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Conserved domains on  [gi|157864847|ref|XP_001681132|]
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cathepsin L-like protease [Leishmania major strain Friedlin]

Protein Classification

Peptidase_C1A and DUF3586 domain-containing protein( domain architecture ID 11488251)

Peptidase_C1A and DUF3586 domain-containing protein

Graphical summary

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List of domain hits

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: 748.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847   1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
Cdd:PTZ00203   1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  81 FGITKFFDLSEAEFAARYLNGAAYFAAVKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
Cdd:PTZ00203  81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
Cdd:PTZ00203 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
Cdd:PTZ00203 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
                        330       340
                 ....*....|....*....|....*.
gi 157864847 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
Cdd:PTZ00203 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
DUF3586 pfam12131
Protein of unknown function (DUF3586); This domain is found in eukaryotes. This domain is ...
355-417 5.49e-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: 5.49e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157864847  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: 748.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847   1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
Cdd:PTZ00203   1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  81 FGITKFFDLSEAEFAARYLNGAAYFAAVKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
Cdd:PTZ00203  81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
Cdd:PTZ00203 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
Cdd:PTZ00203 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
                        330       340
                 ....*....|....*....|....*.
gi 157864847 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
Cdd:PTZ00203 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
Peptidase_C1 pfam00112
Papain family cysteine protease;
126-339 7.59e-99

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 294.45  E-value: 7.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  126 VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRnmN 205
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKK--N 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  206 GTVFTEKSYPYVSGNGdvpECSNSSELAPGARIDGYVS-MESSERVMAAWLAKNGPISIAVDAS--SFMSYHSGVL--TS 280
Cdd:pfam00112  79 GGIVTESDYPYTAKDG---TCKFKKSNSKVAKIKGYGDvPYNDEEALQAALAKNGPVSVAIDAYerDFQLYKSGVYkhTE 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  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 1.36e-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: 1.36e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 127 PDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHV-DNGCGGGLMLQAFEWVlrnMN 205
Cdd:cd02248    1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFEYV---KN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 206 GTVFTEKSYPYVSGNGDvpeCSNSSElAPGARIDGYVSME-SSERVMAAWLAKNGPISIAVDAS-SFMSYHSGVLT--SC 281
Cdd:cd02248   78 GGLASESDYPYTGKDGT---CKYNSS-KVGAKITGYSNVPpGDEEALKAALANYGPVSVAIDASsSFQFYKGGIYSgpCC 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157864847 282 IGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSV 338
Cdd:cd02248  154 SNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
126-338 1.14e-75

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 234.01  E-value: 1.14e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847   126 VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDH-VDNGCGGGLMLQAFEWVLRnm 204
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGgGNCGCNGGLPDNAFEYIKK-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847   205 NGTVFTEKSYPYVsgngdvpecsnsselapgaridgyvsmesservmaawlakngpISIAVDASSFMSYHSGVL--TSCI 282
Cdd:smart00645  79 NGGLETESCYPYT-------------------------------------------GSVAIDASDFQFYKSGIYdhPGCG 115
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 157864847   283 GEQLNHGVLLVGYNMTGE--VPYWVIKNSWGEDWGEKGYVRVTMGV-NACLLTGYPVSV 338
Cdd:smart00645 116 SGTLDHAVLIVGYGTEVEngKDYWIVKNSWGTDWGENGYFRIARGKnNECGIEASVASY 174
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
123-323 2.11e-40

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 149.51  E-value: 2.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 123 LSAVPDAVDWREKgaVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKL---VRLSEQQLVSC----DHVDNGCGGGLMLQ 195
Cdd:COG4870    1 AAALPSSVDLRGY--VTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQarngDGTEGTDDGGSSLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 196 -AFEWvLRNmNGTVfTEKSYPYVSGNGDVPECSNSSELAPGARIDGY--VSMESSERVMAAW---LAKNGPISIAVDA-S 268
Cdd:COG4870   79 dALKL-LRW-SGVV-PESDWPYDDSDFTSQPSAAAYADARNYKIQDYyrLPGGGGATDLDAIkqaLAEGGPVVFGFYVyE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157864847 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 5.49e-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: 5.49e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157864847  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: 748.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847   1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
Cdd:PTZ00203   1 MATSRAALCAVAVVCVVLAAACAPARAIYVGTPAAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  81 FGITKFFDLSEAEFAARYLNGAAYFAAVKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
Cdd:PTZ00203  81 FGITKFFDLSEAEFAARYLNGAAYFAAAKQHAGQHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
Cdd:PTZ00203 161 SQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRNMNGTVFTEKSYPYVSGNGDVPECSNSSELAPGARIDG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
Cdd:PTZ00203 241 YVSMESSERVMAAWLAKNGPISIAVDASSFMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYV 320
                        330       340
                 ....*....|....*....|....*.
gi 157864847 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
Cdd:PTZ00203 321 RVTMGVNACLLTGYPVSVHVSQSPTP 346
Peptidase_C1 pfam00112
Papain family cysteine protease;
126-339 7.59e-99

