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Conserved domains on  [gi|1705630|sp|P00787|]
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RecName: Full=Cathepsin B; AltName: Full=Cathepsin B1; AltName: Full=RSG-2; Contains: RecName: Full=Cathepsin B light chain; Contains: RecName: Full=Cathepsin B heavy chain; Flags: Precursor

Protein Classification

cathepsin B family cysteine peptidase( domain architecture ID 10547727)

cathepsin B family cysteine peptidase belongs to the larger C1 peptidase family (also called papain family), and is a papain-like cysteine peptidase that catalyzes the hydrolysis of peptide bonds in substrates using a catalytic dyad of Cys and His residues

CATH:  3.90.70.10
EC:  3.4.22.-
Gene Ontology:  GO:0008234|GO:0006508
MEROPS:  C1
PubMed:  12887050|11517925
SCOP:  4000859

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
81-328 5.47e-149

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: 418.60  E-value: 5.47e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   81 PESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIqCGDGCNGGYPSGAWN 160
Cdd:cd02620   1 PESFDAREKWPNCISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSG-CGDGCNGGYPDAAWK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  161 FWTRKGLVSGGvynshigCLPYTIPPCEHHVNGSRPPCTGEGDTPKCNKmceaGYSTSYKEDKHYGYTSYSVSDSEKEIM 240
Cdd:cd02620  80 YLTTTGVVTGG-------CQPYTIPPCGHHPEGPPPCCGTPYCTPKCQD----GCEKTYEEDKHKGKSAYSVPSDETDIM 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  241 AEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHCG 320
Cdd:cd02620 149 KEIMTNGPVQAAFTVYEDFLYYKSGVYQHTSGKQLGGHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNECG 228

                ....*...
gi 1705630  321 IESEIVAG 328
Cdd:cd02620 229 IESEVVAG 236
Propeptide_C1 pfam08127
Peptidase family C1 propeptide; This motif is found at the N terminal of some members of the ...
26-65 6.26e-19

Peptidase family C1 propeptide; This motif is found at the N terminal of some members of the Peptidase_C1 family (pfam00112) and is involved in activation of this peptidase.


:

Pssm-ID: 462365  Cd Length: 40  Bit Score: 78.74  E-value: 6.26e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1705630     26 LSDDMINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGG 65
Cdd:pfam08127   1 LSDEFIDYINSKNTTWKAGRNFHNTTLSYIKRLLGVKPDP 40
 
Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
81-328 5.47e-149

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: 418.60  E-value: 5.47e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   81 PESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIqCGDGCNGGYPSGAWN 160
Cdd:cd02620   1 PESFDAREKWPNCISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSG-CGDGCNGGYPDAAWK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  161 FWTRKGLVSGGvynshigCLPYTIPPCEHHVNGSRPPCTGEGDTPKCNKmceaGYSTSYKEDKHYGYTSYSVSDSEKEIM 240
Cdd:cd02620  80 YLTTTGVVTGG-------CQPYTIPPCGHHPEGPPPCCGTPYCTPKCQD----GCEKTYEEDKHKGKSAYSVPSDETDIM 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  241 AEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHCG 320
Cdd:cd02620 149 KEIMTNGPVQAAFTVYEDFLYYKSGVYQHTSGKQLGGHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNECG 228

                ....*...
gi 1705630  321 IESEIVAG 328
Cdd:cd02620 229 IESEVVAG 236
Peptidase_C1 pfam00112
Papain family cysteine protease;
80-329 6.26e-83

