|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
1-346 |
0e+00 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 749.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
Cdd:PTZ00203 1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
Cdd:PTZ00203 81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
Cdd:PTZ00203 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
Cdd:PTZ00203 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
|
330 340
....*....|....*....|....*.
gi 157864857 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
Cdd:PTZ00203 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
126-339 |
6.96e-99 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 294.83 E-value: 6.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 126 VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRnmN 205
Cdd:pfam00112 1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKK--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 206 GTVFTEKSYPYVSGNGdvpECSNSSELAPGARIDGYVS-MESSERVMAAWLAKNGPISIAVDAS--SFMSYHSGVL--TS 280
Cdd:pfam00112 79 GGIVTESDYPYTAKDG---TCKFKKSNSKVAKIKGYGDvPYNDEEALQAALAKNGPVSVAIDAYerDFQLYKSGVYkhTE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 281 CiGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVN-ACLLTGYPVSVH 339
Cdd:pfam00112 156 C-GGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
127-338 |
1.28e-94 |
|
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: 283.75 E-value: 1.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 127 PDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHV-DNGCGGGLMLQAFEWVlrnMN 205
Cdd:cd02248 1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFEYV---KN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 206 GTVFTEKSYPYVSGNGDvpeCSNSSElAPGARIDGYVSME-SSERVMAAWLAKNGPISIAVDAS-SFMSYHSGVLT--SC 281
Cdd:cd02248 78 GGLASESDYPYTGKDGT---CKYNSS-KVGAKITGYSNVPpGDEEALKAALANYGPVSVAIDASsSFQFYKGGIYSgpCC 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157864857 282 IGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSV 338
Cdd:cd02248 154 SNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
126-338 |
1.08e-75 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 234.01 E-value: 1.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 126 VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDH-VDNGCGGGLMLQAFEWVLRnm 204
Cdd:smart00645 1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGgGNCGCNGGLPDNAFEYIKK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 205 NGTVFTEKSYPYVsgngdvpecsnsselapgaridgyvsmesservmaawlakngpISIAVDASSFMSYHSGVL--TSCI 282
Cdd:smart00645 79 NGGLETESCYPYT-------------------------------------------GSVAIDASDFQFYKSGIYdhPGCG 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157864857 283 GEQLNHGVLLVGYNMTGE--VPYWVIKNSWGEDWGEKGYVRVTMGV-NACLLTGYPVSV 338
Cdd:smart00645 116 SGTLDHAVLIVGYGTEVEngKDYWIVKNSWGTDWGENGYFRIARGKnNECGIEASVASY 174
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
123-323 |
2.24e-40 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 149.51 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 123 LSAVPDAVDWREKgaVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKL---VRLSEQQLVSC----DHVDNGCGGGLMLQ 195
Cdd:COG4870 1 AAALPSSVDLRGY--VTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQarngDGTEGTDDGGSSLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 196 -AFEWvLRNmNGTVfTEKSYPYVSGNGDVPECSNSSELAPGARIDGY--VSMESSERVMAAW---LAKNGPISIAVDA-S 268
Cdd:COG4870 79 dALKL-LRW-SGVV-PESDWPYDDSDFTSQPSAAAYADARNYKIQDYyrLPGGGGATDLDAIkqaLAEGGPVVFGFYVyE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157864857 269 SFMSYHSGVLTSCIGEQL--NHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVT 323
Cdd:COG4870 156 SFYNYTGGVYYPTPGDASlgGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWIS 212
|
|
| DUF3586 |
pfam12131 |
Protein of unknown function (DUF3586); This domain is found in eukaryotes. This domain is ... |
355-417 |
5.27e-32 |
|
Protein of unknown function (DUF3586); This domain is found in eukaryotes. This domain is about 80 amino acids in length and is found associated with pfam08246, and pfam00112.