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 294.45  E-value: 7.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  126 VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLMLQAFEWVLRnmN 205
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKK--N 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  206 GTVFTEKSYPYVSGNGdvpECSNSSELAPGARIDGYVS-MESSERVMAAWLAKNGPISIAVDAS--SFMSYHSGVL--TS 280
Cdd:pfam00112  79 GGIVTESDYPYTAKDG---TCKFKKSNSKVAKIKGYGDvPYNDEEALQAALAKNGPVSVAIDAYerDFQLYKSGVYkhTE 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  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 1.36e-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: 1.36e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 127 PDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHV-DNGCGGGLMLQAFEWVlrnMN 205
Cdd:cd02248    1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFEYV---KN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 206 GTVFTEKSYPYVSGNGDvpeCSNSSElAPGARIDGYVSME-SSERVMAAWLAKNGPISIAVDAS-SFMSYHSGVLT--SC 281
Cdd:cd02248   78 GGLASESDYPYTGKDGT---CKYNSS-KVGAKITGYSNVPpGDEEALKAALANYGPVSVAIDASsSFQFYKGGIYSgpCC 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157864847 282 IGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNACLLTGYPVSV 338
Cdd:cd02248  154 SNTNLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
126-338 1.14e-75

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 234.01  E-value: 1.14e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847   126 VPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDH-VDNGCGGGLMLQAFEWVLRnm 204
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGgGNCGCNGGLPDNAFEYIKK-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847   205 NGTVFTEKSYPYVsgngdvpecsnsselapgaridgyvsmesservmaawlakngpISIAVDASSFMSYHSGVL--TSCI 282
Cdd:smart00645  79 NGGLETESCYPYT-------------------------------------------GSVAIDASDFQFYKSGIYdhPGCG 115
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 157864847   283 GEQLNHGVLLVGYNMTGE--VPYWVIKNSWGEDWGEKGYVRVTMGV-NACLLTGYPVSV 338
Cdd:smart00645 116 SGTLDHAVLIVGYGTEVEngKDYWIVKNSWGTDWGENGYFRIARGKnNECGIEASVASY 174
PTZ00021 PTZ00021
falcipain-2; Provisional
37-322 8.99e-62

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 208.09  E-value: 8.99e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  37 LFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQAR-NPHARFGITKFFDLSEAEFAARYL---------NG----- 101
Cdd:PTZ00021 168 SFYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAHNNKeNVLYKKGMNRFGDLSFEEFKKKYLtlksfdfksNGkkspr 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 102 -AAYFAAVKQhagqhYRKARADLSAVpdAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVS 180
Cdd:PTZ00021 248 vINYDDVIKK-----YKPKDATFDHA--KYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVD 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 181 CDHVDNGCGGGLMLQAFEWVLrNMNGtVFTEKSYPYVsgnGDVPECSNSSELAPGARIDGYVSMeSSERVMAAwLAKNGP 260
Cdd:PTZ00021 321 CSFKNNGCYGGLIPNAFEDMI-ELGG-LCSEDDYPYV---SDTPELCNIDRCKEKYKIKSYVSI-PEDKFKEA-IRFLGP 393
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157864847 261 ISIAVDAS-SFMSYHSGVLTSCIGEQLNHGVLLVGYNM---------TGEVPYW-VIKNSWGEDWGEKGYVRV 322
Cdd:PTZ00021 394 ISVSIAVSdDFAFYKGGIFDGECGEEPNHAVILVGYGMeeiynsdtkKMEKRYYyIIKNSWGESWGEKGFIRI 466
PTZ00200 PTZ00200
cysteine proteinase; Provisional
38-340 1.28e-59