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 250.15  E-value: 6.26e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630     80 LPESFDAREQWSncptIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNgrVNVEVSAEDLLTCCGiqCGDGCNGGYPSGAW 159
Cdd:pfam00112   1 LPESFDWREKGA----VTPVKDQGQCGSCWAFSAVGALEGRYCIKTG--KLVSLSEQQLVDCDT--FNNGCNGGLPDNAF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    160 NFWTR-KGLVSGGVYnshigclPYTippcehhvngsrppctgeGDTPKCNKmceAGYSTSYKEDKHYGYTSYsvsDSEKE 238
Cdd:pfam00112  73 EYIKKnGGIVTESDY-------PYT------------------AKDGTCKF---KKSNSKVAKIKGYGDVPY---NDEEA 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    239 IMAEIYKNGPVEGAFTVFS-DFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGEN 317
Cdd:pfam00112 122 LQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVN 201
                         250
                  ....*....|...
gi 1705630    318 -HCGIESEIVAGI 329
Cdd:pfam00112 202 nECGIASEASYPI 214
Pept_C1 smart00645
Papain family cysteine protease;
80-329 7.85e-57

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 182.01  E-value: 7.85e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630      80 LPESFDAREQWSNCPtiaqIRDQGSCGSCWAFGAVEAMSDRICIHTNGrvNVEVSAEDLLTCCGiQCGDGCNGGYPSGAW 159
Cdd:smart00645   1 LPESFDWRKKGAVTP----VKDQGQCGSCWAFSATGALEGRYCIKTGK--LVSLSEQQLVDCSG-GGNCGCNGGLPDNAF 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630     160 NFWTRKGLVSGGvynshiGCLPYTIppcehhvngsrppctgegdtpkcnkmceagystsykedkhygytsysvsdsekei 239
Cdd:smart00645  74 EYIKKNGGLETE------SCYPYTG------------------------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630     240 maeiykngpveGAFTVFSDFLTYKSGVYKH-EAGDVMGGHAIRILGWG--IENGVPYWLVANSWNVDWGDNGFFKILRGE 316
Cdd:smart00645  93 -----------SVAIDASDFQFYKSGIYDHpGCGSGTLDHAVLIVGYGteVENGKDYWIVKNSWGTDWGENGYFRIARGK 161
                          250
                   ....*....|....
gi 1705630     317 -NHCGIESEIVAGI 329
Cdd:smart00645 162 nNECGIEASVASYP 175
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
79-324 1.47e-31

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 125.06  E-value: 1.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    79 NLPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTN--------GRVNVEVSAEDLLTCCGIQcgDGC 150
Cdd:PTZ00049 380 ELPKNFTWGDPFNNNTREYDVTNQLLCGSCYIASQMYAFKRRIEIALTknldkkylNNFDDLLSIQTVLSCSFYD--QGC 457
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   151 NGGYPSgawnfwtrkgLVSGGVYNSHI---GCLPY--TIPPCEHHVNGSRPPCTGEGDTPKCNKMCEAGYSTS-YKED-- 222
Cdd:PTZ00049 458 NGGFPY----------LVSKMAKLQGIpldKVFPYtaTEQTCPYQVDQSANSMNGSANLRQINAVFFSSETQSdMHADfe 527
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   223 ------------KHYGYTS--YSVS--DSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVY----------------KHE 270
Cdd:PTZ00049 528 apisseparwyaKDYNYIGgcYGCNqcNGEKIMMNEIYRNGPIVASFEASPDFYDYADGVYyvedfpharrctvdlpKHN 607
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705630   271 AGDVMGG-----HAIRILGWGIE--NGVP--YWLVANSWNVDWGDNGFFKILRGENHCGIESE 324
Cdd:PTZ00049 608 GVYNITGwekvnHAIVLVGWGEEeiNGKLykYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQ 670
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
80-312 7.42e-27

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 109.84  E-value: 7.42e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   80 LPESFDAREQWSncptiaQIRDQGSCGSCWAFGAVEAM-SDRICIHTNGRVNVEVSAEDL---LTCCGIQCGDGCNGGYP 155
Cdd:COG4870   4 LPSSVDLRGYVT------PVKDQGSLGSCWAFATAAALeSYLKKQAGAPGTSLDLSELFLynqARNGDGTEGTDDGGSSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  156 SGAWNFWTRKGLVSggvynshIGCLPYTIppcehhvngsrppctgegdtpkcNKMCEAGYSTSYKEDKHYGYTSY----- 230
Cdd:COG4870  78 RDALKLLRWSGVVP-------ESDWPYDD-----------------------SDFTSQPSAAAYADARNYKIQDYyrlpg 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  231 -SVSDSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGD-VMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNG 308
Cdd:COG4870 128 gGGATDLDAIKQALAEGGPVVFGFYVYESFYNYTGGVYYPTPGDaSLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNG 207

