|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
117-332 |
1.02e-110 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 320.64 E-value: 1.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 117 PPSVDWRKKGNfVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCaqDFNNHGCQGGLPSQAFEYILYN 196
Cdd:pfam00112 2 PESFDWREKGA-VTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDC--DTFNNGCNGGLPDNAFEYIKKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 197 KGIMGEDTYPYQGKDGYCKF-QPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQ-DFMMYRTGIYSSTSCHK 274
Cdd:pfam00112 79 GGIVTESDYPYTAKDGTCKFkKSNSKVAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23110955 275 tpdKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKN-MCGLAACASYPI 332
Cdd:pfam00112 159 ---ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
117-331 |
1.05e-109 |
|
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: 318.03 E-value: 1.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 117 PPSVDWRKKGnFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNhGCQGGLPSQAFEYIlYN 196
Cdd:cd02248 1 PESVDWREKG-AVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNN-GCNGGNPDNAFEYV-KN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 197 KGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSChkTP 276
Cdd:cd02248 78 GGLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASSSFQFYKGGIYSGPCC--SN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23110955 277 DKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYP 331
Cdd:cd02248 156 TNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
116-331 |
3.27e-80 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 241.72 E-value: 3.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 116 YPPSVDWRKKGNfVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNhGCQGGLPSQAFEYILY 195
Cdd:smart00645 1 LPESFDWRKKGA-VTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNC-GCNGGLPDNAFEYIKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 196 NKGIMGEDTYPYQGkdgyckfqpgkaigfvkdvanitiydeeamveavalynpvsFAFEVTQDFMMYRTGIYSSTSChkT 275
Cdd:smart00645 79 NGGLETESCYPYTG-----------------------------------------SVAIDASDFQFYKSGIYDHPGC--G 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 276 PDKVNHAVLAVGYGEK--NGIPYWIVKNSWGPQWGMNGYFLIERGK-NMCGL-AACASYP 331
Cdd:smart00645 116 SGTLDHAVLIVGYGTEveNGKDYWIVKNSWGTDWGENGYFRIARGKnNECGIeASVASYP 175
|
|
| PTZ00021 |
PTZ00021 |
falcipain-2; Provisional |
28-335 |
6.41e-67 |
|
falcipain-2; Provisional
Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 218.10 E-value: 6.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 28 NSLEKFH-FKSWMSKHRKTYST-EEYHHRLQTFASNWRKINAHNNG-NHTFKMALNQFSDMSFAEIKHKYL---WSEPQN 101
Cdd:PTZ00021 161 TNLENVNsFYLFIKEHGKKYQTpDEMQQRYLSFVENLAKINAHNNKeNVLYKKGMNRFGDLSFEEFKKKYLtlkSFDFKS 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 102 CSAT---KSNYLRGTGPYPP--------SVDWRKKgNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLV 170
Cdd:PTZ00021 241 NGKKsprVINYDDVIKKYKPkdatfdhaKYDWRLH-NGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 171 DCAqdFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQG-KDGYCKFQPGKAIGFVKDVANITiydEEAMVEAVALYNPV 249
Cdd:PTZ00021 320 DCS--FKNNGCYGGLIPNAFEDMIELGGLCSEDDYPYVSdTPELCNIDRCKEKYKIKSYVSIP---EDKFKEAIRFLGPI 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 250 SFAFEVTQDFMMYRTGIYSStSCHKTPdkvNHAVLAVGYGEKNGIP----------YWIVKNSWGPQWGMNGYFLIERGK 319
Cdd:PTZ00021 395 SVSIAVSDDFAFYKGGIFDG-ECGEEP---NHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGFIRIETDE 470
|
330 340
....*....|....*....|
gi 23110955 320 N----MCGLAACASypIPLV 335
Cdd:PTZ00021 471 NglmkTCSLGTEAY--VPLI 488
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
116-315 |
3.26e-42 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 151.44 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 116 YPPSVDWRkkgNFVSPVKNQGACGSCWTFSTTGALESAIAIATGK---MLSLAEQQLVDCA-QDFNNHG--CQGGLPSQA 189
Cdd:COG4870 4 LPSSVDLR---GYVTPVKDQGSLGSCWAFATAAALESYLKKQAGApgtSLDLSELFLYNQArNGDGTEGtdDGGSSLRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 190 FeYILYNKGIMGEDTYPYQGKDGYCK---FQPGKAIGF-VKDVANIT----IYDEEAMVEAVALYNPVSFAFEVTQDFMM 261
Cdd:COG4870 81 L-KLLRWSGVVPESDWPYDDSDFTSQpsaAAYADARNYkIQDYYRLPggggATDLDAIKQALAEGGPVVFGFYVYESFYN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23110955 262 YRTGIYSSTSchKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLI 315
Cdd:COG4870 160 YTGGVYYPTP--GDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| Inhibitor_I29 |
pfam08246 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
35-90 |
4.82e-22 |
|
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: 87.70 E-value: 4.82e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 23110955 35 FKSWMSKHRKTY-STEEYHHRLQTFASNWRKINAHN-NGNHTFKMALNQFSDMSFAEI 90
Cdd:pfam08246 1 FDDWMKKYGKSYrSEEEELYRFQIFKENLKRIEEHNsNGNVTYKLGLNKFADLTDEEF 58
|
|
| Inhibitor_I29 |
smart00848 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
35-89 |
7.49e-19 |
|
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.
