNAFEYVK-NG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 222 GLDTEKAYPYTGKDETCKFSAENVGVQVLNSVNITLGAEDELKHAVGLVRPVSIAFEVIHSFRLYKSGVYTDSHCgsTPM 301
Cdd:cd02248  79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASSSFQFYKGGIYSGPCC--SNT 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 18424347 302 DVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKMEMGKNMCGIATCASYP 355
Cdd:cd02248 157 NLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
141-355 1.71e-87

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 260.98  E-value: 1.71e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347    141 LPETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGaFNNYGCNGGLPSQAFEYIKSN 220
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSG-GGNCGCNGGLPDNAFEYIKKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347    221 GGLDTEKAYPYTGkdetckfsaenvgvqvlnsvnitlgaedelkhavglvrpvsIAFEVIHSFRLYKSGVYTDSHCGSTp 300
Cdd:smart00645  80 GGLETESCYPYTG-----------------------------------------SVAIDASDFQFYKSGIYDHPGCGSG- 117

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 18424347    301 mDVNHAVLAVGYGV--EDGVPYWLIKNSWGADWGDKGYFKMEMGK-NMCGI-ATCASYP 355
Cdd:smart00645 118 -TLDHAVLIVGYGTevENGKDYWIVKNSWGTDWGENGYFRIARGKnNECGIeASVASYP 175
PTZ00021 PTZ00021
falcipain-2; Provisional
 29-357 7.88e-78

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 246.99  E-value: 7.88e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   29 SNPIRMVSDGLREVEESVSQILGQSR-------HVLSFARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRS-TNKKGLSY 100
Cdd:PTZ00021 132 VENFRKNFGNLKNVKKVYLINFADSKflmtnleNVNSFYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAhNNKENVLY 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  101 KLGVNQFADLTWQEFQRTKLgaaqncsaTLKGS---------------------HKVTEAALPETK-DWREDGIVSPVKD 158
Cdd:PTZ00021 212 KKGMNRFGDLSFEEFKKKYL--------TLKSFdfksngkksprvinyddvikkYKPKDATFDHAKyDWRLHNGVTPVKD 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  159 QGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCagAFNNYGCNGGLPSQAFEYIKSNGGLDTEKAYPYTG-KDET 237
Cdd:PTZ00021 284 QKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDC--SFKNNGCYGGLIPNAFEDMIELGGLCSEDDYPYVSdTPEL 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  238 CKFSAENVGVQVLNSVNItlgAEDELKHAVGLVRPVSIAFEVIHSFRLYKSGVYtDSHCGSTPmdvNHAVLAVGYGVEDG 317
Cdd:PTZ00021 362 CNIDRCKEKYKIKSYVSI---PEDKFKEAIRFLGPISVSIAVSDDFAFYKGGIF-DGECGEEP---NHAVILVGYGMEEI 434

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18424347  318 VP----------YWLIKNSWGADWGDKGYFKMEMGKN----MCGIATCASYPVV 357
Cdd:PTZ00021 435 YNsdtkkmekryYYIIKNSWGESWGEKGFIRIETDENglmkTCSLGTEAYVPLI 488
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
138-339 3.66e-40

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 146.82  E-value: 3.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 138 EAALPETKDWRedGIVSPVKDQGGCGSCWTFSTTGALEAAY---HQAFGKGISLSEQQLVDCA---GAFNNYGCNGGLPS 211
Cdd:COG4870   1 AAALPSSVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLkkqAGAPGTSLDLSELFLYNQArngDGTEGTDDGGSSLR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 212 QAFEYIKSNGgLDTEKAYPYTGKDETCKFSA----ENVGVQVLNSVNITLGAE----DELKHAVGLVRPVSIAFEVIHSF 283
Cdd:COG4870  79 DALKLLRWSG-VVPESDWPYDDSDFTSQPSAaayaDARNYKIQDYYRLPGGGGatdlDAIKQALAEGGPVVFGFYVYESF 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18424347 284 RLYKSGVYTDShcGSTPMDVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKM 339
Cdd:COG4870 158 YNYTGGVYYPT--PGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 59-114 2.08e-18