Pssm-ID: 403378 Cd Length: 75 Bit Score: 116.50 E-value: 5.27e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157864857 355 HAPKRVTVKQITCTDYFCRKGCKTTVIPTKECLPNGAGGSFQMECGDHQVLKLTYTSMNCTGE 417
Cdd:pfam12131 13 EAPKRVTVVQKTCTDYGCRKGCKSTTFPTGVCLKNTGGGSVMMTCGESEVLELIYRSSSCSGP 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00203 |
PTZ00203 |
cathepsin L protease; Provisional |
1-346 |
0e+00 |
|
cathepsin L protease; Provisional
Pssm-ID: 185513 [Multi-domain] Cd Length: 348 Bit Score: 749.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
Cdd:PTZ00203 1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
Cdd:PTZ00203 81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
Cdd:PTZ00203 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
Cdd:PTZ00203 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
|
330 340
....*....|....*....|....*.
gi 157864857 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
Cdd:PTZ00203 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
|
|
| Peptidase_C1 |
pfam00112 |
Papain family cysteine protease; |
126-339 |
6.96e-99 |
|
Papain family cysteine protease;
Pssm-ID: 425470 [Multi-domain] Cd Length: 214 Bit Score: 294.83 E-value: 6.96e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 126 VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRnmN 205
Cdd:pfam00112 1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKK--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 206 GTVFTEKSYPYVSGNGdvpECSNSSELAPGARIDGYVS-MESSERVMAAWLAKNGPISIAVDAS--SFMSYHSGVL--TS 280
Cdd:pfam00112 79 GGIVTESDYPYTAKDG---TCKFKKSNSKVAKIKGYGDvPYNDEEALQAALAKNGPVSVAIDAYerDFQLYKSGVYkhTE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 281 CiGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVN-ACLLTGYPVSVH 339
Cdd:pfam00112 156 C-GGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNnECGIASEASYPI 214
|
|
| Peptidase_C1A |
cd02248 |
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ... |
127-338 |
1.28e-94 |
|
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: 283.75 E-value: 1.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 127 PDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHV-DNGCGGGLMLQAFEWVlrnMN 205
Cdd:cd02248 1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFEYV---KN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 206 GTVFTEKSYPYVSGNGDvpeCSNSSElAPGARIDGYVSME-SSERVMAAWLAKNGPISIAVDAS-SFMSYHSGVLT--SC 281
Cdd:cd02248 78 GGLASESDYPYTGKDGT---CKYNSS-KVGAKITGYSNVPpGDEEALKAALANYGPVSVAIDASsSFQFYKGGIYSgpCC 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157864857 282 IGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSV 338
Cdd:cd02248 154 SNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
|
|
| Pept_C1 |
smart00645 |
Papain family cysteine protease; |
126-338 |
1.08e-75 |
|
Papain family cysteine protease;
Pssm-ID: 214761 [Multi-domain] Cd Length: 175 Bit Score: 234.01 E-value: 1.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 126 VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDH-VDNGCGGGLMLQAFEWVLRnm 204
Cdd:smart00645 1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGgGNCGCNGGLPDNAFEYIKK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 205 NGTVFTEKSYPYVsgngdvpecsnsselapgaridgyvsmesservmaawlakngpISIAVDASSFMSYHSGVL--TSCI 282
