|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
120-336 |
1.51e-130 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 371.10 E-value: 1.51e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 120 VPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKygNHGCNGGLMDQAFEYIRDN 199
Cdd:pfam00112 1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTF--NNGCNGGLPDNAFEYIKKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 200 HGVDTEESYPYKGRDMKCHFNKKTVG-ADDKGYVDTPEGDEEQLKIAVATQGPISIAIDAGHRSFQLYKKGVYYDEECSS 278
Cdd:pfam00112 79 GGIVTESDYPYTAKDGTCKFKKSNSKvAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74959463 279 eELDHGVLLVGYGTDpEHGDYWIVKNSWGAGWGEKGYIRIARNRNNHCGVATKASYPL 336
Cdd:pfam00112 159 -ELNHAVLLVGYGTE-NGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
121-335 |
5.03e-122 |
|
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: 349.23 E-value: 5.03e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 121 PDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKyGNHGCNGGLMDQAFEYIRdNH 200
Cdd:cd02248 1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEYVK-NG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 201 GVDTEESYPYKGRDMKCHFNKKTVGADDKGYVDTPEGDEEQLKIAVATQGPISIAIDAGHrSFQLYKKGVYYDEECSSEE 280
Cdd:cd02248 79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNTN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 74959463 281 LDHGVLLVGYGTDpEHGDYWIVKNSWGAGWGEKGYIRIARNrNNHCGVATKASYP 335
Cdd:cd02248 158 LNHAVLLVGYGTE-NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
120-335 |
4.21e-96 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 282.16 E-value: 4.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 120 VPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKyGNHGCNGGLMDQAFEYIRDN 199
Cdd:smart00645 1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGG-GNCGCNGGLPDNAFEYIKKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 200 HGVDTEESYPYKGrdmkchfnkktvgaddkgyvdtpegdeeqlkiavatqgpiSIAIDAGHrsFQLYKKGVYYDEECSSE 279
Cdd:smart00645 80 GGLETESCYPYTG----------------------------------------SVAIDASD--FQFYKSGIYDHPGCGSG 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74959463 280 ELDHGVLLVGYGTDPEHG-DYWIVKNSWGAGWGEKGYIRIARNRNNHCGV-ATKASYP 335
Cdd:smart00645 118 TLDHAVLIVGYGTEVENGkDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
|
|
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
32-323 |
2.69e-65 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 209.94 E-value: 2.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 32 WDDYKEDFDKEYSE-SEEQTYMEAFVKNMIHIenhnRDHRLGRKTFEMGLNHIADLPFSQY--RKLNGYR-----RLFGD 103
Cdd:PTZ00203 38 FEEFKRTYQRAYGTlTEEQQRLANFERNLELM----REHQARNPHARFGITKFFDLSEAEFaaRYLNGAAyfaaaKQHAG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 104 SRIKNSSSFLApfnvQVPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKygNHG 183
Cdd:PTZ00203 114 QHYRKARADLS----AVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHV--DNG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 184 CNGGLMDQAFEYI-RDNHG-VDTEESYPY---KGRDMKCHFNKKTV-GADDKGYVdTPEGDEEQLKIAVATQGPISIAID 257
Cdd:PTZ00203 188 CGGGLMLQAFEWVlRNMNGtVFTEKSYPYvsgNGDVPECSNSSELApGARIDGYV-SMESSERVMAAWLAKNGPISIAVD 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74959463 258 AGhrSFQLYKKGVYydEECSSEELDHGVLLVGYGTDPEHgDYWIVKNSWGAGWGEKGYIRIARNRN 323
Cdd:PTZ00203 267 AS--SFMSYHSGVL--TSCIGEQLNHGVLLVGYNMTGEV-PYWVIKNSWGEDWGEKGYVRVTMGVN 327
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
120-318 |
1.15e-41 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 149.90 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 120 VPDEVDWRDthLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVS---LSEQNLVDCSTK-YGNHG--CNGGLMDQAF 193