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 201.46  E-value: 1.28e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  38 FEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHARfGITKFFDLSEAEFAARY-----LNGAAYFAAVKQHA 112
Cdd:PTZ00200 126 FEEFNKKYNRKHATHAERLNRFLTFRNNYLEVKSHKGDEPYSK-EINKFSDLTEEEFRKLFpvikvPPKSNSTSHNNDFK 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 113 GQHY---------RKAR------ADLSAV-PDAVDWREKGAVTPVKNQGA-CGSCWAFSAVGNIESQWAVAGHKLVRLSE 175
Cdd:PTZ00200 205 ARHVsnptylknlKKAKntdedvKDPSKItGEGLDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRDKSVDLSE 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 176 QQLVSCDHVDNGCGGGLMLQAFEWVlrnMNGTVFTEKSYPYVSGNGdvpECSNSSelAPGARIDGYVSMESSErVMAAWL 255
Cdd:PTZ00200 285 QELVNCDTKSQGCSGGYPDTALEYV---KNKGLSSSSDVPYLAKDG---KCVVSS--TKKVYIDSYLVAKGKD-VLNKSL 355
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 256 AKnGPISIAVDAS-SFMSYHSGVLTSCIGEQLNHGVLLV--GYNMTGEVPYWVIKNSWGEDWGEKGY---VRVTMGVNAC 329
Cdd:PTZ00200 356 VI-SPTVVYIAVSrELLKYKSGVYNGECGKSLNHAVLLVgeGYDEKTKKRYWIIKNSWGTDWGENGYmrlERTNEGTDKC 434
                        330
                 ....*....|....
gi 157864847 330 --LLTGY-PVSVHV 340
Cdd:PTZ00200 435 giLTVGLtPVFYSS 448
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
123-323 2.11e-40

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 149.51  E-value: 2.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 123 LSAVPDAVDWREKgaVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKL---VRLSEQQLVSC----DHVDNGCGGGLMLQ 195
Cdd:COG4870    1 AAALPSSVDLRGY--VTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQarngDGTEGTDDGGSSLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 196 -AFEWvLRNmNGTVfTEKSYPYVSGNGDVPECSNSSELAPGARIDGY--VSMESSERVMAAW---LAKNGPISIAVDA-S 268
Cdd:COG4870   79 dALKL-LRW-SGVV-PESDWPYDDSDFTSQPSAAAYADARNYKIQDYyrLPGGGGATDLDAIkqaLAEGGPVVFGFYVyE 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157864847 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 157864847 127 PDAVDWREK----GAVTPVKNQGACGSCWAFSAVGNIESQWAVA--GHKLVRLSEQQLVSCDHV-DNGCGGGLMLQAFEW 199
Cdd:cd02620    1 PESFDAREKwpncISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQsnGKENVLLSAQDLLSCCSGcGDGCNGGYPDAAWKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 200 vLRNmNGTVfTEKSYPYVSGNGDV---------------PECSNSSELAPGARI---DGYVSMESSERVMAAWLAKNGPI 261
Cdd:cd02620   81 -LTT-TGVV-TGGCQPYTIPPCGHhpegpppccgtpyctPKCQDGCEKTYEEDKhkgKSAYSVPSDETDIMKEIMTNGPV 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157864847 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 2.25e-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: 2.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 130 VDWREKGaVTPVKNQGACGSCWAFSAVGNIESQWAVAG--HKLVRLSEQQLVSCDHV-----DNGCGGGLMLQAFEWVLR 202
Cdd:cd02619    2 VDLRPLR-LTPVKNQGSRGSCWAFASAYALESAYRIKGgeDEYVDLSPQYLYICANDeclgiNGSCDGGGPLSALLKLVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 203 NmNGtVFTEKSYPYVSGNGDVPECSNSSELAPGARIDGYVSMESS-ERVMAAWLAKNGPISIAVDASS-FMSYHSGVLTS 280
Cdd:cd02619   81 L-KG-IPPEEDYPYGAESDGEEPKSEAALNAAKVKLKDYRRVLKNnIEDIKEALAKGGPVVAGFDVYSgFDRLKEGIIYE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 157864847 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 4.44e-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: 4.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 127 PDAVDWREKGA----VTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLV------RLSEQQLVSCDHVDNGCGGGLmlqa 196
Cdd:cd02621    2 PKSFDWGDVNNgfnyVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDplgqqpILSPQHVLSCSQYSQGCDGGF---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 197 FEWVLRNM--NGtVFTEKSYPYVSGngDVPECSNSSE------LAPGARIDGYVSMESSERVMaaW-LAKNGPISIAVDA 267
Cdd:cd02621   78 PFLVGKFAedFG-IVTEDYFPYTAD--DDRPCKASPSecrryyFSDYNYVGGCYGCTNEDEMK--WeIYRNGPIVVAFEV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 268 -SSFMSYHSGV------LTSCIG--------EQLNHGVLLVGY---NMTGEvPYWVIKNSWGEDWGEKGYVRVTMGVNAC 329
Cdd:cd02621  153 ySDFDFYKEGVyhhtdnDEVSDGdndnfnpfELTNHAVLLVGWgedEIKGE-KYWIVKNSWGSSWGEKGYFKIRRGTNEC 231