                ....
gi 1705630  309 FFKI 312
Cdd:COG4870 208 YFWI 211
Propeptide_C1 pfam08127
Peptidase family C1 propeptide; This motif is found at the N terminal of some members of the ...
26-65 6.26e-19

Peptidase family C1 propeptide; This motif is found at the N terminal of some members of the Peptidase_C1 family (pfam00112) and is involved in activation of this peptidase.


Pssm-ID: 462365  Cd Length: 40  Bit Score: 78.74  E-value: 6.26e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1705630     26 LSDDMINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGG 65
Cdd:pfam08127   1 LSDEFIDYINSKNTTWKAGRNFHNTTLSYIKRLLGVKPDP 40
 
Name Accession Description Interval E-value
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
81-328 5.47e-149

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: 418.60  E-value: 5.47e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   81 PESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIqCGDGCNGGYPSGAWN 160
Cdd:cd02620   1 PESFDAREKWPNCISIGEIRDQGNCGSCWAFSAVEAFSDRLCIQSNGKENVLLSAQDLLSCCSG-CGDGCNGGYPDAAWK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  161 FWTRKGLVSGGvynshigCLPYTIPPCEHHVNGSRPPCTGEGDTPKCNKmceaGYSTSYKEDKHYGYTSYSVSDSEKEIM 240
Cdd:cd02620  80 YLTTTGVVTGG-------CQPYTIPPCGHHPEGPPPCCGTPYCTPKCQD----GCEKTYEEDKHKGKSAYSVPSDETDIM 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  241 AEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHCG 320
Cdd:cd02620 149 KEIMTNGPVQAAFTVYEDFLYYKSGVYQHTSGKQLGGHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNECG 228

                ....*...
gi 1705630  321 IESEIVAG 328
Cdd:cd02620 229 IESEVVAG 236
Peptidase_C1 pfam00112
Papain family cysteine protease;
80-329 6.26e-83

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 250.15  E-value: 6.26e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630     80 LPESFDAREQWSncptIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNgrVNVEVSAEDLLTCCGiqCGDGCNGGYPSGAW 159
Cdd:pfam00112   1 LPESFDWREKGA----VTPVKDQGQCGSCWAFSAVGALEGRYCIKTG--KLVSLSEQQLVDCDT--FNNGCNGGLPDNAF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    160 NFWTR-KGLVSGGVYnshigclPYTippcehhvngsrppctgeGDTPKCNKmceAGYSTSYKEDKHYGYTSYsvsDSEKE 238
Cdd:pfam00112  73 EYIKKnGGIVTESDY-------PYT------------------AKDGTCKF---KKSNSKVAKIKGYGDVPY---NDEEA 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    239 IMAEIYKNGPVEGAFTVFS-DFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGEN 317
Cdd:pfam00112 122 LQAALAKNGPVSVAIDAYErDFQLYKSGVYKHTECGGELNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVN 201
                         250
                  ....*....|...
gi 1705630    318 -HCGIESEIVAGI 329
Cdd:pfam00112 202 nECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
81-324 5.70e-60

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: 191.30  E-value: 5.70e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   81 PESFDAREQWsncpTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNgrVNVEVSAEDLLTCCGiQCGDGCNGGYPSGAWN 160
Cdd:cd02248   1 PESVDWREKG----AVTPVKDQGSCGSCWAFSTVGALEGAYAIKTG--KLVSLSEQQLVDCST-SGNNGCNGGNPDNAFE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  161 FWTRKGLVSGGVYnshigclPYTippcehhvngsrppctgeGDTPKCNkmceagYSTSYKEDKHYGYTSYSVSDsEKEIM 240
Cdd:cd02248  74 YVKNGGLASESDY-------PYT------------------GKDGTCK------YNSSKVGAKITGYSNVPPGD-EEALK 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  241 AEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGG-HAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHC 319
Cdd:cd02248 122 AALANYGPVSVAIDASSSFQFYKGGIYSGPCCSNTNLnHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGSNLC 201