Cdd:COG4870 4 LPSSVDLRG--YVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNQARNgDGTEGtdDGGSSLRDAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 194 EYIRdNHGVDTEESYPYKGRDMK------CHFNKKTVGADDKGYVDTPEG--DEEQLKIAVATQGPISIAIdAGHRSFQL 265
Cdd:COG4870 82 KLLR-WSGVVPESDWPYDDSDFTsqpsaaAYADARNYKIQDYYRLPGGGGatDLDAIKQALAEGGPVVFGF-YVYESFYN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 74959463 266 YKKGVYYDEECSSEELDHGVLLVGYgTDPEHGDYWIVKNSWGAGWGEKGYIRI 318
Cdd:COG4870 160 YTGGVYYPTPGDASLGGHAVAIVGY-DDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| Inhibitor_I29 |
pfam08246 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
32-91 |
6.23e-10 |
|
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: 54.19 E-value: 6.23e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74959463 32 WDDYKEDFDKEY-SESEEQTYMEAFVKNMIHIENHNRDhrlGRKTFEMGLNHIADLPFSQY 91
Cdd:pfam08246 1 FDDWMKKYGKSYrSEEEELYRFQIFKENLKRIEEHNSN---GNVTYKLGLNKFADLTDEEF 58
|
|
| Inhibitor_I29 |
smart00848 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
32-86 |
6.09e-09 |
|
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: 51.48 E-value: 6.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 74959463 32 WDDYKEDFDKEY-SESEEQTYMEAFVKNMIHIENHNRDHrlgRKTFEMGLNHIADL 86
Cdd:smart00848 1 FEQWKKKHGKSYsSEEEEARRFAIFKENLKKIEEHNKKY---EHSYKLGVNQFSDL 53
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
120-336 |
1.51e-130 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 371.10 E-value: 1.51e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 120 VPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKygNHGCNGGLMDQAFEYIRDN 199
Cdd:pfam00112 1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTF--NNGCNGGLPDNAFEYIKKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 200 HGVDTEESYPYKGRDMKCHFNKKTVG-ADDKGYVDTPEGDEEQLKIAVATQGPISIAIDAGHRSFQLYKKGVYYDEECSS 278
Cdd:pfam00112 79 GGIVTESDYPYTAKDGTCKFKKSNSKvAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74959463 279 eELDHGVLLVGYGTDpEHGDYWIVKNSWGAGWGEKGYIRIARNRNNHCGVATKASYPL 336
Cdd:pfam00112 159 -ELNHAVLLVGYGTE-NGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
121-335 |
5.03e-122 |
|
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: 349.23 E-value: 5.03e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 121 PDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKyGNHGCNGGLMDQAFEYIRdNH 200
Cdd:cd02248 1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEYVK-NG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 201 GVDTEESYPYKGRDMKCHFNKKTVGADDKGYVDTPEGDEEQLKIAVATQGPISIAIDAGHrSFQLYKKGVYYDEECSSEE 280
Cdd:cd02248 79 GLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNTN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 74959463 281 LDHGVLLVGYGTDpEHGDYWIVKNSWGAGWGEKGYIRIARNrNNHCGVATKASYP 335
Cdd:cd02248 158 LNHAVLLVGYGTE-NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
120-335 |
4.21e-96 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 282.16 E-value: 4.21e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 120 VPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKyGNHGCNGGLMDQAFEYIRDN 199
Cdd:smart00645 1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGG-GNCGCNGGLPDNAFEYIKKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 200 HGVDTEESYPYKGrdmkchfnkktvgaddkgyvdtpegdeeqlkiavatqgpiSIAIDAGHrsFQLYKKGVYYDEECSSE 279
Cdd:smart00645 80 GGLETESCYPYTG----------------------------------------SVAIDASD--FQFYKSGIYDHPGCGSG 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 74959463 280 ELDHGVLLVGYGTDPEHG-DYWIVKNSWGAGWGEKGYIRIARNRNNHCGV-ATKASYP 335