                 ....*..
gi 157864847 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 5.49e-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: 5.49e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157864847  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 8.69e-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: 8.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 126 VPDAVDWREKGAV---TPVKNQ---GACGSCWAFSAVG------NIESQWAVAghkLVRLSEQQLVSCDHVDNgCGGGLM 193
Cdd:cd02698    1 LPKSWDWRNVNGVnyvSPTRNQhipQYCGSCWAHGSTSaladriNIARKGAWP---SVYLSVQVVIDCAGGGS-CHGGDP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 194 LQAFEWVLRNmnGTVfTEKSYPYVSGNGD---VPECSNSSELA--------PGARIDGYVSMESSERVMAAwLAKNGPIS 262
Cdd:cd02698   77 GGVYEYAHKH--GIP-DETCNPYQAKDGEcnpFNRCGTCNPFGecfaiknyTLYFVSDYGSVSGRDKMMAE-IYARGPIS 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157864847 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 157864847 141 VKNQGACGSCWAFSAVGNIESQWAVAGHKLV----------RLSEQQLVSCDHVDNGCGGGL--------------MLQA 196
Cdd:PTZ00049 400 VTNQLLCGSCYIASQMYAFKRRIEIALTKNLdkkylnnfddLLSIQTVLSCSFYDQGCNGGFpylvskmaklqgipLDKV 479
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 197 FEWV----------------------LRNMNGTVFTEKSYPYVSGNGDVPECSNSSELApgARIDGYV------SMESSE 248
Cdd:PTZ00049 480 FPYTateqtcpyqvdqsansmngsanLRQINAVFFSSETQSDMHADFEAPISSEPARWY--AKDYNYIggcygcNQCNGE 557
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 249 RVMAAWLAKNGPISIAVDAS-SFMSYHSGV---------------LTSCIG-------EQLNHGVLLVGYNMTGE----V 301
Cdd:PTZ00049 558 KIMMNEIYRNGPIVASFEASpDFYDYADGVyyvedfpharrctvdLPKHNGvynitgwEKVNHAIVLVGWGEEEIngklY 637
                        250       260
                 ....*....|....*....|....*.
gi 157864847 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 157864847 127 PDAVDWREKG------AVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKL------VRLSEQQLVSCDHVDNGCGGGLml 194
Cdd:PTZ00364 206 PAAWSWGDVGgasflpAAPPASPGRGCNSSYVEAALAAMMARVMVASNRTdplgqqTFLSARHVLDCSQYGQGCAGGF-- 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 195 qaFEWVLR--NMNGtVFTEKSY--PYVSGNGDVPECSNSSE-----LAPGARIDGYVSMESSERVMAAWLAKNGPI--SI 263
Cdd:PTZ00364 284 --PEEVGKfaETFG-ILTTDSYyiPYDSGDGVERACKTRRPsrryyFTNYGPLGGYYGAVTDPDEIIWEIYRHGPVpaSV 360
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847 264 AVDA-----------SSFMSYHSGVLTSCIG--------EQLNHGVLLVGYNmTGEV--PYWVIKNSWGE--DWGEKGYV 320
Cdd:PTZ00364 361 YANSdwyncdensteDVRYVSLDDYSTASADrplrhyfaSNVNHTVLIIGWG-TDENggDYWLVLDPWGSrrSWCDGGTR 439
                        250
                 ....*....|....*.
gi 157864847 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 7.88e-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: 7.88e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157864847    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 157864847   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 157864847  141 VKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSC------DHVDNGCGGGLMLQAFEwvlrnMNGTVFTEKSY 214
Cdd:PTZ00462  547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCskgehkDRCDEGSNPLEFLQIIE-----DNGFLPADSNY 621
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157864847  215 PY--VSGNGDVP-ECSNSSELAPGARI-------------DGYVSMESSE---------RVMAAWLAKNGPISIAVDASS 269
Cdd:PTZ00462  622 LYnyTKVGEDCPdEEDHWMNLLDHGKIlnhnkkepnsldgKAYRAYESEHfhdkmdafiKIIKDEIMNKGSVIAYIKAEN 701
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157864847  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 157864847 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 157864847  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 157864847 285 QLNHGVLLVGYNM--TGEVPYWVIKNSWGEDWGEKGY 319
Cdd:cd00585  357 LMTHAMVLTGVDLdeDGKPVKWKVENSWGEKVGKKGY 393
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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