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Conserved domains on  [gi|18413507|ref|NP_567377|]
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Papain family cysteine protease [Arabidopsis thaliana]

Protein Classification

C1 family peptidase( domain architecture ID 11276840)

C1 family peptidase (also called papain family protein) 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
SCOP:  4000859

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
144-359 1.61e-112

Papain family cysteine protease;


:

Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 326.81  E-value: 1.61e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   144 LPKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKENNGCGGGKVETAYEFIMNNGG 223
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKKNGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   224 LGTDNDYPYKALNGVCEgRLKEDNKNVMIDGYENLPANDEAALMKAVA-HQPVTAVVDSSSREFQLYESGVFDGT-CGTN 301
Cdd:pfam00112  81 IVTESDYPYTAKDGTCK-FKKSNSKVAKIKGYGDVPYNDEEALQAALAkNGPVSVAIDAYERDFQLYKSGVYKHTeCGGE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18413507   302 LNHGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKMARNIANprgLCGIAMRASYPL 359
Cdd:pfam00112 160 LNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNN---ECGIASEASYPI 214
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
56-111 1.01e-19

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.


:

Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 81.91  E-value: 1.01e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18413507     56 FESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNAEN-LSYRLGLNRFADLSLHE 111
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYeHSYKLGVNQFSDLTPEE 57
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
144-359 1.61e-112

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 326.81  E-value: 1.61e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   144 LPKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKENNGCGGGKVETAYEFIMNNGG 223
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKKNGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   224 LGTDNDYPYKALNGVCEgRLKEDNKNVMIDGYENLPANDEAALMKAVA-HQPVTAVVDSSSREFQLYESGVFDGT-CGTN 301
Cdd:pfam00112  81 IVTESDYPYTAKDGTCK-FKKSNSKVAKIKGYGDVPYNDEEALQAALAkNGPVSVAIDAYERDFQLYKSGVYKHTeCGGE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18413507   302 LNHGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKMARNIANprgLCGIAMRASYPL 359
Cdd:pfam00112 160 LNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNN---ECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
145-358 5.12e-102

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: 299.92  E-value: 5.12e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 145 PKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKE-NNGCGGGKVETAYEfIMNNGG 223
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFE-YVKNGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 224 LGTDNDYPYKALNGVCegRLKEDNKNVMIDGYENLPANDEAALMKAVA-HQPVTAVVDSSSrEFQLYESGVFDGTCG--T 300
Cdd:cd02248  80 LASESDYPYTGKDGTC--KYNSSKVGAKITGYSNVPPGDEEALKAALAnYGPVSVAIDASS-SFQFYKGGIYSGPCCsnT 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18413507 301 NLNHGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKMARNianpRGLCGIAMRASYP 358
Cdd:cd02248 157 NLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARG----SNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
144-358 1.64e-79

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 241.33  E-value: 1.64e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507    144 LPKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKE-NNGCGGGKVETAYEFIMNNG 222
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGgNCGCNGGLPDNAFEYIKKNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507    223 GLGTDNDYPYKAlngvcegrlkednkNVMIDGyenlpandeaalmkavahqpvtavvdsssREFQLYESGVFDGT-CGTN 301
Cdd:smart00645  81 GLETESCYPYTG--------------SVAIDA-----------------------------SDFQFYKSGIYDHPgCGSG 117
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18413507    302 -LNHGVVVVGYGT--ENGRDYWIVKNSRGDTWGEAGYMKMARNIANprgLCGI-AMRASYP 358
Cdd:smart00645 118 tLDHAVLIVGYGTevENGKDYWIVKNSWGTDWGENGYFRIARGKNN---ECGIeASVASYP 175
PTZ00200 PTZ00200
cysteine proteinase; Provisional
51-351 3.83e-72

