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Conserved domains on  [gi|2096748026|ref|XP_043577531|]
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cysteine proteinase 4-like [Chiloscyllium plagiosum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 480-692 5.84e-116

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: 346.53  E-value: 5.84e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 480 PAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCTQSvGNRGCNGGFKVRALLFIKEHG 559
Cdd:cd02248     1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEYVKNGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 560 INSEESYPYTAKDGDCKSNKKDTVATCKGVTIIPKNSEADLAAAVATVGPISVSIDAEHrSFMLYKSGIFYEPHCSSVNL 639
Cdd:cd02248    80 LASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNTNL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2096748026 640 DHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGYVHMAKDmDNNCGIATTAVYP 692
Cdd:cd02248   159 NHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Peptidase_C1 super family cl23744
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 188-281 1.33e-52

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.


The actual alignment was detected with superfamily member pfam00112:

Pssm-ID: 451520 [Multi-domain]  Cd Length: 214  Bit Score: 180.81  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 188 IPKSVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSGpqGNQGCGGGWMENAFLYVHEN 267
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDT--FNNGCNGGLPDNAFEYIKKN 78

                          90
                  ....*....|....
gi 2096748026 268 NGIDSETGYPYTGQ 281
Cdd:pfam00112  79 GGIVTESDYPYTAK 92
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 101-159 2.32e-17

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: 76.51  E-value: 2.32e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  101 WEKWKVLHQKQYTENEEGVRRM-VWEKNFRFIENHNLEYslgKHSFNLKMNHFGDMTLEE 159
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFaIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
 
Name Accession Description Interval E-value
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 480-692 5.84e-116

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: 346.53  E-value: 5.84e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 480 PAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCTQSvGNRGCNGGFKVRALLFIKEHG 559
Cdd:cd02248     1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEYVKNGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 560 INSEESYPYTAKDGDCKSNKKDTVATCKGVTIIPKNSEADLAAAVATVGPISVSIDAEHrSFMLYKSGIFYEPHCSSVNL 639
Cdd:cd02248    80 LASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNTNL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2096748026 640 DHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGYVHMAKDmDNNCGIATTAVYP 692
Cdd:cd02248   159 NHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Peptidase_C1 pfam00112
Papain family cysteine protease;
479-692 5.71e-114

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 341.44  E-value: 5.71e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 479 LPAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCtqSVGNRGCNGGFKVRALLFIKE- 557
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDC--DTFNNGCNGGLPDNAFEYIKKn 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 558 HGINSEESYPYTAKDGDCKSNKKD-TVATCKGVTIIPKNSEADLAAAVATVGPISVSIDAEHRSFMLYKSGIFYEPHCSS 636
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNsKVAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2096748026 637 vNLDHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGYVHMAKDMDNNCGIATTAVYP 692
Cdd:pfam00112 159 -ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYP 213
Pept_C1 smart00645
Papain family cysteine protease;
479-692 4.90e-81

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 254.81  E-value: 4.90e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  479 LPAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCTQSvGNRGCNGGFKVRALLFIKEH 558
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGG-GNCGCNGGLPDNAFEYIKKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  559 -GINSEESYPYTAkdgdcksnkkdtvatckgvtiipknseadlaaavatvgpiSVSIDAEHrsFMLYKSGIFYEPHCSSV 637
Cdd:smart00645  80 gGLETESCYPYTG----------------------------------------SVAIDASD--FQFYKSGIYDHPGCGSG 117

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2096748026  638 NLDHEVLAVGYGT--ENQKPYWIVKNSWGTSWGNEGYVHMAKDMDNNCGI-ATTAVYP 692
Cdd:smart00645 118 TLDHAVLIVGYGTevENGKDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 446-694 9.77e-55

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 191.07  E-value: 9.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 446 LTAEEFG-QYLNKFN-----KKGGGNFTFKVFTANKNVelPAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNK 519
Cdd:PTZ00203   89 LSEAEFAaRYLNGAAyfaaaKQHAGQHYRKARADLSAV--PDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVA 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 520 TGKLISLSEQYLMDCTQSvgNRGCNGGFKVRALLFIKEH---GINSEESYPYTAKDGDCK--SNKKDTV--ATCKGVTII 592
Cdd:PTZ00203  167 GHKLVRLSEQQLVSCDHV--DNGCGGGLMLQAFEWVLRNmngTVFTEKSYPYVSGNGDVPecSNSSELApgARIDGYVSM 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 593 PKNsEADLAAAVATVGPISVSIDAEhrSFMLYKSGIFyePHCSSVNLDHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGY 672
Cdd:PTZ00203  245 ESS-ERVMAAWLAKNGPISIAVDAS--SFMSYHSGVL--TSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGY 319