Cdd:smart00645 79 NGGLETESCYPYT-------------------------------------------GSVAIDASDFQFYKSGIYdhPGCG 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 157864857 283 GEQLNHGVLLVGYNMTGE--VPYWVIKNSWGEDWGEKGYVRVTMGV-NACLLTGYPVSV 338
Cdd:smart00645 116 SGTLDHAVLIVGYGTEVEngKDYWIVKNSWGTDWGENGYFRIARGKnNECGIEASVASY 174
|
|
| PTZ00021 |
PTZ00021 |
falcipain-2; Provisional |
37-322 |
3.45e-61 |
|
falcipain-2; Provisional
Pssm-ID: 240232 [Multi-domain] Cd Length: 489 Bit Score: 206.55 E-value: 3.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 37 LFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQAR-NPHARFGITKFFDLSEAEFAARYL---------NG----- 101
Cdd:PTZ00021 168 SFYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAHNNKeNVLYKKGMNRFGDLSFEEFKKKYLtlksfdfksNGkkspr 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 102 -AAYFAAAKQhagqhYRKARADLSAVpdAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVS 180
Cdd:PTZ00021 248 vINYDDVIKK-----YKPKDATFDHA--KYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 181 CDHVDNGCGGGLMLQAFEWVLrNMNGtVFTEKSYPYVsgnGDVPECSNSSELAPGARIDGYVSMeSSERVMAAwLAKNGP 260
Cdd:PTZ00021 321 CSFKNNGCYGGLIPNAFEDMI-ELGG-LCSEDDYPYV---SDTPELCNIDRCKEKYKIKSYVSI-PEDKFKEA-IRFLGP 393
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157864857 261 ISIAVDAS-SFMSYHSGVLTSCIGEQLNHGVLLVGYNM---------TGEVPYW-VIKNSWGEDWGEKGYVRV 322
Cdd:PTZ00021 394 ISVSIAVSdDFAFYKGGIFDGECGEEPNHAVILVGYGMeeiynsdtkKMEKRYYyIIKNSWGESWGEKGFIRI 466
|
|
| PTZ00200 |
PTZ00200 |
cysteine proteinase; Provisional |
38-340 |
5.17e-59 |
|
cysteine proteinase; Provisional
Pssm-ID: 240310 [Multi-domain] Cd Length: 448 Bit Score: 199.54 E-value: 5.17e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 38 FEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHARfGITKFFDLSEAEFAARY-----LNGAAYFAAAKQHA 112
Cdd:PTZ00200 126 FEEFNKKYNRKHATHAERLNRFLTFRNNYLEVKSHKGDEPYSK-EINKFSDLTEEEFRKLFpvikvPPKSNSTSHNNDFK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 113 GQHY---------RKAR------ADLSAV-PDAVDWREKGAVTPVKNQGA-CGSCWAFSAVGNIESQWAVAGHKLVRLSE 175
Cdd:PTZ00200 205 ARHVsnptylknlKKAKntdedvKDPSKItGEGLDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRDKSVDLSE 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 176 QQLVSCDHVDNGCGGGLMLQAFEWVlrnMNGTVFTEKSYPYVSGNGdvpECSNSSelAPGARIDGYVSMESSErVMAAWL 255
Cdd:PTZ00200 285 QELVNCDTKSQGCSGGYPDTALEYV---KNKGLSSSSDVPYLAKDG---KCVVSS--TKKVYIDSYLVAKGKD-VLNKSL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 256 AKnGPISIAVDAS-SFMSYHSGVLTSCIGEQLNHGVLLV--GYNMTGEVPYWVIKNSWGEDWGEKGY---VRVTMGVNAC 329
Cdd:PTZ00200 356 VI-SPTVVYIAVSrELLKYKSGVYNGECGKSLNHAVLLVgeGYDEKTKKRYWIIKNSWGTDWGENGYmrlERTNEGTDKC 434
|
330
....*....|....
gi 157864857 330 --LLTGY-PVSVHV 340
Cdd:PTZ00200 435 giLTVGLtPVFYSS 448
|
|
| COG4870 |
COG4870 |
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones]; |
123-323 |
2.24e-40 |
|
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443898 [Multi-domain] Cd Length: 426 Bit Score: 149.51 E-value: 2.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 123 LSAVPDAVDWREKgaVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKL---VRLSEQQLVSC----DHVDNGCGGGLMLQ 195
Cdd:COG4870 1 AAALPSSVDLRGY--VTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQarngDGTEGTDDGGSSLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 196 -AFEWvLRNmNGTVfTEKSYPYVSGNGDVPECSNSSELAPGARIDGY--VSMESSERVMAAW---LAKNGPISIAVDA-S 268