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 231.51  E-value: 3.83e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   51 EATLMFESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNAENLsYRLGLNRFADLSLHEYGEICHGADPRPPRN---- 126
Cdd:PTZ00200 121 EVYLEFEEFNKKYNRKHATHAERLNRFLTFRNNYLEVKSHKGDEP-YSKEINKFSDLTEEEFRKLFPVIKVPPKSNstsh 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  127 -------HV----FMTSSNRYKTSDGDVL------PKSVDWRNEGAVTEVKDQGL-CRSCWAFSTVGAVEGLNKIVTGEL 188
Cdd:PTZ00200 200 nndfkarHVsnptYLKNLKKAKNTDEDVKdpskitGEGLDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRDKS 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  189 VTLSEQDLINCNKENNGCGGGKVETAYEFIMNNgGLGTDNDYPYKALNGVCegrLKEDNKNVMIDGYENLPANDeaALMK 268
Cdd:PTZ00200 280 VDLSEQELVNCDTKSQGCSGGYPDTALEYVKNK-GLSSSSDVPYLAKDGKC---VVSSTKKVYIDSYLVAKGKD--VLNK 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  269 AVAHQPvTAVVDSSSREFQLYESGVFDGTCGTNLNHGVVVV--GYGTENGRDYWIVKNSRGDTWGEAGYMKMARNiANPR 346
Cdd:PTZ00200 354 SLVISP-TVVYIAVSRELLKYKSGVYNGECGKSLNHAVLLVgeGYDEKTKKRYWIIKNSWGTDWGENGYMRLERT-NEGT 431

                 ....*
gi 18413507  347 GLCGI 351
Cdd:PTZ00200 432 DKCGI 436
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
144-338 9.50e-32

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 124.09  E-value: 9.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 144 LPKSVDWRNegAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVT---LSEQDLIN-----CNKENNGCGGGKVETAY 215
Cdd:COG4870   4 LPSSVDLRG--YVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNqarngDGTEGTDDGGSSLRDAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 216 EFiMNNGGLGTDNDYPYKALNGVCE--GRLKEDNKNVMIDGYENLP----ANDEAALMKAVA-HQPVTAV--VDSSsreF 286
Cdd:COG4870  82 KL-LRWSGVVPESDWPYDDSDFTSQpsAAAYADARNYKIQDYYRLPggggATDLDAIKQALAeGGPVVFGfyVYES---F 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 18413507 287 QLYESGVFDGTCGTNL--NHGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKM 338
Cdd:COG4870 158 YNYTGGVYYPTPGDASlgGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
56-111 1.01e-19

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.


Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 81.91  E-value: 1.01e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18413507     56 FESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNAEN-LSYRLGLNRFADLSLHE 111
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYeHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
56-112 2.65e-18

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: 77.69  E-value: 2.65e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18413507    56 FESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNA-ENLSYRLGLNRFADLSLHEY 112
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSnGNVTYKLGLNKFADLTDEEF 58
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
144-359 1.61e-112

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 326.81  E-value: 1.61e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   144 LPKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKENNGCGGGKVETAYEFIMNNGG 223
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTFNNGCNGGLPDNAFEYIKKNGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   224 LGTDNDYPYKALNGVCEgRLKEDNKNVMIDGYENLPANDEAALMKAVA-HQPVTAVVDSSSREFQLYESGVFDGT-CGTN 301
Cdd:pfam00112  81 IVTESDYPYTAKDGTCK-FKKSNSKVAKIKGYGDVPYNDEEALQAALAkNGPVSVAIDAYERDFQLYKSGVYKHTeCGGE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18413507   302 LNHGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKMARNIANprgLCGIAMRASYPL 359
Cdd:pfam00112 160 LNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNN---ECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
145-358 5.12e-102

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: 299.92  E-value: 5.12e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 145 PKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKE-NNGCGGGKVETAYEfIMNNGG 223
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSgNNGCNGGNPDNAFE-YVKNGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 224 LGTDNDYPYKALNGVCegRLKEDNKNVMIDGYENLPANDEAALMKAVA-HQPVTAVVDSSSrEFQLYESGVFDGTCG--T 300
Cdd:cd02248  80 LASESDYPYTGKDGTC--KYNSSKVGAKITGYSNVPPGDEEALKAALAnYGPVSVAIDASS-SFQFYKGGIYSGPCCsnT 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18413507 301 NLNHGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKMARNianpRGLCGIAMRASYP 358
Cdd:cd02248 157 NLNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARG----SNLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
144-358 1.64e-79