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: 78.05  E-value: 2.08e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18424347     59 FARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRSTNKKG-LSYKLGVNQFADLTWQE 114
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYeHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 59-115 2.15e-18

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: 78.07  E-value: 2.15e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18424347    59 FARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRSTNKKG-LSYKLGVNQFADLTWQEF 115
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGnVTYKLGLNKFADLTDEEF 58
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
141-356 2.16e-116

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 336.05  E-value: 2.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   141 LPETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGafNNYGCNGGLPSQAFEYIKSN 220
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDT--FNNGCNGGLPDNAFEYIKKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   221 GGLDTEKAYPYTGKDETCKFSAENVG-VQVLNSVNITLGAEDELKHAVGLVRPVSIAFEVIH-SFRLYKSGVYTDSHCGS 298
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNSKvAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18424347   299 TpmdVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKMEMGKN-MCGIATCASYPV 356
Cdd:pfam00112 159 E---LNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 142-355 2.26e-115

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: 333.44  E-value: 2.26e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 142 PETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGAFNNyGCNGGLPSQAFEYIKsNG 221
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNN-GCNGGNPDNAFEYVK-NG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 222 GLDTEKAYPYTGKDETCKFSAENVGVQVLNSVNITLGAEDELKHAVGLVRPVSIAFEVIHSFRLYKSGVYTDSHCgsTPM 301
Cdd:cd02248  79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASSSFQFYKGGIYSGPCC--SNT 156

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 18424347 302 DVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKMEMGKNMCGIATCASYP 355
Cdd:cd02248 157 NLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
141-355 1.71e-87

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 260.98  E-value: 1.71e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347    141 LPETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGaFNNYGCNGGLPSQAFEYIKSN 220
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSG-GGNCGCNGGLPDNAFEYIKKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347    221 GGLDTEKAYPYTGkdetckfsaenvgvqvlnsvnitlgaedelkhavglvrpvsIAFEVIHSFRLYKSGVYTDSHCGSTp 300
Cdd:smart00645  80 GGLETESCYPYTG-----------------------------------------SVAIDASDFQFYKSGIYDHPGCGSG- 117

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 18424347    301 mDVNHAVLAVGYGV--EDGVPYWLIKNSWGADWGDKGYFKMEMGK-NMCGI-ATCASYP 355
Cdd:smart00645 118 -TLDHAVLIVGYGTevENGKDYWIVKNSWGTDWGENGYFRIARGKnNECGIeASVASYP 175
PTZ00021 PTZ00021
falcipain-2; Provisional
 29-357 7.88e-78

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 246.99  E-value: 7.88e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   29 SNPIRMVSDGLREVEESVSQILGQSR-------HVLSFARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRS-TNKKGLSY 100
Cdd:PTZ00021 132 VENFRKNFGNLKNVKKVYLINFADSKflmtnleNVNSFYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAhNNKENVLY 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  101 KLGVNQFADLTWQEFQRTKLgaaqncsaTLKGS---------------------HKVTEAALPETK-DWREDGIVSPVKD 158
Cdd:PTZ00021 212 KKGMNRFGDLSFEEFKKKYL--------TLKSFdfksngkksprvinyddvikkYKPKDATFDHAKyDWRLHNGVTPVKD 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  159 QGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCagAFNNYGCNGGLPSQAFEYIKSNGGLDTEKAYPYTG-KDET 237
Cdd:PTZ00021 284 QKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDC--SFKNNGCYGGLIPNAFEDMIELGGLCSEDDYPYVSdTPEL 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  238 CKFSAENVGVQVLNSVNItlgAEDELKHAVGLVRPVSIAFEVIHSFRLYKSGVYtDSHCGSTPmdvNHAVLAVGYGVEDG 317
Cdd:PTZ00021 362 CNIDRCKEKYKIKSYVSI---PEDKFKEAIRFLGPISVSIAVSDDFAFYKGGIF-DGECGEEP---NHAVILVGYGMEEI 434