                ....*
gi 1705630  320 GIESE 324
Cdd:cd02248 202 GIASY 206
Pept_C1 smart00645
Papain family cysteine protease;
80-329 7.85e-57

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 182.01  E-value: 7.85e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630      80 LPESFDAREQWSNCPtiaqIRDQGSCGSCWAFGAVEAMSDRICIHTNGrvNVEVSAEDLLTCCGiQCGDGCNGGYPSGAW 159
Cdd:smart00645   1 LPESFDWRKKGAVTP----VKDQGQCGSCWAFSATGALEGRYCIKTGK--LVSLSEQQLVDCSG-GGNCGCNGGLPDNAF 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630     160 NFWTRKGLVSGGvynshiGCLPYTIppcehhvngsrppctgegdtpkcnkmceagystsykedkhygytsysvsdsekei 239
Cdd:smart00645  74 EYIKKNGGLETE------SCYPYTG------------------------------------------------------- 92
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630     240 maeiykngpveGAFTVFSDFLTYKSGVYKH-EAGDVMGGHAIRILGWG--IENGVPYWLVANSWNVDWGDNGFFKILRGE 316
Cdd:smart00645  93 -----------SVAIDASDFQFYKSGIYDHpGCGSGTLDHAVLIVGYGteVENGKDYWIVKNSWGTDWGENGYFRIARGK 161
                          250
                   ....*....|....
gi 1705630     317 -NHCGIESEIVAGI 329
Cdd:smart00645 162 nNECGIEASVASYP 175
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
80-330 7.46e-47

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: 158.70  E-value: 7.46e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   80 LPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVE----VSAEDLLTCCgiQCGDGCNGGYP 155
Cdd:cd02621   1 LPKSFDWGDVNNGFNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPLGqqpiLSPQHVLSCS--QYSQGCDGGFP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  156 SGAWNFWTRKGLVSGGvynshigCLPYTippcehhvNGSRPPCTgegdTPKCNkmCEAGYSTSYkedkHY-GYTsYSVSD 234
Cdd:cd02621  79 FLVGKFAEDFGIVTED-------YFPYT--------ADDDRPCK----ASPSE--CRRYYFSDY----NYvGGC-YGCTN 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  235 sEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGG-------------HAIRILGWG--IENGVPYWLVANS 299
Cdd:cd02621 133 -EDEMKWEIYRNGPIVVAFEVYSDFDFYKEGVYHHTDNDEVSDgdndnfnpfeltnHAVLLVGWGedEIKGEKYWIVKNS 211
                       250       260       270
                ....*....|....*....|....*....|.
gi 1705630  300 WNVDWGDNGFFKILRGENHCGIESEIVAGIP 330
Cdd:cd02621 212 WGSSWGEKGYFKIRRGTNECGIESQAVFAYP 242
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
80-315 3.71e-39

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: 138.70  E-value: 3.71e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   80 LPESFDAREQwSNCPTIAQIRDQ---GSCGSCWAFGAVEAMSDRICIHTNGR-VNVEVSAEDLLTCCGiqcGDGCNGGYP 155
Cdd:cd02698   1 LPKSWDWRNV-NGVNYVSPTRNQhipQYCGSCWAHGSTSALADRINIARKGAwPSVYLSVQVVIDCAG---GGSCHGGDP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  156 SGAWNFWTRKGLVsggvynsHIGCLPYtippcehhvNGSRPPCTGEGDTPKCNKMceaGYSTSYKEdkhygYTSYSVSD- 234
Cdd:cd02698  77 GGVYEYAHKHGIP-------DETCNPY---------QAKDGECNPFNRCGTCNPF---GECFAIKN-----YTLYFVSDy 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  235 ----SEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGI-ENGVPYWLVANSWNVDWGDNGF 309
Cdd:cd02698 133 gsvsGRDKMMAEIYARGPISCGIMATEALENYTGGVYKEYVQDPLINHIISVAGWGVdENGVEYWIVRNSWGEPWGERGW 212