Pssm-ID: 214853 [Multi-domain] Cd Length: 57 Bit Score: 78.82 E-value: 7.49e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 23110955 35 FKSWMSKHRKTYST-EEYHHRLQTFASNWRKINAHN-NGNHTFKMALNQFSDMSFAE 89
Cdd:smart00848 1 FEQWKKKHGKSYSSeEEEARRFAIFKENLKKIEEHNkKYEHSYKLGVNQFSDLTPEE 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
117-332 |
1.02e-110 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 320.64 E-value: 1.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 117 PPSVDWRKKGNfVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCaqDFNNHGCQGGLPSQAFEYILYN 196
Cdd:pfam00112 2 PESFDWREKGA-VTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDC--DTFNNGCNGGLPDNAFEYIKKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 197 KGIMGEDTYPYQGKDGYCKF-QPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQ-DFMMYRTGIYSSTSCHK 274
Cdd:pfam00112 79 GGIVTESDYPYTAKDGTCKFkKSNSKVAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 23110955 275 tpdKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKN-MCGLAACASYPI 332
Cdd:pfam00112 159 ---ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
117-331 |
1.05e-109 |
|
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: 318.03 E-value: 1.05e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 117 PPSVDWRKKGnFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNhGCQGGLPSQAFEYIlYN 196
Cdd:cd02248 1 PESVDWREKG-AVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNN-GCNGGNPDNAFEYV-KN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 197 KGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSSTSChkTP 276
Cdd:cd02248 78 GGLASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASSSFQFYKGGIYSGPCC--SN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 23110955 277 DKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLAACASYP 331
Cdd:cd02248 156 TNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
116-331 |
3.27e-80 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 241.72 E-value: 3.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 116 YPPSVDWRKKGNfVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCAQDFNNhGCQGGLPSQAFEYILY 195
Cdd:smart00645 1 LPESFDWRKKGA-VTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNC-GCNGGLPDNAFEYIKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 196 NKGIMGEDTYPYQGkdgyckfqpgkaigfvkdvanitiydeeamveavalynpvsFAFEVTQDFMMYRTGIYSSTSChkT 275
Cdd:smart00645 79 NGGLETESCYPYTG-----------------------------------------SVAIDASDFQFYKSGIYDHPGC--G 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 276 PDKVNHAVLAVGYGEK--NGIPYWIVKNSWGPQWGMNGYFLIERGK-NMCGL-AACASYP 331
Cdd:smart00645 116 SGTLDHAVLIVGYGTEveNGKDYWIVKNSWGTDWGENGYFRIARGKnNECGIeASVASYP 175
|
|
| PTZ00021 |
PTZ00021 |
falcipain-2; Provisional |
28-335 |
6.41e-67 |
|
falcipain-2; Provisional
Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 218.10 E-value: 6.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 28 NSLEKFH-FKSWMSKHRKTYST-EEYHHRLQTFASNWRKINAHNNG-NHTFKMALNQFSDMSFAEIKHKYL---WSEPQN 101
Cdd:PTZ00021 161 TNLENVNsFYLFIKEHGKKYQTpDEMQQRYLSFVENLAKINAHNNKeNVLYKKGMNRFGDLSFEEFKKKYLtlkSFDFKS 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 102 CSAT---KSNYLRGTGPYPP--------SVDWRKKgNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLV 170