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18424347  318 VP----------YWLIKNSWGADWGDKGYFKMEMGKN----MCGIATCASYPVV 357
Cdd:PTZ00021 435 YNsdtkkmekryYYIIKNSWGESWGEKGFIRIETDENglmkTCSLGTEAYVPLI 488
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 59-358 1.03e-69

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 221.88  E-value: 1.03e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   59 FARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRSTNKKGLSYKLGVNQFADLTWQEFQRTKLGAAQNCSATLK--GSH-- 134
Cdd:PTZ00203  38 FEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHARFGITKFFDLSEAEFAARYLNGAAYFAAAKQhaGQHyr 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  135 --KVTEAALPETKDWREDGIVSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGAFNnyGCNGGLPSQ 212
Cdd:PTZ00203 118 kaRADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDN--GCGGGLMLQ 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  213 AFEYI--KSNGGLDTEKAYPYT---GKDETCKFSAENV-GVQVLNSVNITlGAEDELKHAVGLVRPVSIAFEViHSFRLY 286
Cdd:PTZ00203 196 AFEWVlrNMNGTVFTEKSYPYVsgnGDVPECSNSSELApGARIDGYVSME-SSERVMAAWLAKNGPISIAVDA-SSFMSY 273

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18424347  287 KSGVYTDshcgSTPMDVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKMEMGKNMCGIatcASYPVVA 358
Cdd:PTZ00203 274 HSGVLTS----CIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLL---TGYPVSV 338
PTZ00200 PTZ00200
cysteine proteinase; Provisional
 57-350 8.43e-68

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 219.95  E-value: 8.43e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   57 LSFARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRS-TNKKGlsYKLGVNQFADLTWQEFQR------------------ 117
Cdd:PTZ00200 124 LEFEEFNKKYNRKHATHAERLNRFLTFRNNYLEVKShKGDEP--YSKEINKFSDLTEEEFRKlfpvikvppksnstshnn 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  118 -------------TKLGAAQNCSATLKGSHKVTeaalPETKDWREDGIVSPVKDQGG-CGSCWTFSTTGALEAAYHQAFG 183
Cdd:PTZ00200 202 dfkarhvsnptylKNLKKAKNTDEDVKDPSKIT----GEGLDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRD 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  184 KGISLSEQQLVDCAgaFNNYGCNGGLPSQAFEYIKSNGgLDTEKAYPYTGKDETCKFSAENVgvQVLNSVNITLGAEDEL 263
Cdd:PTZ00200 278 KSVDLSEQELVNCD--TKSQGCSGGYPDTALEYVKNKG-LSSSSDVPYLAKDGKCVVSSTKK--VYIDSYLVAKGKDVLN 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  264 KHAVglVRPVSIAFEVIHSFRLYKSGVYtDSHCGSTPmdvNHAVLAVGYGVED--GVPYWLIKNSWGADWGDKGYFKME- 340
Cdd:PTZ00200 353 KSLV--ISPTVVYIAVSRELLKYKSGVY-NGECGKSL---NHAVLLVGEGYDEktKKRYWIIKNSWGTDWGENGYMRLEr 426

                        330
                 ....*....|..
gi 18424347  341 --MGKNMCGIAT 350
Cdd:PTZ00200 427 tnEGTDKCGILT 438
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
 141-358 1.75e-46