                ....*.
gi 1705630  310 FKILRG 315
Cdd:cd02698 213 FRIVTS 218
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
83-312 7.35e-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: 129.56  E-value: 7.35e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   83 SFDAREQWsncptIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQC---GDGCNGGYPSGAW 159
Cdd:cd02619   1 SVDLRPLR-----LTPVKNQGSRGSCWAFASAYALESAYRIKGGEDEYVDLSPQYLYICANDEClgiNGSCDGGGPLSAL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  160 -NFWTRKGLVSGGVYnshigclPYTIPPCEHHVNGSRPpctgegdtPKCNKMCEAGYSTSYKEDkhygytsysvsdsEKE 238
Cdd:cd02619  76 lKLVALKGIPPEEDY-------PYGAESDGEEPKSEAA--------LNAAKVKLKDYRRVLKNN-------------IED 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  239 IMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEA------GDVMGGHAIRILGWGIEN--GVPYWLVANSWNVDWGDNGFF 310
Cdd:cd02619 128 IKEALAKGGPVVAGFDVYSGFDRLKEGIIYEEIvyllyeDGDLGGHAVVIVGYDDNYveGKGAFIVKNSWGTDWGDNGYG 207

                ..
gi 1705630  311 KI 312
Cdd:cd02619 208 RI 209
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
79-324 1.47e-31

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 125.06  E-value: 1.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    79 NLPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTN--------GRVNVEVSAEDLLTCCGIQcgDGC 150
Cdd:PTZ00049 380 ELPKNFTWGDPFNNNTREYDVTNQLLCGSCYIASQMYAFKRRIEIALTknldkkylNNFDDLLSIQTVLSCSFYD--QGC 457
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   151 NGGYPSgawnfwtrkgLVSGGVYNSHI---GCLPY--TIPPCEHHVNGSRPPCTGEGDTPKCNKMCEAGYSTS-YKED-- 222
Cdd:PTZ00049 458 NGGFPY----------LVSKMAKLQGIpldKVFPYtaTEQTCPYQVDQSANSMNGSANLRQINAVFFSSETQSdMHADfe 527
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   223 ------------KHYGYTS--YSVS--DSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVY----------------KHE 270
Cdd:PTZ00049 528 apisseparwyaKDYNYIGgcYGCNqcNGEKIMMNEIYRNGPIVASFEASPDFYDYADGVYyvedfpharrctvdlpKHN 607
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1705630   271 AGDVMGG-----HAIRILGWGIE--NGVP--YWLVANSWNVDWGDNGFFKILRGENHCGIESE 324
Cdd:PTZ00049 608 GVYNITGwekvnHAIVLVGWGEEeiNGKLykYWIGRNSWGKNWGKEGYFKIIRGKNFSGIESQ 670
PTZ00203 PTZ00203
cathepsin L protease; Provisional
81-319 7.71e-30

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 116.72  E-value: 7.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    81 PESFDAREQWSNCPtiaqIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVevSAEDLLTCCGIQcgDGCNGGYPSGAWN 160
Cdd:PTZ00203 127 PDAVDWREKGAVTP----VKNQGACGSCWAFSAVGNIESQWAVAGHKLVRL--SEQQLVSCDHVD--NGCGGGLMLQAFE 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   161 FWTRKglVSGGVYNShigclpytippcehhvnGSRPPCTGEGDTPKCNKMCEAGYSTSYKedkhyGYTSysVSDSEKEIM 240
Cdd:PTZ00203 199 WVLRN--MNGTVFTE-----------------KSYPYVSGNGDVPECSNSSELAPGARID-----GYVS--MESSERVMA 252
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1705630   241 AEIYKNGPVEGAFTVfSDFLTYKSGVYKHEAGDVMGgHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHC 319
Cdd:PTZ00203 253 AWLAKNGPISIAVDA-SSFMSYHSGVLTSCIGEQLN-HGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGVNAC 329
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
80-312 7.42e-27