Cdd:PTZ00021 241 NGKKsprVINYDDVIKKYKPkdatfdhaKYDWRLH-NGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELV 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 171 DCAqdFNNHGCQGGLPSQAFEYILYNKGIMGEDTYPYQG-KDGYCKFQPGKAIGFVKDVANITiydEEAMVEAVALYNPV 249
Cdd:PTZ00021 320 DCS--FKNNGCYGGLIPNAFEDMIELGGLCSEDDYPYVSdTPELCNIDRCKEKYKIKSYVSIP---EDKFKEAIRFLGPI 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 250 SFAFEVTQDFMMYRTGIYSStSCHKTPdkvNHAVLAVGYGEKNGIP----------YWIVKNSWGPQWGMNGYFLIERGK 319
Cdd:PTZ00021 395 SVSIAVSDDFAFYKGGIFDG-ECGEEP---NHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGFIRIETDE 470
|
330 340
....*....|....*....|
gi 23110955 320 N----MCGLAACASypIPLV 335
Cdd:PTZ00021 471 NglmkTCSLGTEAY--VPLI 488
|
|
| PTZ00200 |
PTZ00200 |
cysteine proteinase; Provisional |
35-324 |
4.29e-63 |
|
cysteine proteinase; Provisional
Pssm-ID: 240310 [Multi-domain] Cd Length: 448 Bit Score: 206.85 E-value: 4.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 35 FKSWMSKHRKTYSTE-EYHHRLQTFASNWRKINAHNnGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATKS------ 107
Cdd:PTZ00200 126 FEEFNKKYNRKHATHaERLNRFLTFRNNYLEVKSHK-GDEPYSKEINKFSDLTEEEFRKLFPVIKVPPKSNSTShnndfk 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 108 -------------NYLRGTG--PYPPS------VDWRKkGNFVSPVKNQGA-CGSCWTFSTTGALESAIAIATGKMLSLA 165
Cdd:PTZ00200 205 arhvsnptylknlKKAKNTDedVKDPSkitgegLDWRR-ADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRDKSVDLS 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 166 EQQLVDCaqDFNNHGCQGGLPSQAFEYIlYNKGIMGEDTYPYQGKDGYC-------KFQPGKAIGFVKDVANITIydeea 238
Cdd:PTZ00200 284 EQELVNC--DTKSQGCSGGYPDTALEYV-KNKGLSSSSDVPYLAKDGKCvvsstkkVYIDSYLVAKGKDVLNKSL----- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 239 mveavaLYNPVSFAFEVTQDFMMYRTGIYSStSCHKTPdkvNHAVLAVG--YGEKNGIPYWIVKNSWGPQWGMNGYFLIE 316
Cdd:PTZ00200 356 ------VISPTVVYIAVSRELLKYKSGVYNG-ECGKSL---NHAVLLVGegYDEKTKKRYWIIKNSWGTDWGENGYMRLE 425
|
330
....*....|.
gi 23110955 317 R---GKNMCGL 324
Cdd:PTZ00200 426 RtneGTDKCGI 436
|
|
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
35-332 |
2.04e-61 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 199.54 E-value: 2.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 35 FKSWMSKHRKTYST-EEYHHRLQTFASNWRKINAHNNGNHTFKMALNQFSDMSFAEIKHKYLWSEPQNCSATK--SNYLR 111
Cdd:PTZ00203 38 FEEFKRTYQRAYGTlTEEQQRLANFERNLELMREHQARNPHARFGITKFFDLSEAEFAARYLNGAAYFAAAKQhaGQHYR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 112 GTGP----YPPSVDWRKKGNfVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAEQQLVDCaqDFNNHGCQGGLPS 187
Cdd:PTZ00203 118 KARAdlsaVPDAVDWREKGA-VTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSC--DHVDNGCGGGLML 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 188 QAFEYILYNKG--IMGEDTYPYQGKDG-------YCKFQPGKAI-GFVKDVANitiydEEAMVEAVALYNPVSFAFEVTQ 257
Cdd:PTZ00203 195 QAFEWVLRNMNgtVFTEKSYPYVSGNGdvpecsnSSELAPGARIdGYVSMESS-----ERVMAAWLAKNGPISIAVDASS 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23110955 258 dFMMYRTGIYssTSChkTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGLaacASYPI 332
Cdd:PTZ00203 270 -FMSYHSGVL--TSC--IGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLL---TGYPV 336