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: 158.32  E-value: 1.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 141 LPETKDWREDGI----VSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGIS------LSEQQLVDCAgaFNNYGCNGGLP 210
Cdd:cd02621   1 LPKSFDWGDVNNgfnyVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPlgqqpiLSPQHVLSCS--QYSQGCDGGFP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 211 SQAFEYIKSNGgLDTEKAYPYTGKDE-TCKFSAENVG---VQVLNSVNITLGA--EDELKHAVGLVRPVSIAFEVIHSFR 284
Cdd:cd02621  79 FLVGKFAEDFG-IVTEDYFPYTADDDrPCKASPSECRryyFSDYNYVGGCYGCtnEDEMKWEIYRNGPIVVAFEVYSDFD 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 285 LYKSGVY---TDSHCGSTPMD-------VNHAVLAVGYGVED--GVPYWLIKNSWGADWGDKGYFKMEMGKNMCGIatcA 352
Cdd:cd02621 158 FYKEGVYhhtDNDEVSDGDNDnfnpfelTNHAVLLVGWGEDEikGEKYWIVKNSWGSSWGEKGYFKIRRGTNECGI---E 234


                ....*.
gi 18424347 353 SYPVVA 358
Cdd:cd02621 235 SQAVFA 240
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
 153-348 1.01e-45

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: 156.28  E-value: 1.01e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 153 VSPVKDQGGCGSCWTFSTTGALeAAYHQAFGKG---ISLSEQQLVDCAGaFNNYGCNGGLPSQAFEYIKSNGgLDTEKAY 229
Cdd:cd02620  16 IGEIRDQGNCGSCWAFSAVEAF-SDRLCIQSNGkenVLLSAQDLLSCCS-GCGDGCNGGYPDAAWKYLTTTG-VVTGGCQ 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 230 PYT----GKDETCKFSAENVGVQVLNSVNITLGAEDELKH------AVGLVR-----------PVSIAFEVIHSFRLYKS 288
Cdd:cd02620  93 PYTippcGHHPEGPPPCCGTPYCTPKCQDGCEKTYEEDKHkgksaySVPSDEtdimkeimtngPVQAAFTVYEDFLYYKS 172

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 289 GVYtdSHCGSTPMDVnHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKMEMGKNMCGI 348
Cdd:cd02620 173 GVY--QHTSGKQLGG-HAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNECGI 229
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 146-354 2.47e-43

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: 149.59  E-value: 2.47e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 146 DWREDGIvSPVKDQGGCGSCWTFSTTGALEAAYHQAFGKG--ISLSEQQLVDCAG---AFNNYGCNGGLPSQAFEYIKSN 220
Cdd:cd02619   3 DLRPLRL-TPVKNQGSRGSCWAFASAYALESAYRIKGGEDeyVDLSPQYLYICANdecLGINGSCDGGGPLSALLKLVAL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 221 GGLDTEKAYPYTGKDETCKFS---AENVGVQVLNSVNITL-GAEDELKHAVGLVRPVSIAFEVIHSFRLYKSGVYTDSH- 295
Cdd:cd02619  82 KGIPPEEDYPYGAESDGEEPKseaALNAAKVKLKDYRRVLkNNIEDIKEALAKGGPVVAGFDVYSGFDRLKEGIIYEEIv 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18424347 296 --CGSTPMDVNHAVLAVGYGVE--DGVPYWLIKNSWGADWGDKGYFKMEMgKNMCGIATCASY 354
Cdd:cd02619 162 ylLYEDGDLGGHAVVIVGYDDNyvEGKGAFIVKNSWGTDWGDNGYGRISY-EDVYEMTFGANV 223
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
138-339 3.66e-40

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 146.82  E-value: 3.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 138 EAALPETKDWRedGIVSPVKDQGGCGSCWTFSTTGALEAAY---HQAFGKGISLSEQQLVDCA---GAFNNYGCNGGLPS 211
Cdd:COG4870   1 AAALPSSVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLkkqAGAPGTSLDLSELFLYNQArngDGTEGTDDGGSSLR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 212 QAFEYIKSNGgLDTEKAYPYTGKDETCKFSA----ENVGVQVLNSVNITLGAE----DELKHAVGLVRPVSIAFEVIHSF 283
Cdd:COG4870  79 DALKLLRWSG-VVPESDWPYDDSDFTSQPSAaayaDARNYKIQDYYRLPGGGGatdlDAIKQALAEGGPVVFGFYVYESF 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18424347 284 RLYKSGVYTDShcGSTPMDVNHAVLAVGYGVEDGVPYWLIKNSWGADWGDKGYFKM 339
Cdd:COG4870 158 YNYTGGVYYPT--PGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
 141-343 1.99e-32