                         250       260
                  ....*....|....*....|..
gi 2096748026 673 VHMAKDMdNNCGIATTAVYPEV 694
Cdd:PTZ00203  320 VRVTMGV-NACLLTGYPVSVHV 340
Peptidase_C1 pfam00112
Papain family cysteine protease;
188-281 1.33e-52

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 180.81  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 188 IPKSVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSGpqGNQGCGGGWMENAFLYVHEN 267
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDT--FNNGCNGGLPDNAFEYIKKN 78

                          90
                  ....*....|....
gi 2096748026 268 NGIDSETGYPYTGQ 281
Cdd:pfam00112  79 GGIVTESDYPYTAK 92
Pept_C1 smart00645
Papain family cysteine protease;
188-280 7.48e-51

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 174.69  E-value: 7.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  188 IPKSVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSGPqGNQGCGGGWMENAFLYVHEN 267
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGG-GNCGCNGGLPDNAFEYIKKN 79

                           90
                   ....*....|...
gi 2096748026  268 NGIDSETGYPYTG 280
Cdd:smart00645  80 GGLETESCYPYTG 92
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 189-281 7.02e-50

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: 173.19  E-value: 7.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 189 PKSVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSGPqGNQGCGGGWMENAFLYVhENN 268
Cdd:cd02248     1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEYV-KNG 78

                          90
                  ....*....|...
gi 2096748026 269 GIDSETGYPYTGQ 281
Cdd:cd02248    79 GLASESDYPYTGK 91
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
477-686 3.16e-44

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 164.54  E-value: 3.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 477 VELPAAVDWRpkGYVTPVKDQGQCGSCWAFSTTGVLEGQV---FNKTGKLISLSEQYLMDCTQ---SVGNRGCNGGFKVR 550
Cdd:COG4870     2 AALPSSVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLkkqAGAPGTSLDLSELFLYNQARngdGTEGTDDGGSSLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 551 ALLFIKEHGINSEESYPYTAKDGDCKSNK----KDTVATCKGVTIIP-KNSEADLAA---AVATVGPISVSIDAeHRSFM 622
Cdd:COG4870    80 ALKLLRWSGVVPESDWPYDDSDFTSQPSAaayaDARNYKIQDYYRLPgGGGATDLDAikqALAEGGPVVFGFYV-YESFY 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096748026 623 LYKSGIFYEPHCSSVNLDHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGYVHMA-KDMDNNCGIA 686
Cdd:COG4870   159 NYTGGVYYPTPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWISyDDLLIGAGAA 223
PTZ00021 PTZ00021
falcipain-2; Provisional
 108-288 2.21e-35

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 140.29  E-value: 2.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 108 HQKQY-TENEEGVRRMVWEKNFRFIENHNleySLGKHSFNLKMNHFGDMTLEEFNEQMNGFRHFKPRNSSRPLSRIPELA 186
Cdd:PTZ00021  176 HGKKYqTPDEMQQRYLSFVENLAKINAHN---NKENVLYKKGMNRFGDLSFEEFKKKYLTLKSFDFKSNGKKSPRVINYD 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 187 EIPK------------SVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSgpQGNQGCGG 254
Cdd:PTZ00021  253 DVIKkykpkdatfdhaKYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCS--FKNNGCYG 330

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2096748026 255 GWMENAFLYVHENNGIDSETGYPYTGQVrpPDIC 288
Cdd:PTZ00021  331 GLIPNAFEDMIELGGLCSEDDYPYVSDT--PELC 362
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
185-281 1.96e-19

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 91.35  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 185 LAEIPKSVDWRdeGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKL---IPLSEQNLVDC--SGPQGNQGCGGGWMEN 259
Cdd:COG4870     1 AAALPSSVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQarNGDGTEGTDDGGSSLR 78

                          90       100
                  ....*....|....*....|..
gi 2096748026 260 AFLYVHENNGIDSETGYPYTGQ 281
Cdd:COG4870    79 DALKLLRWSGVVPESDWPYDDS 100
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 101-159 2.32e-17

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: 76.51  E-value: 2.32e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  101 WEKWKVLHQKQYTENEEGVRRM-VWEKNFRFIENHNLEYslgKHSFNLKMNHFGDMTLEE 159
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFaIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 101-160 2.72e-16