|
|
| Peptidase_C1A_CathepsinC |
cd02621 |
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ... |
117-332 |
1.71e-50 |
|
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: 167.95 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 117 PPSVDWRKKG---NFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLSLAE------QQLVDCAQdfNNHGCQGGLPS 187
Cdd:cd02621 2 PKSFDWGDVNngfNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPLGQqpilspQHVLSCSQ--YSQGCDGGFPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 188 QAFEYIlYNKGIMGEDTYPYQG-KDGYCKFQP-GKAIGFVKDVANITIY----DEEAMVEAVALYNPVSFAFEVTQDFMM 261
Cdd:cd02621 80 LVGKFA-EDFGIVTEDYFPYTAdDDRPCKASPsECRRYYFSDYNYVGGCygctNEDEMKWEIYRNGPIVVAFEVYSDFDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 262 YRTGIYSSTSCHKTPD----------KVNHAVLAVGYGE--KNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGL--AAC 327
Cdd:cd02621 159 YKEGVYHHTDNDEVSDgdndnfnpfeLTNHAVLLVGWGEdeIKGEKYWIVKNSWGSSWGEKGYFKIRRGTNECGIesQAV 238
|
....*
gi 23110955 328 ASYPI 332
Cdd:cd02621 239 FAYPI 243
|
|
| Peptidase_C1A_CathepsinB |
cd02620 |
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ... |
117-324 |
7.97e-49 |
|
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: 163.60 E-value: 7.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 117 PPSVDWRKK-GN--FVSPVKNQGACGSCWTFSTTGALESAIAIATG--KMLSLAEQQLVDCAqDFNNHGCQGGLPSQAFE 191
Cdd:cd02620 1 PESFDAREKwPNciSIGEIRDQGNCGSCWAFSAVEAFSDRLCIQSNgkENVLLSAQDLLSCC-SGCGDGCNGGYPDAAWK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 192 YiLYNKGIMGEDTYPYQ--------------GKDGYC--KFQPGKAIGFVKDVA-NITIY----DEEAMVEAVALYNPVS 250
Cdd:cd02620 80 Y-LTTTGVVTGGCQPYTippcghhpegpppcCGTPYCtpKCQDGCEKTYEEDKHkGKSAYsvpsDETDIMKEIMTNGPVQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23110955 251 FAFEVTQDFMMYRTGIYSstscHKTPDKVN-HAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLIERGKNMCGL 324
Cdd:cd02620 159 AAFTVYEDFLYYKSGVYQ----HTSGKQLGgHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNECGI 229
|
|
| Peptidase_C1 |
cd02619 |
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
119-330 |
1.16e-47 |
|
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: 159.99 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 119 SVDWRKKGnfVSPVKNQGACGSCWTFSTTGALESAIAIATG--KMLSLAEQQLVDCAQDF---NNHGCQGGLPSQAFEYI 193
Cdd:cd02619 1 SVDLRPLR--LTPVKNQGSRGSCWAFASAYALESAYRIKGGedEYVDLSPQYLYICANDEclgINGSCDGGGPLSALLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 194 LYNKGIMGEDTYPYQGKDGYCKFQPGKA--IGFVKDVAN--ITIYDEEAMVEAVALYNPVSFAFEVTQDFMMYRTGIYSS 269
Cdd:cd02619 79 VALKGIPPEEDYPYGAESDGEEPKSEAAlnAAKVKLKDYrrVLKNNIEDIKEALAKGGPVVAGFDVYSGFDRLKEGIIYE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23110955 270 TSCHKTPDKV---NHAVLAVGYG--EKNGIPYWIVKNSWGPQWGMNGYFLIERgKNMCGLAACASY 330
Cdd:cd02619 159 EIVYLLYEDGdlgGHAVVIVGYDdnYVEGKGAFIVKNSWGTDWGDNGYGRISY-EDVYEMTFGANV 223
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
116-315 |
3.26e-42 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 151.44 E-value: 3.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 116 YPPSVDWRkkgNFVSPVKNQGACGSCWTFSTTGALESAIAIATGK---MLSLAEQQLVDCA-QDFNNHG--CQGGLPSQA 189