Cdd:smart00645 118 TLDHAVLIVGYGTEVENGkDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
|
|
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
32-323 |
2.69e-65 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 209.94 E-value: 2.69e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 32 WDDYKEDFDKEYSE-SEEQTYMEAFVKNMIHIenhnRDHRLGRKTFEMGLNHIADLPFSQY--RKLNGYR-----RLFGD 103
Cdd:PTZ00203 38 FEEFKRTYQRAYGTlTEEQQRLANFERNLELM----REHQARNPHARFGITKFFDLSEAEFaaRYLNGAAyfaaaKQHAG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 104 SRIKNSSSFLApfnvQVPDEVDWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKygNHG 183
Cdd:PTZ00203 114 QHYRKARADLS----AVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHV--DNG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 184 CNGGLMDQAFEYI-RDNHG-VDTEESYPY---KGRDMKCHFNKKTV-GADDKGYVdTPEGDEEQLKIAVATQGPISIAID 257
Cdd:PTZ00203 188 CGGGLMLQAFEWVlRNMNGtVFTEKSYPYvsgNGDVPECSNSSELApGARIDGYV-SMESSERVMAAWLAKNGPISIAVD 266
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74959463 258 AGhrSFQLYKKGVYydEECSSEELDHGVLLVGYGTDPEHgDYWIVKNSWGAGWGEKGYIRIARNRN 323
Cdd:PTZ00203 267 AS--SFMSYHSGVL--TSCIGEQLNHGVLLVGYNMTGEV-PYWVIKNSWGEDWGEKGYVRVTMGVN 327
|
|
| PTZ00021 |
PTZ00021 |
falcipain-2; Provisional |
41-337 |
9.13e-62 |
|
falcipain-2; Provisional
Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 204.62 E-value: 9.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 41 KEYSESEE-QTYMEAFVKNMIHIENHN-RDHRLGRKtfemGLNHIADLPFSQYRKLNGYRRLFG-DSRIKNSSSFLAPFN 117
Cdd:PTZ00021 178 KKYQTPDEmQQRYLSFVENLAKINAHNnKENVLYKK----GMNRFGDLSFEEFKKKYLTLKSFDfKSNGKKSPRVINYDD 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 118 V----QVPDEV------DWRDTHLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKygNHGCNGG 187
Cdd:PTZ00021 254 VikkyKPKDATfdhakyDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSFK--NNGCYGG 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 188 LMDQAFEYIRDNHGVDTEESYPYKG-RDMKCHFNKKTVGADDKGYVDTPegdEEQLKIAVATQGPISIAIdAGHRSFQLY 266
Cdd:PTZ00021 332 LIPNAFEDMIELGGLCSEDDYPYVSdTPELCNIDRCKEKYKIKSYVSIP---EDKFKEAIRFLGPISVSI-AVSDDFAFY 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 267 KKGVyYDEECsSEELDHGVLLVGYGT----DPEHGD-----YWIVKNSWGAGWGEKGYIRIARNRNNH---CGVATKASY 334
Cdd:PTZ00021 408 KGGI-FDGEC-GEEPNHAVILVGYGMeeiyNSDTKKmekryYYIIKNSWGESWGEKGFIRIETDENGLmktCSLGTEAYV 485
|
...
gi 74959463 335 PLV 337
Cdd:PTZ00021 486 PLI 488
|
|
| PTZ00200 |
PTZ00200 |
cysteine proteinase; Provisional |
33-330 |
6.91e-55 |
|
cysteine proteinase; Provisional
Pssm-ID: 240310 [Multi-domain] Cd Length: 448 Bit Score: 185.67 E-value: 6.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 33 DDYKEDFDKEY-SESEEQTYMEAFVKNMIHIENHNrdhrlGRKTFEMGLNHIADLPFSQYRKLNGYRRLFGDSRIKNSSS 111
Cdd:PTZ00200 127 EEFNKKYNRKHaTHAERLNRFLTFRNNYLEVKSHK-----GDEPYSKEINKFSDLTEEEFRKLFPVIKVPPKSNSTSHNN 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 112 FLAPFNVQVPD------------------------EVDWRDTHLVTDVKNQG-MCGSCWAFSATGALEGQHARKLGQLVS 166
Cdd:PTZ00200 202 DFKARHVSNPTylknlkkakntdedvkdpskitgeGLDWRRADAVTKVKDQGlNCGSCWAFSSVGSVESLYKIYRDKSVD 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 167 LSEQNLVDCSTKygNHGCNGGLMDQAFEYIRdNHGVDTEESYPYKGRDMKCHFNKKtvgadDKGYVDT---PEGDEeqlk 243
Cdd:PTZ00200 282 LSEQELVNCDTK--SQGCSGGYPDTALEYVK-NKGLSSSSDVPYLAKDGKCVVSST-----KKVYIDSylvAKGKD---- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 244 iaVATQ----GPISIAIdAGHRSFQLYKKGVYyDEECSSEeLDHGVLLVGYGTDPEHGD-YWIVKNSWGAGWGEKGYIRI 318
Cdd:PTZ00200 350 --VLNKslviSPTVVYI-AVSRELLKYKSGVY-NGECGKS-LNHAVLLVGEGYDEKTKKrYWIIKNSWGTDWGENGYMRL 424
|
330
....*....|....