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: 73.45  E-value: 2.72e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096748026 101 WEKWKVLHQKQY-TENEEGVRRMVWEKNFRFIENHNleySLGKHSFNLKMNHFGDMTLEEF 160
Cdd:pfam08246   1 FDDWMKKYGKSYrSEEEELYRFQIFKENLKRIEEHN---SNGNVTYKLGLNKFADLTDEEF 58
 
Name Accession Description Interval E-value
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 480-692 5.84e-116

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: 346.53  E-value: 5.84e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 480 PAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCTQSvGNRGCNGGFKVRALLFIKEHG 559
Cdd:cd02248     1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEYVKNGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 560 INSEESYPYTAKDGDCKSNKKDTVATCKGVTIIPKNSEADLAAAVATVGPISVSIDAEHrSFMLYKSGIFYEPHCSSVNL 639
Cdd:cd02248    80 LASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNTNL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2096748026 640 DHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGYVHMAKDmDNNCGIATTAVYP 692
Cdd:cd02248   159 NHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Peptidase_C1 pfam00112
Papain family cysteine protease;
479-692 5.71e-114

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 341.44  E-value: 5.71e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 479 LPAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCtqSVGNRGCNGGFKVRALLFIKE- 557
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDC--DTFNNGCNGGLPDNAFEYIKKn 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 558 HGINSEESYPYTAKDGDCKSNKKD-TVATCKGVTIIPKNSEADLAAAVATVGPISVSIDAEHRSFMLYKSGIFYEPHCSS 636
Cdd:pfam00112  79 GGIVTESDYPYTAKDGTCKFKKSNsKVAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2096748026 637 vNLDHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGYVHMAKDMDNNCGIATTAVYP 692
Cdd:pfam00112 159 -ELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYP 213
Pept_C1 smart00645
Papain family cysteine protease;
479-692 4.90e-81

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 254.81  E-value: 4.90e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  479 LPAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCTQSvGNRGCNGGFKVRALLFIKEH 558
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGG-GNCGCNGGLPDNAFEYIKKN 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  559 -GINSEESYPYTAkdgdcksnkkdtvatckgvtiipknseadlaaavatvgpiSVSIDAEHrsFMLYKSGIFYEPHCSSV 637
Cdd:smart00645  80 gGLETESCYPYTG----------------------------------------SVAIDASD--FQFYKSGIYDHPGCGSG 117

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2096748026  638 NLDHEVLAVGYGT--ENQKPYWIVKNSWGTSWGNEGYVHMAKDMDNNCGI-ATTAVYP 692
Cdd:smart00645 118 TLDHAVLIVGYGTevENGKDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 446-694 9.77e-55

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 191.07  E-value: 9.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 446 LTAEEFG-QYLNKFN-----KKGGGNFTFKVFTANKNVelPAAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNK 519
Cdd:PTZ00203   89 LSEAEFAaRYLNGAAyfaaaKQHAGQHYRKARADLSAV--PDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVA 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 520 TGKLISLSEQYLMDCTQSvgNRGCNGGFKVRALLFIKEH---GINSEESYPYTAKDGDCK--SNKKDTV--ATCKGVTII 592
Cdd:PTZ00203  167 GHKLVRLSEQQLVSCDHV--DNGCGGGLMLQAFEWVLRNmngTVFTEKSYPYVSGNGDVPecSNSSELApgARIDGYVSM 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 593 PKNsEADLAAAVATVGPISVSIDAEhrSFMLYKSGIFyePHCSSVNLDHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGY 672
Cdd:PTZ00203  245 ESS-ERVMAAWLAKNGPISIAVDAS--SFMSYHSGVL--TSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGY 319

                         250       260
                  ....*....|....*....|..
gi 2096748026 673 VHMAKDMdNNCGIATTAVYPEV 694
Cdd:PTZ00203  320 VRVTMGV-NACLLTGYPVSVHV 340
Peptidase_C1 pfam00112
Papain family cysteine protease;
188-281 1.33e-52

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 180.81  E-value: 1.33e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 188 IPKSVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSGpqGNQGCGGGWMENAFLYVHEN 267
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDT--FNNGCNGGLPDNAFEYIKKN 78

                          90
                  ....*....|....
gi 2096748026 268 NGIDSETGYPYTGQ 281
Cdd:pfam00112  79 GGIVTESDYPYTAK 92
Pept_C1 smart00645
Papain family cysteine protease;
188-280 7.48e-51