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: 121.37  E-value: 1.99e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 141 LPETKDWRE-DGI--VSPVKDQ---GGCGSCWTFSTTGALEAAYH---QAFGKGISLSEQQLVDCAGAFNnygCNGGLPS 211
Cdd:cd02698   1 LPKSWDWRNvNGVnyVSPTRNQhipQYCGSCWAHGSTSALADRINiarKGAWPSVYLSVQVVIDCAGGGS---CHGGDPG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347 212 QAFEYIKSNGGLDtEKAYPYTGKDE---------TCKFSAENVGVQVLNSVNI----TLGAEDELKHAVGLVRPVSIAFE 278
Cdd:cd02698  78 GVYEYAHKHGIPD-ETCNPYQAKDGecnpfnrcgTCNPFGECFAIKNYTLYFVsdygSVSGRDKMMAEIYARGPISCGIM 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18424347 279 VIHSFRLYKSGVYTDShcGSTPMdVNHAVLAVGYGVED-GVPYWLIKNSWGADWGDKGYFKMEMGK 343
Cdd:cd02698 157 ATEALENYTGGVYKEY--VQDPL-INHIISVAGWGVDEnGVEYWIVRNSWGEPWGERGWFRIVTSS 219
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
 123-354 5.43e-22

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 97.33  E-value: 5.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  123 AQNCSATLKGSHKVTEAA-LPETKDW--------REDgivsPVKDQGGCGSCWTFSTTGALEAAYHQAFGKGIS------ 187
Cdd:PTZ00049 362 LENYEDTEKAPHRELEIDeLPKNFTWgdpfnnntREY----DVTNQLLCGSCYIASQMYAFKRRIEIALTKNLDkkylnn 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  188 ----LSEQQLVDCAgaFNNYGCNGGLPSQAFEYIKSNGgLDTEKAYPYTGKDETC-----KFSAENVGVQVLNSVNITLG 258
Cdd:PTZ00049 438 fddlLSIQTVLSCS--FYDQGCNGGFPYLVSKMAKLQG-IPLDKVFPYTATEQTCpyqvdQSANSMNGSANLRQINAVFF 514

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  259 ------------------------AED--------ELKHAVG-------LVR--PVSIAFEVIHSFRLYKSGVY---TDS 294
Cdd:PTZ00049 515 ssetqsdmhadfeapisseparwyAKDynyiggcyGCNQCNGekimmneIYRngPIVASFEASPDFYDYADGVYyveDFP 594

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18424347  295 HCGSTPMD---------------VNHAVLAVGYGVE--DGVP--YWLIKNSWGADWGDKGYFKMEMGKNMCGIATCASY 354
Cdd:PTZ00049 595 HARRCTVDlpkhngvynitgwekVNHAIVLVGWGEEeiNGKLykYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQSLF 673
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 59-114 2.08e-18

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: 78.05  E-value: 2.08e-18
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18424347     59 FARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRSTNKKG-LSYKLGVNQFADLTWQE 114
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYeHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 59-115 2.15e-18

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: 78.07  E-value: 2.15e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18424347    59 FARFTHRYGKKYQNVEEMKLRFSIFKENLDLIRSTNKKG-LSYKLGVNQFADLTWQEF 115
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGnVTYKLGLNKFADLTDEEF 58
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 141-358 7.40e-16