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 109.84  E-value: 7.42e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   80 LPESFDAREQWSncptiaQIRDQGSCGSCWAFGAVEAM-SDRICIHTNGRVNVEVSAEDL---LTCCGIQCGDGCNGGYP 155
Cdd:COG4870   4 LPSSVDLRGYVT------PVKDQGSLGSCWAFATAAALeSYLKKQAGAPGTSLDLSELFLynqARNGDGTEGTDDGGSSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  156 SGAWNFWTRKGLVSggvynshIGCLPYTIppcehhvngsrppctgegdtpkcNKMCEAGYSTSYKEDKHYGYTSY----- 230
Cdd:COG4870  78 RDALKLLRWSGVVP-------ESDWPYDD-----------------------SDFTSQPSAAAYADARNYKIQDYyrlpg 127
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630  231 -SVSDSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGD-VMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNG 308
Cdd:COG4870 128 gGGATDLDAIKQALAEGGPVVFGFYVYESFYNYTGGVYYPTPGDaSLGGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNG 207

                ....
gi 1705630  309 FFKI 312
Cdd:COG4870 208 YFWI 211
PTZ00200 PTZ00200
cysteine proteinase; Provisional
67-321 1.19e-25

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 106.70  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    67 NLPERVGFSEDINLP-----ESFDareqWSNCPTIAQIRDQGS-CGSCWAFGAVEAMSDRICIHTNgrVNVEVSAEDLLT 140
Cdd:PTZ00200 216 NLKKAKNTDEDVKDPskitgEGLD----WRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRD--KSVDLSEQELVN 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   141 C---CGiqcgdGCNGGYPSGAWNFWTRKGLVSGGVYnshigclPYTippcehhvnGSRPPCtgegdtpkcnkmceagyst 217
Cdd:PTZ00200 290 CdtkSQ-----GCSGGYPDTALEYVKNKGLSSSSDV-------PYL---------AKDGKC------------------- 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   218 SYKEDKHYGYTSYSVSdSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGgHAIRILGWGI--ENGVPYWL 295
Cdd:PTZ00200 330 VVSSTKKVYIDSYLVA-KGKDVLNKSLVISPTVVYIAVSRELLKYKSGVYNGECGKSLN-HAVLLVGEGYdeKTKKRYWI 407
                        250       260
                 ....*....|....*....|....*....
gi 1705630   296 VANSWNVDWGDNGFFKILR---GENHCGI 321
Cdd:PTZ00200 408 IKNSWGTDWGENGYMRLERtneGTDKCGI 436
PTZ00021 PTZ00021
falcipain-2; Provisional
35-324 2.88e-21

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 94.07  E-value: 2.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    35 NKQNTTWQAGRNFYNvDISY--------------LKKLcgtvlgGPNLPERVGFSEDIN----LPESFD-AREQWSNCPT 95
Cdd:PTZ00021 205 NKENVLYKKGMNRFG-DLSFeefkkkyltlksfdFKSN------GKKSPRVINYDDVIKkykpKDATFDhAKYDWRLHNG 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    96 IAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVevsAEDLLTCCGIQcGDGCNGGYPSGAW-NFWTRKGLVSGGVYn 174
Cdd:PTZ00021 278 VTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSL---SEQELVDCSFK-NNGCYGGLIPNAFeDMIELGGLCSEDDY- 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   175 shigclPYTippcehhvngsrppctgeGDTP-KCN-KMCeagystsykeDKHYGYTSYsVSDSEKEIMAEIYKNGPVEGA 252
Cdd:PTZ00021 353 ------PYV------------------SDTPeLCNiDRC----------KEKYKIKSY-VSIPEDKFKEAIRFLGPISVS 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   253 FTVFSDFLTYKSGVYKHEAGDVMgGHAIRILGWGIENGVP----------YWLVANSWNVDWGDNGFFKILRGEN----H 318
Cdd:PTZ00021 398 IAVSDDFAFYKGGIFDGECGEEP-NHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGFIRIETDENglmkT 476