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 174.69  E-value: 7.48e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  188 IPKSVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSGPqGNQGCGGGWMENAFLYVHEN 267
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGG-GNCGCNGGLPDNAFEYIKKN 79

                           90
                   ....*....|...
gi 2096748026  268 NGIDSETGYPYTG 280
Cdd:smart00645  80 GGLETESCYPYTG 92
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
 189-281 7.02e-50

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: 173.19  E-value: 7.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 189 PKSVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSGPqGNQGCGGGWMENAFLYVhENN 268
Cdd:cd02248     1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTS-GNNGCNGGNPDNAFEYV-KNG 78

                          90
                  ....*....|...
gi 2096748026 269 GIDSETGYPYTGQ 281
Cdd:cd02248    79 GLASESDYPYTGK 91
PTZ00200 PTZ00200
cysteine proteinase; Provisional
 484-692 7.36e-49

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 177.96  E-value: 7.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 484 DWRPKGYVTPVKDQG-QCGSCWAFSTTGVLEG---QVFNKTgklISLSEQYLMDCTQSvgNRGCNGGFKVRALLFIKEHG 559
Cdd:PTZ00200  239 DWRRADAVTKVKDQGlNCGSCWAFSSVGSVESlykIYRDKS---VDLSEQELVNCDTK--SQGCSGGYPDTALEYVKNKG 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 560 INSEESYPYTAKDGDCKsNKKDTVATCKGVTIipkNSEADLAAAVATVGPISVSIdAEHRSFMLYKSGIfYEPHCSsVNL 639
Cdd:PTZ00200  314 LSSSSDVPYLAKDGKCV-VSSTKKVYIDSYLV---AKGKDVLNKSLVISPTVVYI-AVSRELLKYKSGV-YNGECG-KSL 386

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2096748026 640 DHEVLAVG--YGTENQKPYWIVKNSWGTSWGNEGYVHMA--KDMDNNCGIATTAVYP 692
Cdd:PTZ00200  387 NHAVLLVGegYDEKTKKRYWIIKNSWGTDWGENGYMRLErtNEGTDKCGILTVGLTP 443
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
477-686 3.16e-44

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 164.54  E-value: 3.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 477 VELPAAVDWRpkGYVTPVKDQGQCGSCWAFSTTGVLEGQV---FNKTGKLISLSEQYLMDCTQ---SVGNRGCNGGFKVR 550
Cdd:COG4870     2 AALPSSVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLkkqAGAPGTSLDLSELFLYNQARngdGTEGTDDGGSSLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 551 ALLFIKEHGINSEESYPYTAKDGDCKSNK----KDTVATCKGVTIIP-KNSEADLAA---AVATVGPISVSIDAeHRSFM 622
Cdd:COG4870    80 ALKLLRWSGVVPESDWPYDDSDFTSQPSAaayaDARNYKIQDYYRLPgGGGATDLDAikqALAEGGPVVFGFYV-YESFY 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2096748026 623 LYKSGIFYEPHCSSVNLDHEVLAVGYGTENQKPYWIVKNSWGTSWGNEGYVHMA-KDMDNNCGIA 686
Cdd:COG4870   159 NYTGGVYYPTPGDASLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWISyDDLLIGAGAA 223
PTZ00021 PTZ00021
falcipain-2; Provisional
 481-692 1.33e-43

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 164.17  E-value: 1.33e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 481 AAVDWRPKGYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCtqSVGNRGCNGGFKVRALL-FIKEHG 559
Cdd:PTZ00021  268 AKYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDC--SFKNNGCYGGLIPNAFEdMIELGG 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 560 INSEESYPYTA-KDGDCKSNKKDTVATCKGVTIIPKNSeadLAAAVATVGPISVSIDAEHrSFMLYKSGIFyEPHCSSvN 638
Cdd:PTZ00021  346 LCSEDDYPYVSdTPELCNIDRCKEKYKIKSYVSIPEDK---FKEAIRFLGPISVSIAVSD-DFAFYKGGIF-DGECGE-E 419

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2096748026 639 LDHEVLAVGYGTE---------NQKPYW-IVKNSWGTSWGNEGYVHMAKD---MDNNCGIATTAVYP 692
Cdd:PTZ00021  420 PNHAVILVGYGMEeiynsdtkkMEKRYYyIIKNSWGESWGEKGFIRIETDengLMKTCSLGTEAYVP 486
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 483-672 2.73e-42