Cdd:COG4870 4 LPSSVDLR---GYVTPVKDQGSLGSCWAFATAAALESYLKKQAGApgtSLDLSELFLYNQArNGDGTEGtdDGGSSLRDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 190 FeYILYNKGIMGEDTYPYQGKDGYCK---FQPGKAIGF-VKDVANIT----IYDEEAMVEAVALYNPVSFAFEVTQDFMM 261
Cdd:COG4870 81 L-KLLRWSGVVPESDWPYDDSDFTSQpsaAAYADARNYkIQDYYRLPggggATDLDAIKQALAEGGPVVFGFYVYESFYN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 23110955 262 YRTGIYSSTSchKTPDKVNHAVLAVGYGEKNGIPYWIVKNSWGPQWGMNGYFLI 315
Cdd:COG4870 160 YTGGVYYPTP--GDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
|
|
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
117-319 |
3.24e-38 |
|
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: 136.00 E-value: 3.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 117 PPSVDWR--KKGNFVSPVKNQ---GACGSCWTFSTTGALESAIAIAT---GKMLSLAEQQLVDCAQDFNnhgCQGGLPSQ 188
Cdd:cd02698 2 PKSWDWRnvNGVNYVSPTRNQhipQYCGSCWAHGSTSALADRINIARkgaWPSVYLSVQVVIDCAGGGS---CHGGDPGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 189 AFEYILyNKGIMGEDTYPYQGKDGYCK---------------FQPGKAIGFVKDVAniTIYDEEAMVEAVALYNPVSFAF 253
Cdd:cd02698 79 VYEYAH-KHGIPDETCNPYQAKDGECNpfnrcgtcnpfgecfAIKNYTLYFVSDYG--SVSGRDKMMAEIYARGPISCGI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23110955 254 EVTQDFMMYRTGIYSSTSCHKTPdkvNHAVLAVGYG-EKNGIPYWIVKNSWGPQWGMNGYFLIERGK 319
Cdd:cd02698 156 MATEALENYTGGVYKEYVQDPLI---NHIISVAGWGvDENGVEYWIVRNSWGEPWGERGWFRIVTSS 219
|
|
| PTZ00049 |
PTZ00049 |
cathepsin C-like protein; Provisional |
100-333 |
1.32e-27 |
|
cathepsin C-like protein; Provisional
Pssm-ID: 240244 [Multi-domain] Cd Length: 693 Bit Score: 113.51 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 100 QNCSATKSNYLRGTG--PYPPSVDWR---KKGNFVSPVKNQGACGSCWTFSTTGALESAIAIATGKMLS----------L 164
Cdd:PTZ00049 363 ENYEDTEKAPHRELEidELPKNFTWGdpfNNNTREYDVTNQLLCGSCYIASQMYAFKRRIEIALTKNLDkkylnnfddlL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 165 AEQQLVDCAqdFNNHGCQGGLPsqafeYILYN----KGIMGEDTYPYQGKDGYCKFQPGKAIGFVKDVANIT-------- 232
Cdd:PTZ00049 443 SIQTVLSCS--FYDQGCNGGFP-----YLVSKmaklQGIPLDKVFPYTATEQTCPYQVDQSANSMNGSANLRqinavffs 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 233 --------------IYDEEA-------------------------MVEavaLYN--PVSFAFEVTQDFMMYRTGIYSSTS 271
Cdd:PTZ00049 516 setqsdmhadfeapISSEPArwyakdynyiggcygcnqcngekimMNE---IYRngPIVASFEASPDFYDYADGVYYVED 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 272 ------C-----HKTP-------DKVNHAVLAVGYGEK--NGIP--YWIVKNSWGPQWGMNGYFLIERGKNMCGLAACAS 329
Cdd:PTZ00049 593 fpharrCtvdlpKHNGvynitgwEKVNHAIVLVGWGEEeiNGKLykYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQSL 672
|
....
gi 23110955 330 YPIP 333
Cdd:PTZ00049 673 FIEP 676
|
|
| Inhibitor_I29 |
pfam08246 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
35-90 |
4.82e-22 |
|
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: 87.70 E-value: 4.82e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 23110955 35 FKSWMSKHRKTY-STEEYHHRLQTFASNWRKINAHN-NGNHTFKMALNQFSDMSFAEI 90
Cdd:pfam08246 1 FDDWMKKYGKSYrSEEEELYRFQIFKENLKRIEEHNsNGNVTYKLGLNKFADLTDEEF 58
|
|
| Inhibitor_I29 |
smart00848 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
35-89 |
7.49e-19 |
|
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.