Cdd:COG4870 79 dALKL-LRW-SGVV-PESDWPYDDSDFTSQPSAAAYADARNYKIQDYyrLPGGGGATDLDAIkqaLAEGGPVVFGFYVyE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157864857 269 SFMSYHSGVLTSCIGEQL--NHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVT 323
Cdd:COG4870 156 SFYNYTGGVYYPTPGDASlgGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWIS 212
|
|
| Peptidase_C1A_CathepsinB |
cd02620 |
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ... |
127-338 |
2.84e-40 |
|
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: 143.95 E-value: 2.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 127 PDAVDWREK----GAVTPVKNQGACGSCWAFSAVGNIESQWAVA--GHKLVRLSEQQLVSCDHV-DNGCGGGLMLQAFEW 199
Cdd:cd02620 1 PESFDAREKwpncISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQsnGKENVLLSAQDLLSCCSGcGDGCNGGYPDAAWKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 200 vLRNmNGTVfTEKSYPYVSGNGDV---------------PECSNSSELAPGARI---DGYVSMESSERVMAAWLAKNGPI 261
Cdd:cd02620 81 -LTT-TGVV-TGGCQPYTIPPCGHhpegpppccgtpyctPKCQDGCEKTYEEDKhkgKSAYSVPSDETDIMKEIMTNGPV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157864857 262 SIAVD-ASSFMSYHSGVLTSCIGEQLN-HGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSV 338
Cdd:cd02620 158 QAAFTvYEDFLYYKSGVYQHTSGKQLGgHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNECGIESEVVAG 236
|
|
| Peptidase_C1 |
cd02619 |
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ... |
130-326 |
2.23e-36 |
|
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: 133.41 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 130 VDWREKGaVTPVKNQGACGSCWAFSAVGNIESQWAVAG--HKLVRLSEQQLVSCDHV-----DNGCGGGLMLQAFEWVLR 202
Cdd:cd02619 2 VDLRPLR-LTPVKNQGSRGSCWAFASAYALESAYRIKGgeDEYVDLSPQYLYICANDeclgiNGSCDGGGPLSALLKLVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 203 NmNGtVFTEKSYPYVSGNGDVPECSNSSELAPGARIDGYVSMESS-ERVMAAWLAKNGPISIAVDASS-FMSYHSGVLTS 280
Cdd:cd02619 81 L-KG-IPPEEDYPYGAESDGEEPKSEAALNAAKVKLKDYRRVLKNnIEDIKEALAKGGPVVAGFDVYSgFDRLKEGIIYE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 157864857 281 CIGEQL-------NHGVLLVGYNM--TGEVPYWVIKNSWGEDWGEKGYVRVTMGV 326
Cdd:cd02619 159 EIVYLLyedgdlgGHAVVIVGYDDnyVEGKGAFIVKNSWGTDWGDNGYGRISYED 213
|
|
| Peptidase_C1A_CathepsinC |
cd02621 |
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ... |
127-336 |
4.31e-36 |
|
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: 132.89 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 127 PDAVDWREKGA----VTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLV------RLSEQQLVSCDHVDNGCGGGLmlqa 196
Cdd:cd02621 2 PKSFDWGDVNNgfnyVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDplgqqpILSPQHVLSCSQYSQGCDGGF---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 197 FEWVLRNM--NGtVFTEKSYPYVSGngDVPECSNSSE------LAPGARIDGYVSMESSERVMaaW-LAKNGPISIAVDA 267
Cdd:cd02621 78 PFLVGKFAedFG-IVTEDYFPYTAD--DDRPCKASPSecrryyFSDYNYVGGCYGCTNEDEMK--WeIYRNGPIVVAFEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 268 -SSFMSYHSGV------LTSCIG--------EQLNHGVLLVGY---NMTGEvPYWVIKNSWGEDWGEKGYVRVTMGVNAC 329
Cdd:cd02621 153 ySDFDFYKEGVyhhtdnDEVSDGdndnfnpfELTNHAVLLVGWgedEIKGE-KYWIVKNSWGSSWGEKGYFKIRRGTNEC 231
|
....*..
gi 157864857 330 LLTGYPV 336
Cdd:cd02621 232 GIESQAV 238
|
|
| DUF3586 |
pfam12131 |
Protein of unknown function (DUF3586); This domain is found in eukaryotes. This domain is ... |
355-417 |
5.27e-32 |
|
Protein of unknown function (DUF3586); This domain is found in eukaryotes. This domain is about 80 amino acids in length and is found associated with pfam08246, and pfam00112.