gi 74959463 319 ARNR--NNHCGVAT 330
Cdd:PTZ00200 425 ERTNegTDKCGILT 438
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
120-318 |
1.15e-41 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 149.90 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 120 VPDEVDWRDthLVTDVKNQGMCGSCWAFSATGALEGQHARKLGQLVS---LSEQNLVDCSTK-YGNHG--CNGGLMDQAF 193
Cdd:COG4870 4 LPSSVDLRG--YVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNQARNgDGTEGtdDGGSSLRDAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 194 EYIRdNHGVDTEESYPYKGRDMK------CHFNKKTVGADDKGYVDTPEG--DEEQLKIAVATQGPISIAIdAGHRSFQL 265
Cdd:COG4870 82 KLLR-WSGVVPESDWPYDDSDFTsqpsaaAYADARNYKIQDYYRLPGGGGatDLDAIKQALAEGGPVVFGF-YVYESFYN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 74959463 266 YKKGVYYDEECSSEELDHGVLLVGYgTDPEHGDYWIVKNSWGAGWGEKGYIRI 318
Cdd:COG4870 160 YTGGVYYPTPGDASLGGHAVAIVGY-DDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| Peptidase_C1A_CathepsinC |
cd02621 |
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ... |
121-332 |
1.15e-41 |
|
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: 145.22 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 121 PDEVDWRDTHL----VTDVKNQGMCGSCWAFSATGALEgqhAR---------KLGQLVSLSEQNLVDCStKYgNHGCNGG 187
Cdd:cd02621 2 PKSFDWGDVNNgfnyVSPVRNQGGCGSCYAFASVYALE---ARimiasnktdPLGQQPILSPQHVLSCS-QY-SQGCDGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 188 LMDQAFEYIRDNhGVDTEESYPYKGRDM-KCHFNKKTVG---ADDKGYVDTPEG--DEEQLKIAVATQGPISIAIDAgHR 261
Cdd:cd02621 77 FPFLVGKFAEDF-GIVTEDYFPYTADDDrPCKASPSECRryyFSDYNYVGGCYGctNEDEMKWEIYRNGPIVVAFEV-YS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 262 SFQLYKKGVY----YDEECSS--------EELDHGVLLVGYGTDPEHG-DYWIVKNSWGAGWGEKGYIRIARNRnNHCGV 328
Cdd:cd02621 155 DFDFYKEGVYhhtdNDEVSDGdndnfnpfELTNHAVLLVGWGEDEIKGeKYWIVKNSWGSSWGEKGYFKIRRGT-NECGI 233
|
....
gi 74959463 329 ATKA 332
Cdd:cd02621 234 ESQA 237
|
|
| Peptidase_C1A_CathepsinB |
cd02620 |
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ... |
135-327 |
6.96e-41 |
|
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: 142.79 E-value: 6.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 135 VKNQGMCGSCWAFSATGALEGQHARKLG--QLVSLSEQNLVDCSTKYGnHGCNGGLMDQAFEYIRdNHGVDTEESYPYKG 212
Cdd:cd02620 19 IRDQGNCGSCWAFSAVEAFSDRLCIQSNgkENVLLSAQDLLSCCSGCG-DGCNGGYPDAAWKYLT-TTGVVTGGCQPYTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 213 RDMKCHFNKKTVGAD--------DKGYVDTPE-------------GDEEQLKIAVATQGPISIAIDAgHRSFQLYKKGVY 271
Cdd:cd02620 97 PPCGHHPEGPPPCCGtpyctpkcQDGCEKTYEedkhkgksaysvpSDETDIMKEIMTNGPVQAAFTV-YEDFLYYKSGVY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 74959463 272 YDEEcSSEELDHGVLLVGYGTdpEHG-DYWIVKNSWGAGWGEKGYIRIARNRnNHCG 327
Cdd:cd02620 176 QHTS-GKQLGGHAVKIIGWGV--ENGvPYWLAANSWGTDWGENGYFRILRGS-NECG 228
|
|
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
120-320 |
1.45e-40 |
|
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: 142.17 E-value: 1.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 120 VPDEVDWRD---THLVTDVKNQGM---CGSCWAFSATGALEGQH--ARKL-GQLVSLSEQNLVDCStkyGNHGCNGGLMD 190
Cdd:cd02698 1 LPKSWDWRNvngVNYVSPTRNQHIpqyCGSCWAHGSTSALADRIniARKGaWPSVYLSVQVVIDCA---GGGSCHGGDPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 191 QAFEYIRdNHGVDTEESYPYKGRDMKC-------------------HFNKKTVGadDKGYVDtpegDEEQLKIAVATQGP 251