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: 152.67  E-value: 2.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 483 VDWRPKgYVTPVKDQGQCGSCWAFSTTGVLEGQVFNKTG--KLISLSEQYLMDCT---QSVGNRGCNGGFKVRALL-FIK 556
Cdd:cd02619     2 VDLRPL-RLTPVKNQGSRGSCWAFASAYALESAYRIKGGedEYVDLSPQYLYICAndeCLGINGSCDGGGPLSALLkLVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 557 EHGINSEESYPYTAKDGDCKSN-KKDTVATCKGVT---IIPKNSEADLAAAVATVGPISVSIDAeHRSFMLYKSGIFYEP 632
Cdd:cd02619    81 LKGIPPEEDYPYGAESDGEEPKsEAALNAAKVKLKdyrRVLKNNIEDIKEALAKGGPVVAGFDV-YSGFDRLKEGIIYEE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2096748026 633 ----HCSSVNL-DHEVLAVGYGTENQ--KPYWIVKNSWGTSWGNEGY 672
Cdd:cd02619   160 ivylLYEDGDLgGHAVVIVGYDDNYVegKGAFIVKNSWGTDWGDNGY 206
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
 493-685 2.17e-41

Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.


Pssm-ID: 239111 [Multi-domain]  Cd Length: 236  Bit Score: 150.88  E-value: 2.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 493 PVKDQGQCGSCWAFSTTGVL--------EGQVfnktgkLISLSEQYLMDCTQSVGNrGCNGGFKVRALLFIKEHGINSEE 564
Cdd:cd02620    18 EIRDQGNCGSCWAFSAVEAFsdrlciqsNGKE------NVLLSAQDLLSCCSGCGD-GCNGGYPDAAWKYLTTTGVVTGG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 565 SYPYTAKDGDCKSNKKDTV-------ATC-KGVTIIPK-------------NSEADLAAAVATVGPISVSIDAeHRSFML 623
Cdd:cd02620    91 CQPYTIPPCGHHPEGPPPCcgtpyctPKCqDGCEKTYEedkhkgksaysvpSDETDIMKEIMTNGPVQAAFTV-YEDFLY 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2096748026 624 YKSGIFYepHCSSVNLD-HEVLAVGYGTENQKPYWIVKNSWGTSWGNEGYVHMAKDmDNNCGI 685
Cdd:cd02620   170 YKSGVYQ--HTSGKQLGgHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRG-SNECGI 229
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
 479-691 2.49e-40

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: 147.92  E-value: 2.49e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 479 LPAAVDWRPKG----YVTPVKDQGQCGSCWAFSTTGVLEGQV---FNKTGKL---ISLSEQYLMDCTQSvgNRGCNGGFK 548
Cdd:cd02621     1 LPKSFDWGDVNngfnYVSPVRNQGGCGSCYAFASVYALEARImiaSNKTDPLgqqPILSPQHVLSCSQY--SQGCDGGFP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 549 VRALLFIKEHGINSEESYPYTA-KDGDCKSNKKDT----------VATCKGVTiipknSEADLAAAVATVGPISVSIDAe 617
Cdd:cd02621    79 FLVGKFAEDFGIVTEDYFPYTAdDDRPCKASPSECrryyfsdynyVGGCYGCT-----NEDEMKWEIYRNGPIVVAFEV- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 618 HRSFMLYKSGIF----YEPHCSSVN--------LDHEVLAVGYGTENQK--PYWIVKNSWGTSWGNEGYVHMAKDMdNNC 683
Cdd:cd02621   153 YSDFDFYKEGVYhhtdNDEVSDGDNdnfnpfelTNHAVLLVGWGEDEIKgeKYWIVKNSWGSSWGEKGYFKIRRGT-NEC 231


                  ....*...
gi 2096748026 684 GIATTAVY 691
Cdd:cd02621   232 GIESQAVF 239
PTZ00021 PTZ00021
falcipain-2; Provisional
 108-288 2.21e-35

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 140.29  E-value: 2.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 108 HQKQY-TENEEGVRRMVWEKNFRFIENHNleySLGKHSFNLKMNHFGDMTLEEFNEQMNGFRHFKPRNSSRPLSRIPELA 186
Cdd:PTZ00021  176 HGKKYqTPDEMQQRYLSFVENLAKINAHN---NKENVLYKKGMNRFGDLSFEEFKKKYLTLKSFDFKSNGKKSPRVINYD 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 187 EIPK------------SVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSgpQGNQGCGG 254
Cdd:PTZ00021  253 DVIKkykpkdatfdhaKYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCS--FKNNGCYG 330