Pssm-ID: 403378 Cd Length: 75 Bit Score: 116.50 E-value: 5.27e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157864857 355 HAPKRVTVKQITCTDYFCRKGCKTTVIPTKECLPNGAGGSFQMECGDHQVLKLTYTSMNCTGE 417
Cdd:pfam12131 13 EAPKRVTVVQKTCTDYGCRKGCKSTTFPTGVCLKNTGGGSVMMTCGESEVLELIYRSSSCSGP 75
|
|
| Peptidase_C1A_CathepsinX |
cd02698 |
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ... |
126-326 |
8.77e-27 |
|
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: 107.50 E-value: 8.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 126 VPDAVDWREKGAV---TPVKNQ---GACGSCWAFSAVG------NIESQWAVAghkLVRLSEQQLVSCDHVDNgCGGGLM 193
Cdd:cd02698 1 LPKSWDWRNVNGVnyvSPTRNQhipQYCGSCWAHGSTSaladriNIARKGAWP---SVYLSVQVVIDCAGGGS-CHGGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 194 LQAFEWVLRNmnGTVfTEKSYPYVSGNGD---VPECSNSSELA--------PGARIDGYVSMESSERVMAAwLAKNGPIS 262
Cdd:cd02698 77 GGVYEYAHKH--GIP-DETCNPYQAKDGEcnpFNRCGTCNPFGecfaiknyTLYFVSDYGSVSGRDKMMAE-IYARGPIS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157864857 263 IAVDASSFM-SYHSGVLTSCIGEQL-NHGVLLVGYNMTGE-VPYWVIKNSWGEDWGEKGYVRVTMGV 326
Cdd:cd02698 153 CGIMATEALeNYTGGVYKEYVQDPLiNHIISVAGWGVDENgVEYWIVRNSWGEPWGERGWFRIVTSS 219
|
|
| PTZ00049 |
PTZ00049 |
cathepsin C-like protein; Provisional |
141-327 |
1.44e-17 |
|
cathepsin C-like protein; Provisional
Pssm-ID: 240244 [Multi-domain] Cd Length: 693 Bit Score: 85.39 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 141 VKNQGACGSCWAFSAVGNIESQWAVAGHKLV----------RLSEQQLVSCDHVDNGCGGGL--------------MLQA 196
Cdd:PTZ00049 400 VTNQLLCGSCYIASQMYAFKRRIEIALTKNLdkkylnnfddLLSIQTVLSCSFYDQGCNGGFpylvskmaklqgipLDKV 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 197 FEWV----------------------LRNMNGTVFTEKSYPYVSGNGDVPECSNSSELApgARIDGYV------SMESSE 248
Cdd:PTZ00049 480 FPYTateqtcpyqvdqsansmngsanLRQINAVFFSSETQSDMHADFEAPISSEPARWY--AKDYNYIggcygcNQCNGE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 249 RVMAAWLAKNGPISIAVDAS-SFMSYHSGV---------------LTSCIG-------EQLNHGVLLVGYNMTGE----V 301
Cdd:PTZ00049 558 KIMMNEIYRNGPIVASFEASpDFYDYADGVyyvedfpharrctvdLPKHNGvynitgwEKVNHAIVLVGWGEEEIngklY 637
|
250 260
....*....|....*....|....*.
gi 157864857 302 PYWVIKNSWGEDWGEKGYVRVTMGVN 327
Cdd:PTZ00049 638 KYWIGRNSWGKNWGKEGYFKIIRGKN 663
|
|
| PTZ00364 |
PTZ00364 |
dipeptidyl-peptidase I precursor; Provisional |
127-336 |
8.87e-16 |
|
dipeptidyl-peptidase I precursor; Provisional
Pssm-ID: 240381 [Multi-domain] Cd Length: 548 Bit Score: 79.55 E-value: 8.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 127 PDAVDWREKG------AVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKL------VRLSEQQLVSCDHVDNGCGGGLml 194
Cdd:PTZ00364 206 PAAWSWGDVGgasflpAAPPASPGRGCNSSYVEAALAAMMARVMVASNRTdplgqqTFLSARHVLDCSQYGQGCAGGF-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 195 qaFEWVLR--NMNGtVFTEKSY--PYVSGNGDVPECSNSSE-----LAPGARIDGYVSMESSERVMAAWLAKNGPI--SI 263
Cdd:PTZ00364 284 --PEEVGKfaETFG-ILTTDSYyiPYDSGDGVERACKTRRPsrryyFTNYGPLGGYYGAVTDPDEIIWEIYRHGPVpaSV 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 264 AVDA-----------SSFMSYHSGVLTSCIG--------EQLNHGVLLVGYNmTGEV--PYWVIKNSWGE--DWGEKGYV 320
Cdd:PTZ00364 361 YANSdwyncdensteDVRYVSLDDYSTASADrplrhyfaSNVNHTVLIIGWG-TDENggDYWLVLDPWGSrrSWCDGGTR 439
|
250
....*....|....*.