Cdd:cd02698 78 GVYEYAH-KHGIPDETCNPYQAKDGECnpfnrcgtcnpfgecfaikNYTLYFVS--DYGSVS----GRDKMMAEIYARGP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74959463 252 ISIAIDAgHRSFQLYKKGVYyDEECSSEELDHGVLLVGYGTDPEHGDYWIVKNSWGAGWGEKGYIRIAR 320
Cdd:cd02698 151 ISCGIMA-TEALENYTGGVY-KEYVQDPLINHIISVAGWGVDENGVEYWIVRNSWGEPWGERGWFRIVT 217
|
|
| Peptidase_C1 |
cd02619 |
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
123-318 |
1.08e-39 |
|
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: 139.57 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 123 EVDWRDTHLvTDVKNQGMCGSCWAFSATGALEGQHARKLG--QLVSLSEQNLVDCSTKY---GNHGCNGGLMDQAFEYIR 197
Cdd:cd02619 1 SVDLRPLRL-TPVKNQGSRGSCWAFASAYALESAYRIKGGedEYVDLSPQYLYICANDEclgINGSCDGGGPLSALLKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 198 DNHGVDTEESYPYKGRDMKCHF------NKKTVGADDKGYVDTpeGDEEQLKIAVATQGPISIAIDAGHRSFQL----YK 267
Cdd:cd02619 80 ALKGIPPEEDYPYGAESDGEEPkseaalNAAKVKLKDYRRVLK--NNIEDIKEALAKGGPVVAGFDVYSGFDRLkegiIY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 74959463 268 KGVYYDEECSSEELDHGVLLVGYGTDP-EHGDYWIVKNSWGAGWGEKGYIRI 318
Cdd:cd02619 158 EEIVYLLYEDGDLGGHAVVIVGYDDNYvEGKGAFIVKNSWGTDWGDNGYGRI 209
|
|
| PTZ00049 |
PTZ00049 |
cathepsin C-like protein; Provisional |
115-323 |
8.60e-23 |
|
cathepsin C-like protein; Provisional
Pssm-ID: 240244 [Multi-domain] Cd Length: 693 Bit Score: 99.26 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 115 PFNVQVPDEvdwrdthlvtDVKNQGMCGSCWAFSATGAL----EGQHARKLGQLV------SLSEQNLVDCStkYGNHGC 184
Cdd:PTZ00049 390 PFNNNTREY----------DVTNQLLCGSCYIASQMYAFkrriEIALTKNLDKKYlnnfddLLSIQTVLSCS--FYDQGC 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 185 NGGlmdqaFEYIRDNH----GVDTEESYPYKGRDMKCHFNKKTVG----------------------------------- 225
Cdd:PTZ00049 458 NGG-----FPYLVSKMaklqGIPLDKVFPYTATEQTCPYQVDQSAnsmngsanlrqinavffssetqsdmhadfeapiss 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 226 ------ADDKGYVDTPEG-----DEEQLKIAVATQGPISIAIDAGhRSFQLYKKGVYYDEE------CSS---------- 278
Cdd:PTZ00049 533 eparwyAKDYNYIGGCYGcnqcnGEKIMMNEIYRNGPIVASFEAS-PDFYDYADGVYYVEDfpharrCTVdlpkhngvyn 611
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 74959463 279 ----EELDHGVLLVGYGTDPEHG---DYWIVKNSWGAGWGEKGYIRIARNRN 323
Cdd:PTZ00049 612 itgwEKVNHAIVLVGWGEEEINGklyKYWIGRNSWGKNWGKEGYFKIIRGKN 663
|
|
| PTZ00364 |
PTZ00364 |
dipeptidyl-peptidase I precursor; Provisional |
91-323 |
3.36e-19 |
|
dipeptidyl-peptidase I precursor; Provisional
Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 88.41 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 91 YRKLNGYRRLFGDSRiKNSSSFLAPFNVQVPDEVDWRDTH---LVTDVKNQG---MCGSCWAFSATGALegqHAR----- 159
Cdd:PTZ00364 177 YSKSRSARKAKTASF-GFRQSFSHQLGDPPPAAWSWGDVGgasFLPAAPPASpgrGCNSSYVEAALAAM---MARvmvas 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 160 ----KLGQLVSLSEQNLVDCStKYGnHGCNGGLMDQAFEYIRDNhGVDTEESY--PYKGRDMKCHFNKKTVGAD-----D 228
Cdd:PTZ00364 253 nrtdPLGQQTFLSARHVLDCS-QYG-QGCAGGFPEEVGKFAETF-GILTTDSYyiPYDSGDGVERACKTRRPSRryyftN 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 229 KGYVDTPEG---DEEQLKIAVATQGPISIAIDAG-------HRSFQLYKKGVYYDEECSS----------EELDHGVLLV 288
Cdd:PTZ00364 330 YGPLGGYYGavtDPDEIIWEIYRHGPVPASVYANsdwyncdENSTEDVRYVSLDDYSTASadrplrhyfaSNVNHTVLII 409
|
250 260 270
....*....|....*....|....*....|....*..