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2096748026 255 GWMENAFLYVHENNGIDSETGYPYTGQVrpPDIC 288
Cdd:PTZ00021  331 GLIPNAFEDMIELGGLCSEDDYPYVSDT--PELC 362
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
 479-694 1.46e-34

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: 131.77  E-value: 1.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 479 LPAAVDWR---PKGYVTPVKDQ---GQCGSCWAFSTTGVLEGQVF---NKTGKLISLSEQYLMDCTQsVGNrgCNGGFKV 549
Cdd:cd02698     1 LPKSWDWRnvnGVNYVSPTRNQhipQYCGSCWAHGSTSALADRINiarKGAWPSVYLSVQVVIDCAG-GGS--CHGGDPG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 550 RALLFIKEHGINSEESYPYTAKDGDCKSNKK----DTVATCKGVTIIPK---------NSEADLAAAVATVGPISVSIDA 616
Cdd:cd02698    78 GVYEYAHKHGIPDETCNPYQAKDGECNPFNRcgtcNPFGECFAIKNYTLyfvsdygsvSGRDKMMAEIYARGPISCGIMA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 617 eHRSFMLYKSGIFYEPHCSSVnLDHEVLAVGYGTENQK-PYWIVKNSWGTSWGNEGYVHMA----KDMDNNCGIATTAVY 691
Cdd:cd02698   158 -TEALENYTGGVYKEYVQDPL-INHIISVAGWGVDENGvEYWIVRNSWGEPWGERGWFRIVtssyKGARYNLAIEEDCAW 235


                  ...
gi 2096748026 692 PEV 694
Cdd:cd02698   236 ADP 238
PTZ00203 PTZ00203
cathepsin L protease; Provisional
 101-279 2.35e-31

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 125.58  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 101 WEKWKVLHQKQY-TENEEGVRRMVWEKNFRFIENHNleySLGKHSfNLKMNHFGDMTLEEFNEQ-MNGFRHFKP--RNSS 176
Cdd:PTZ00203   38 FEEFKRTYQRAYgTLTEEQQRLANFERNLELMREHQ---ARNPHA-RFGITKFFDLSEAEFAARyLNGAAYFAAakQHAG 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 177 RPLSRI-PELAEIPKSVDWRDEGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIPLSEQNLVDCSgpQGNQGCGGG 255
Cdd:PTZ00203  114 QHYRKArADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCD--HVDNGCGGG 191

                         170       180
                  ....*....|....*....|....*.
gi 2096748026 256 WMENAFLYV--HENNGIDSETGYPYT 279
Cdd:PTZ00203  192 LMLQAFEWVlrNMNGTVFTEKSYPYV 217
PTZ00200 PTZ00200
cysteine proteinase; Provisional
 102-284 1.23e-25

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 110.55  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 102 EKWKVLHQkqyTENEEGVRRMVWEKNFRFIENHNleyslGKHSFNLKMNHFGDMTLEEFNEQmngFRHFKPRNSSRPLSR 181
Cdd:PTZ00200  131 KKYNRKHA---THAERLNRFLTFRNNYLEVKSHK-----GDEPYSKEINKFSDLTEEEFRKL---FPVIKVPPKSNSTSH 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 182 IPELAE-----------------------IPKSV-----DWRDEGYVTPVKNQGS-CGSCWAFSSTGALEG--QTFKKtg 230
Cdd:PTZ00200  200 NNDFKArhvsnptylknlkkakntdedvkDPSKItgeglDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESlyKIYRD-- 277

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2096748026 231 KLIPLSEQNLVDCSgpQGNQGCGGGWMENAFLYVHeNNGIDSETGYPYTGQVRP 284
Cdd:PTZ00200  278 KSVDLSEQELVNCD--TKSQGCSGGYPDTALEYVK-NKGLSSSSDVPYLAKDGK 328
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
 191-288 8.73e-21

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: 91.42  E-value: 8.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 191 SVDWRDEgYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTG--KLIPLSEQNLVDCSGPQ---GNQGCGGGWMENAFLYVH 265
Cdd:cd02619     1 SVDLRPL-RLTPVKNQGSRGSCWAFASAYALESAYRIKGGedEYVDLSPQYLYICANDEclgINGSCDGGGPLSALLKLV 79