Pssm-ID: 214853 [Multi-domain] Cd Length: 57 Bit Score: 78.82 E-value: 7.49e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 23110955 35 FKSWMSKHRKTYST-EEYHHRLQTFASNWRKINAHN-NGNHTFKMALNQFSDMSFAE 89
Cdd:smart00848 1 FEQWKKKHGKSYSSeEEEARRFAIFKENLKKIEEHNkKYEHSYKLGVNQFSDLTPEE 57
|
|
| PTZ00364 |
PTZ00364 |
dipeptidyl-peptidase I precursor; Provisional |
115-334 |
8.03e-15 |
|
dipeptidyl-peptidase I precursor; Provisional
Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 74.93 E-value: 8.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 115 PYPPSVDWRKKG--NFVSPVKNQGA---CGSCWTFSTTGALESAIAIAT------GKMLSLAEQQLVDCAQdfNNHGCQG 183
Cdd:PTZ00364 204 PPPAAWSWGDVGgaSFLPAAPPASPgrgCNSSYVEAALAAMMARVMVASnrtdplGQQTFLSARHVLDCSQ--YGQGCAG 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 184 GLPsqaFEYILYNK--GIMGEDTY--PYQGKDGY---CKFQP-------------GKAIGFVKDVANIT--IYDEEAMVE 241
Cdd:PTZ00364 282 GFP---EEVGKFAEtfGILTTDSYyiPYDSGDGVeraCKTRRpsrryyftnygplGGYYGAVTDPDEIIweIYRHGPVPA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 242 AVALYNPVSFAFE-VTQDFMMYRTGIYSSTSC-----HKTPDKVNHAVLAVGYGE-KNGIPYWIVKNSWGPQ--WGMNGY 312
Cdd:PTZ00364 359 SVYANSDWYNCDEnSTEDVRYVSLDDYSTASAdrplrHYFASNVNHTVLIIGWGTdENGGDYWLVLDPWGSRrsWCDGGT 438
|
250 260
....*....|....*....|..
gi 23110955 313 FLIERGKNMCGLaacASYPIPL 334
Cdd:PTZ00364 439 RKIARGVNAYNI---ESEVVVM 457
|
|
| PTZ00462 |
PTZ00462 |
Serine-repeat antigen protein; Provisional |
87-327 |
1.05e-09 |
|
Serine-repeat antigen protein; Provisional
Pssm-ID: 185641 [Multi-domain] Cd Length: 1004 Bit Score: 59.69 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 87 FAEIKHKYLWSEPQNCSATKSNYLRgtgpyppsvdwrKKGNFVS--PVKNQGACGSCWTFSTTGALESAIAIATGKMLSL 164
Cdd:PTZ00462 512 EKEDTLKYDNNDKMFCNKEFCNRLK------------DENNCISkiQIEDQGNCAISWIFASKYHLETIKCMKGYEPHAI 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 165 AEQQLVDCAQDFNNHGCQGGLPSQAFEYILYNKGIMGEDT-YPYQ----GKDgyCK---------FQPGKAIGFVK---- 226
Cdd:PTZ00462 580 SALYIANCSKGEHKDRCDEGSNPLEFLQIIEDNGFLPADSnYLYNytkvGED--CPdeedhwmnlLDHGKILNHNKkepn 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23110955 227 --DVANITIYDEE----------AMVEAVALYNPVSFAFEVTQDFMMYR-TGIYSSTSC-HKTPDkvnHAVLAVGYG--- 289
Cdd:PTZ00462 658 slDGKAYRAYESEhfhdkmdafiKIIKDEIMNKGSVIAYIKAENVLGYEfNGKKVQNLCgDDTAD---HAVNIVGYGnyi 734
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 23110955 290 --EKNGIPYWIVKNSWGPQWGMNGYFLIErgknMCGLAAC 327
Cdd:PTZ00462 735 ndEDEKKSYWIVRNSWGKYWGDEGYFKVD----MYGPSHC 770
|
|
| PepC |
COG3579 |
Aminopeptidase C [Amino acid transport and metabolism]; |
280-313 |
2.92e-03 |
|
Aminopeptidase C [Amino acid transport and metabolism];
Pssm-ID: 442798 [Multi-domain] Cd Length: 440 Bit Score: 39.09 E-value: 2.92e-03
10 20 30
....*....|....*....|....*....|....*.
gi 23110955 280 NHAVLAVGYG-EKNGIP-YWIVKNSWGPQWGMNGYF 313
Cdd:COG3579 362 THAMVITGVDlDQNGKPtRWKVENSWGDDNGYKGYF 397
|
|
| |