                 ....*.
gi 1705630   319 CGIESE 324
Cdd:PTZ00021 477 CSLGTE 482
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
101-326 4.46e-19

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 88.02  E-value: 4.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   101 DQG---SCGSCWAFGAVEAMSDRICIHTN-----GRVNVeVSAEDLLTCCgiQCGDGCNGGYPSGAWNFWTRKGLVSGGV 172
Cdd:PTZ00364 225 PASpgrGCNSSYVEAALAAMMARVMVASNrtdplGQQTF-LSARHVLDCS--QYGQGCAGGFPEEVGKFAETFGILTTDS 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   173 YNshigcLPYTippcehhvngsrppcTGEGDTpKCNKMCEAG---YSTSYKEDKHYgytsYSVSDSEKEIMAEIYKNGPV 249
Cdd:PTZ00364 302 YY-----IPYD---------------SGDGVE-RACKTRRPSrryYFTNYGPLGGY----YGAVTDPDEIIWEIYRHGPV 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630   250 EGAFTVFSDFLTYKSGVYK---------HE------------AGDVmgGHAIRILGWGI-ENGVPYWLVANSW--NVDWG 305
Cdd:PTZ00364 357 PASVYANSDWYNCDENSTEdvryvslddYStasadrplrhyfASNV--NHTVLIIGWGTdENGGDYWLVLDPWgsRRSWC 434
                        250       260
                 ....*....|....*....|.
gi 1705630   306 DNGFFKILRGENHCGIESEIV 326
Cdd:PTZ00364 435 DGGTRKIARGVNAYNIESEVV 455
Propeptide_C1 pfam08127
Peptidase family C1 propeptide; This motif is found at the N terminal of some members of the ...
26-65 6.26e-19

Peptidase family C1 propeptide; This motif is found at the N terminal of some members of the Peptidase_C1 family (pfam00112) and is involved in activation of this peptidase.


Pssm-ID: 462365  Cd Length: 40  Bit Score: 78.74  E-value: 6.26e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1705630     26 LSDDMINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGG 65
Cdd:pfam08127   1 LSDEFIDYINSKNTTWKAGRNFHNTTLSYIKRLLGVKPDP 40
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
91-319 2.86e-07

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 52.37  E-value: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630     91 SNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIhtNGRVNVEVSAEDLLTCCGIQCGDGCN-GGYPSGAWNFWTRKGLV- 168
Cdd:PTZ00462  539 NNCISKIQIEDQGNCAISWIFASKYHLETIKCM--KGYEPHAISALYIANCSKGEHKDRCDeGSNPLEFLQIIEDNGFLp 616
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    169 --SGGVYN-SHIG--ClpytiPPCEHH-VNgsrppCTGEGDTPKCNKMCEAGYSTSykedkhyGYTSYsvsDSE------ 236
Cdd:PTZ00462  617 adSNYLYNyTKVGedC-----PDEEDHwMN-----LLDHGKILNHNKKEPNSLDGK-------AYRAY---ESEhfhdkm 676
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1705630    237 ----KEIMAEIYKNGPVEgAFTVFSDFLTYK-SGV-YKHEAGDVMGGHAIRILGWGieNGV-------PYWLVANSWNVD 303
Cdd:PTZ00462  677 dafiKIIKDEIMNKGSVI-AYIKAENVLGYEfNGKkVQNLCGDDTADHAVNIVGYG--NYIndedekkSYWIVRNSWGKY 753
                         250
                  ....*....|....*..
gi 1705630    304 WGDNGFFKI-LRGENHC 319
Cdd:PTZ00462  754 WGDEGYFKVdMYGPSHC 770
 
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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