                          90       100
                  ....*....|....*....|...
gi 2096748026 266 ENNGIDSETGYPYTGQVRPPDIC 288
Cdd:cd02619    80 ALKGIPPEEDYPYGAESDGEEPK 102
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
185-281 1.96e-19

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 91.35  E-value: 1.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 185 LAEIPKSVDWRdeGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKL---IPLSEQNLVDC--SGPQGNQGCGGGWMEN 259
Cdd:COG4870     1 AAALPSSVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQarNGDGTEGTDDGGSSLR 78

                          90       100
                  ....*....|....*....|..
gi 2096748026 260 AFLYVHENNGIDSETGYPYTGQ 281
Cdd:COG4870    79 DALKLLRWSGVVPESDWPYDDS 100
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
 189-282 1.68e-17

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: 82.43  E-value: 1.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 189 PKSVDWRD----EGYVTPVKNQGSCGSCWAFSSTGALEGQTFKKTGKLIP------LSEQNLVDCSgpQGNQGCGGGWME 258
Cdd:cd02621     2 PKSFDWGDvnngFNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPlgqqpiLSPQHVLSCS--QYSQGCDGGFPF 79

                          90       100
                  ....*....|....*....|....
gi 2096748026 259 NAFLYVhENNGIDSETGYPYTGQV 282
Cdd:cd02621    80 LVGKFA-EDFGIVTEDYFPYTADD 102
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 101-159 2.32e-17

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: 76.51  E-value: 2.32e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  101 WEKWKVLHQKQYTENEEGVRRM-VWEKNFRFIENHNLEYslgKHSFNLKMNHFGDMTLEE 159
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFaIFKENLKKIEEHNKKY---EHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
 101-160 2.72e-16

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: 73.45  E-value: 2.72e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2096748026 101 WEKWKVLHQKQY-TENEEGVRRMVWEKNFRFIENHNleySLGKHSFNLKMNHFGDMTLEEF 160
Cdd:pfam08246   1 FDDWMKKYGKSYrSEEEELYRFQIFKENLKRIEEHN---SNGNVTYKLGLNKFADLTDEEF 58
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
 494-693 4.18e-16

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 82.31  E-value: 4.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 494 VKDQGQCGSCWAFSTTGVLE-----GQVFNKTGKLIS-----LSEQYLMDCtqSVGNRGCNGGFKVRALLFIKEHGINSE 563
Cdd:PTZ00049  400 VTNQLLCGSCYIASQMYAFKrrieiALTKNLDKKYLNnfddlLSIQTVLSC--SFYDQGCNGGFPYLVSKMAKLQGIPLD 477

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 564 ESYPYTAKDGDCKSNKKDTVATCKGVT--------IIPKNSEADLAAA-------------------------------- 603
Cdd:PTZ00049  478 KVFPYTATEQTCPYQVDQSANSMNGSAnlrqinavFFSSETQSDMHADfeapisseparwyakdynyiggcygcnqcnge 557

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 604 ------VATVGPISVSIDAEhRSFMLYKSGIFY---EPHCSSVNLD-----------------HEVLAVGYGTE--NQKP 655
Cdd:PTZ00049  558 kimmneIYRNGPIVASFEAS-PDFYDYADGVYYvedFPHARRCTVDlpkhngvynitgwekvnHAIVLVGWGEEeiNGKL 636

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2096748026 656 --YWIVKNSWGTSWGNEGYVHMAKDMdNNCGIATTAVYPE 693
Cdd:PTZ00049  637 ykYWIGRNSWGKNWGKEGYFKIIRGK-NFSGIESQSLFIE 675
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
 188-278 7.46e-16

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: 77.45  E-value: 7.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 188 IPKSVDWRD---EGYVTPVKNQ---GSCGSCWAFSSTGALEGQTF---KKTGKLIPLSEQNLVDCSGpQGNqgCGGGWME 258
Cdd:cd02698     1 LPKSWDWRNvngVNYVSPTRNQhipQYCGSCWAHGSTSALADRINiarKGAWPSVYLSVQVVIDCAG-GGS--CHGGDPG 77

                          90       100
                  ....*....|....*....|
gi 2096748026 259 NAFLYVHEnNGIDSETGYPY 278
Cdd:cd02698    78 GVYEYAHK-HGIPDETCNPY 96
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 479-690 3.87e-15