gi 157864857 321 RVTMGVNACLLTGYPV 336
Cdd:PTZ00364 440 KIARGVNAYNIESEVV 455
|
|
| Inhibitor_I29 |
smart00848 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
38-93 |
8.03e-15 |
|
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. 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: 68.42 E-value: 8.03e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 157864857 38 FEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPH-ARFGITKFFDLSEAE 93
Cdd:smart00848 1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYEHsYKLGVNQFSDLTPEE 57
|
|
| Inhibitor_I29 |
pfam08246 |
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ... |
38-94 |
2.21e-14 |
|
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: 67.29 E-value: 2.21e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 157864857 38 FEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPH-ARFGITKFFDLSEAEF 94
Cdd:pfam08246 1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGNVtYKLGLNKFADLTDEEF 58
|
|
| PTZ00462 |
PTZ00462 |
Serine-repeat antigen protein; Provisional |
141-329 |
3.76e-10 |
|
Serine-repeat antigen protein; Provisional
Pssm-ID: 185641 [Multi-domain] Cd Length: 1004 Bit Score: 62.39 E-value: 3.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 141 VKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSC------DHVDNGCGGGLMLQAFEwvlrnMNGTVFTEKSY 214
Cdd:PTZ00462 547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCskgehkDRCDEGSNPLEFLQIIE-----DNGFLPADSNY 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864857 215 PY--VSGNGDVP-ECSNSSELAPGARI-------------DGYVSMESSE---------RVMAAWLAKNGPISIAVDASS 269
Cdd:PTZ00462 622 LYnyTKVGEDCPdEEDHWMNLLDHGKIlnhnkkepnsldgKAYRAYESEHfhdkmdafiKIIKDEIMNKGSVIAYIKAEN 701
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157864857 270 FMSYH-SG--VLTSCIGEQLNHGVLLVGY----NMTGEV-PYWVIKNSWGEDWGEKGYVRVTM-GVNAC 329
Cdd:PTZ00462 702 VLGYEfNGkkVQNLCGDDTADHAVNIVGYgnyiNDEDEKkSYWIVRNSWGKYWGDEGYFKVDMyGPSHC 770
|
|
| PepC |
COG3579 |
Aminopeptidase C [Amino acid transport and metabolism]; |
286-319 |
5.63e-06 |
|
Aminopeptidase C [Amino acid transport and metabolism];
Pssm-ID: 442798 [Multi-domain] Cd Length: 440 Bit Score: 48.33 E-value: 5.63e-06
10 20 30
....*....|....*....|....*....|....*.
gi 157864857 286 LNHGVLLVGYNM--TGEVPYWVIKNSWGEDWGEKGY 319
Cdd:COG3579 361 DTHAMVITGVDLdqNGKPTRWKVENSWGDDNGYKGY 396
|
|
| Peptidase_C1_2 |
pfam03051 |
Peptidase C1-like family; This family is closely related to the Peptidase_C1 family pfam00112, ... |
286-319 |
5.77e-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: 41.94 E-value: 5.77e-04
10 20 30
....*....|....*....|....*....|....*.
gi 157864857 286 LNHGVLLVGYNM--TGEVPYWVIKNSWGEDWGEKGY 319
Cdd:pfam03051 359 MTHAMVLTGVDEddDGKPTKWKVENSWGEDSGEKGY 394
|
|
| Peptidase_C1B |
cd00585 |
Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin ... |
285-319 |
3.18e-03 |
|
Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin hydrolases (BH) and bacterial aminopeptidases C (pepC). The proteins of this subfamily contain a large insert relative to the C1A peptidase (papain) subfamily. BH is a cysteine peptidase that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. Bleomycin, a glycopeptide derived from the fungus Streptomyces verticullus, is an effective anticancer drug due to its ability to induce DNA strand breaks. Human BH is the major cause of tumor cell resistance to bleomycin chemotherapy, and is also genetically linked to Alzheimer's disease. In addition to its peptidase activity, the yeast BH (Gal6) binds DNA and acts as a repressor in the Gal4 regulatory system. BH forms a hexameric ring barrel structure with the active sites imbedded in the central channel. The bacterial homolog of BH, called pepC, is a cysteine aminopeptidase possessing broad specificity. Although its crystal structure has not been solved, biochemical analysis shows that pepC also forms a hexamer.
Pssm-ID: 238328 [Multi-domain] Cd Length: 437 Bit Score: 39.50 E-value: 3.18e-03
10 20 30
....*....|....*....|....*....|....*..
gi 157864857 285 QLNHGVLLVGYNM--TGEVPYWVIKNSWGEDWGEKGY 319
Cdd:cd00585 357 LMTHAMVLTGVDLdeDGKPVKWKVENSWGEKVGKKGY 393
|
|
| |