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 78.78  E-value: 7.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  141 LPETKDWREDGIVS---PVKDQG---GCGSCWTFSTTGALEAAYHQA------FGKGISLSEQQLVDCagafNNY--GCN 206
Cdd:PTZ00364 205 PPAAWSWGDVGGASflpAAPPASpgrGCNSSYVEAALAAMMARVMVAsnrtdpLGQQTFLSARHVLDC----SQYgqGCA 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  207 GGLPSQAFEYIKSNGGLDTEKAY-PYTGKD---ETCKFSAENV-----GVQVLNSVNITLGAEDELKHAV---GLVrPVS 274
Cdd:PTZ00364 281 GGFPEEVGKFAETFGILTTDSYYiPYDSGDgveRACKTRRPSRryyftNYGPLGGYYGAVTDPDEIIWEIyrhGPV-PAS 359

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347  275 I-----AFEVIHSFRLYKSGVYTDSHCGSTP---------MDVNHAVLAVGYGV-EDGVPYWLIKNSWGA--DWGDKGYF 337
Cdd:PTZ00364 360 VyansdWYNCDENSTEDVRYVSLDDYSTASAdrplrhyfaSNVNHTVLIIGWGTdENGGDYWLVLDPWGSrrSWCDGGTR 439

                        250       260
                 ....*....|....*....|.
gi 18424347  338 KMEMGKNMCGIatcASYPVVA 358
Cdd:PTZ00364 440 KIARGVNAYNI---ESEVVVM 457
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
 156-346 3.50e-11

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 64.70  E-value: 3.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   156 VKDQGGCGSCWTFSTTGALEAAYHQAFGKGISLSEQQLVDCAGAFNNYGCN-GGLPSQAFEYIKSNGGLDTEKAYPY--T 232
Cdd:PTZ00462  547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCSKGEHKDRCDeGSNPLEFLQIIEDNGFLPADSNYLYnyT 626

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18424347   233 GKDETCKfSAENVGVQVLNSVNI---------TLGAE-----------DELKHAVGLVRP------VSIAFEVIHSFRLY 286
Cdd:PTZ00462  627 KVGEDCP-DEEDHWMNLLDHGKIlnhnkkepnSLDGKayrayesehfhDKMDAFIKIIKDeimnkgSVIAYIKAENVLGY 705

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18424347   287 K-SGVYTDSHCGSTPMDvnHAVLAVGYG-----VEDGVPYWLIKNSWGADWGDKGYFKMEM-GKNMC 346
Cdd:PTZ00462  706 EfNGKKVQNLCGDDTAD--HAVNIVGYGnyindEDEKKSYWIVRNSWGKYWGDEGYFKVDMyGPSHC 770
PepC COG3579
Aminopeptidase C [Amino acid transport and metabolism];
297-339 1.87e-06

Aminopeptidase C [Amino acid transport and metabolism];


Pssm-ID: 442798 [Multi-domain]  Cd Length: 440  Bit Score: 49.49  E-value: 1.87e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18424347 297 GSTPMDvnHAVLAVGYGV-EDGVP-YWLIKNSWGADWGDKGYFKM 339
Cdd:COG3579 357 GESTDT--HAMVITGVDLdQNGKPtRWKVENSWGDDNGYKGYFYM 399
Peptidase_C1B cd00585
Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin ...
 297-339 8.05e-05

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: 44.12  E-value: 8.05e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18424347 297 GSTPMdvNHAVLAVGYGV-EDGVPY-WLIKNSWGADWGDKGYFKM 339
Cdd:cd00585 354 GESLM--THAMVLTGVDLdEDGKPVkWKVENSWGEKVGKKGYFVM 396
Peptidase_C1_2 pfam03051
Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, ...
 303-339 3.68e-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: 42.33  E-value: 3.68e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 18424347   303 VNHAVLAVGYGV-EDGVPY-WLIKNSWGADWGDKGYFKM 339
Cdd:pfam03051 359 MTHAMVLTGVDEdDDGKPTkWKVENSWGEDSGEKGYFVM 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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