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 78.78  E-value: 3.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 479 LPAAVDWRPKG---YVTPVKDQG---QCGSCWAFSTTGVLEGQVF---NKTGKL---ISLSEQYLMDCTQSvgNRGCNGG 546
Cdd:PTZ00364  205 PPAAWSWGDVGgasFLPAAPPASpgrGCNSSYVEAALAAMMARVMvasNRTDPLgqqTFLSARHVLDCSQY--GQGCAGG 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 547 FKVRALLFIKEHGINSEESY--PYTAKDG---DCKSNKKD-----TVATCKGVTIIPKNSEADLAAAVATVGPISVSIDA 616
Cdd:PTZ00364  283 FPEEVGKFAETFGILTTDSYyiPYDSGDGverACKTRRPSrryyfTNYGPLGGYYGAVTDPDEIIWEIYRHGPVPASVYA 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 617 EHRsfmLYKSGIFYEP--------------------HCSSVNLDHEVLAVGYGT-ENQKPYWIVKNSWGT--SWGNEGYV 673
Cdd:PTZ00364  363 NSD---WYNCDENSTEdvryvslddystasadrplrHYFASNVNHTVLIIGWGTdENGGDYWLVLDPWGSrrSWCDGGTR 439

                         250
                  ....*....|....*..
gi 2096748026 674 HMAKDMdNNCGIATTAV 690
Cdd:PTZ00364  440 KIARGV-NAYNIESEVV 455
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
 189-279 1.17e-14

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: 73.84  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 189 PKSVDWRDE--GYVT--PVKNQGSCGSCWAFSSTGALE-------GQTFKktgklIPLSEQNLVDCSGPQGNqGCGGGWM 257
Cdd:cd02620     1 PESFDAREKwpNCISigEIRDQGNCGSCWAFSAVEAFSdrlciqsNGKEN-----VLLSAQDLLSCCSGCGD-GCNGGYP 74

                          90       100
                  ....*....|....*....|..
gi 2096748026 258 ENAFLYVHeNNGIDSETGYPYT 279
Cdd:cd02620    75 DAAWKYLT-TTGVVTGGCQPYT 95
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
 494-672 2.65e-11

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 67.01  E-value: 2.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  494 VKDQGQCGSCWAFSTTGVLEGQVFNKTGKLISLSEQYLMDCTQSVGNRGCN-GGFKVRALLFIKEHGINSEES---YPYT 569
Cdd:PTZ00462   547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCSKGEHKDRCDeGSNPLEFLQIIEDNGFLPADSnylYNYT 626

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026  570 AKDGDCKSNKKDTVATCKGVTIIPKNS--------------EAD------------LAAAVATVGPISVSIDAEHrsFML 623
Cdd:PTZ00462   627 KVGEDCPDEEDHWMNLLDHGKILNHNKkepnsldgkayrayESEhfhdkmdafikiIKDEIMNKGSVIAYIKAEN--VLG 704

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2096748026  624 YK-SGIFYEPHCSSVNLDHEVLAVGYGT-----ENQKPYWIVKNSWGTSWGNEGY 672
Cdd:PTZ00462   705 YEfNGKKVQNLCGDDTADHAVNIVGYGNyindeDEKKSYWIVRNSWGKYWGDEGY 759
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
 189-279 2.40e-06

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 50.66  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 189 PKSVDWRDEG---YVTPVKNQG---SCGSCWAFSSTGALEGQTFKKTGKLIP------LSEQNLVDCSgpQGNQGCGGGW 256
Cdd:PTZ00364  206 PAAWSWGDVGgasFLPAAPPASpgrGCNSSYVEAALAAMMARVMVASNRTDPlgqqtfLSARHVLDCS--QYGQGCAGGF 283

                          90       100
                  ....*....|....*....|....*
gi 2096748026 257 MENAFLYVhENNGIDSETGY--PYT 279
Cdd:PTZ00364  284 PEEVGKFA-ETFGILTTDSYyiPYD 307
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
 184-256 1.49e-04

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 44.94  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2096748026 184 ELAEIPKSVDWRD----EGYVTPVKNQGSCGSCWAFSSTGALE-----GQTFKKTGKLIP-----LSEQNLVDCSGPqgN 249
Cdd:PTZ00049  377 EIDELPKNFTWGDpfnnNTREYDVTNQLLCGSCYIASQMYAFKrrieiALTKNLDKKYLNnfddlLSIQTVLSCSFY--D 454


                  ....*..
gi 2096748026 250 QGCGGGW 256
Cdd:PTZ00049  455 QGCNGGF 461
 
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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