gi 74959463 289 GYGTDPEHGDYWIVKNSWGAG--WGEKGYIRIARNRN 323
Cdd:PTZ00364 410 GWGTDENGGDYWLVLDPWGSRrsWCDGGTRKIARGVN 446
|
|
| PTZ00462 |
PTZ00462 |
Serine-repeat antigen protein; Provisional |
135-326 |
1.93e-12 |
|
Serine-repeat antigen protein; Provisional
Pssm-ID: 185641 [Multi-domain] Cd Length: 1004 Bit Score: 68.16 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 135 VKNQGMCGSCWAFSATGALEGQHARKLGQLVSLSEQNLVDCSTKYGNHGCNGGLMDQAF-EYIRDNHGVDTEESYPYK-- 211
Cdd:PTZ00462 547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCSKGEHKDRCDEGSNPLEFlQIIEDNGFLPADSNYLYNyt 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74959463 212 --GRD----------------MKCHFNKKTVGADDKGYV--------DTPEGDEEQLKIAVATQGPISIAIDAGH-RSFQ 264
Cdd:PTZ00462 627 kvGEDcpdeedhwmnlldhgkILNHNKKEPNSLDGKAYRayesehfhDKMDAFIKIIKDEIMNKGSVIAYIKAENvLGYE 706
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74959463 265 LYKKGVyyDEECSSEELDHGVLLVGYG----TDPEHGDYWIVKNSWGAGWGEKGYIRIARNRNNHC 326
Cdd:PTZ00462 707 FNGKKV--QNLCGDDTADHAVNIVGYGnyinDEDEKKSYWIVRNSWGKYWGDEGYFKVDMYGPSHC 770
|
|
| Inhibitor_I29 |
pfam08246 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
32-91 |
6.23e-10 |
|
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: 54.19 E-value: 6.23e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74959463 32 WDDYKEDFDKEY-SESEEQTYMEAFVKNMIHIENHNRDhrlGRKTFEMGLNHIADLPFSQY 91
Cdd:pfam08246 1 FDDWMKKYGKSYrSEEEELYRFQIFKENLKRIEEHNSN---GNVTYKLGLNKFADLTDEEF 58
|
|
| Inhibitor_I29 |
smart00848 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
32-86 |
6.09e-09 |
|
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: 51.48 E-value: 6.09e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 74959463 32 WDDYKEDFDKEY-SESEEQTYMEAFVKNMIHIENHNRDHrlgRKTFEMGLNHIADL 86
Cdd:smart00848 1 FEQWKKKHGKSYsSEEEEARRFAIFKENLKKIEEHNKKY---EHSYKLGVNQFSDL 53
|
|
| PepC |
COG3579 |
Aminopeptidase C [Amino acid transport and metabolism]; |
281-315 |
1.88e-04 |
|
Aminopeptidase C [Amino acid transport and metabolism];
Pssm-ID: 442798 [Multi-domain] Cd Length: 440 Bit Score: 42.94 E-value: 1.88e-04
10 20 30
....*....|....*....|....*....|....*.
gi 74959463 281 LDHGVLLVGYGTDPE-HGDYWIVKNSWGAGWGEKGY 315
Cdd:COG3579 361 DTHAMVITGVDLDQNgKPTRWKVENSWGDDNGYKGY 396
|
|
| |