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 241.33  E-value: 1.64e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507    144 LPKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKE-NNGCGGGKVETAYEFIMNNG 222
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGgNCGCNGGLPDNAFEYIKKNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507    223 GLGTDNDYPYKAlngvcegrlkednkNVMIDGyenlpandeaalmkavahqpvtavvdsssREFQLYESGVFDGT-CGTN 301
Cdd:smart00645  81 GLETESCYPYTG--------------SVAIDA-----------------------------SDFQFYKSGIYDHPgCGSG 117
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18413507    302 -LNHGVVVVGYGT--ENGRDYWIVKNSRGDTWGEAGYMKMARNIANprgLCGI-AMRASYP 358
Cdd:smart00645 118 tLDHAVLIVGYGTevENGKDYWIVKNSWGTDWGENGYFRIARGKNN---ECGIeASVASYP 175
PTZ00200 PTZ00200
cysteine proteinase; Provisional
51-351 3.83e-72

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 231.51  E-value: 3.83e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   51 EATLMFESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNAENLsYRLGLNRFADLSLHEYGEICHGADPRPPRN---- 126
Cdd:PTZ00200 121 EVYLEFEEFNKKYNRKHATHAERLNRFLTFRNNYLEVKSHKGDEP-YSKEINKFSDLTEEEFRKLFPVIKVPPKSNstsh 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  127 -------HV----FMTSSNRYKTSDGDVL------PKSVDWRNEGAVTEVKDQGL-CRSCWAFSTVGAVEGLNKIVTGEL 188
Cdd:PTZ00200 200 nndfkarHVsnptYLKNLKKAKNTDEDVKdpskitGEGLDWRRADAVTKVKDQGLnCGSCWAFSSVGSVESLYKIYRDKS 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  189 VTLSEQDLINCNKENNGCGGGKVETAYEFIMNNgGLGTDNDYPYKALNGVCegrLKEDNKNVMIDGYENLPANDeaALMK 268
Cdd:PTZ00200 280 VDLSEQELVNCDTKSQGCSGGYPDTALEYVKNK-GLSSSSDVPYLAKDGKC---VVSSTKKVYIDSYLVAKGKD--VLNK 353
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  269 AVAHQPvTAVVDSSSREFQLYESGVFDGTCGTNLNHGVVVV--GYGTENGRDYWIVKNSRGDTWGEAGYMKMARNiANPR 346
Cdd:PTZ00200 354 SLVISP-TVVYIAVSRELLKYKSGVYNGECGKSLNHAVLLVgeGYDEKTKKRYWIIKNSWGTDWGENGYMRLERT-NEGT 431

                 ....*
gi 18413507  347 GLCGI 351
Cdd:PTZ00200 432 DKCGI 436
PTZ00203 PTZ00203
cathepsin L protease; Provisional
52-342 1.22e-66

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 214.56  E-value: 1.22e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   52 ATLMFESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNAENLSYRLGLNRFADLSLHEYGEICHGADPRPPRNHVFMT 131
Cdd:PTZ00203  34 AAALFEEFKRTYQRAYGTLTEEQQRLANFERNLELMREHQARNPHARFGITKFFDLSEAEFAARYLNGAAYFAAAKQHAG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  132 SSNRYKTSDGDVLPKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKENNGCGGGKV 211
Cdd:PTZ00203 114 QHYRKARADLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHVDNGCGGGLM 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  212 ETAYEFIMNN--GGLGTDNDYPYKALNG-VCEGRLKED-NKNVMIDGYENLPANDEAALMKAVAHQPVTAVVDSSSreFQ 287
Cdd:PTZ00203 194 LQAFEWVLRNmnGTVFTEKSYPYVSGNGdVPECSNSSElAPGARIDGYVSMESSERVMAAWLAKNGPISIAVDASS--FM 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18413507  288 LYESGVFDGTCGTNLNHGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKMARNI 342
Cdd:PTZ00203 272 SYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGV 326
PTZ00021 PTZ00021
falcipain-2; Provisional
56-359 2.25e-65

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 215.02  E-value: 2.25e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   56 FESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNA-ENLSYRLGLNRFADLSLHEYGE---ICHGADPRPPRNHVFMT 131
Cdd:PTZ00021 169 FYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAHNNkENVLYKKGMNRFGDLSFEEFKKkylTLKSFDFKSNGKKSPRV 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  132 SS-----NRYKTSDGDVLPKSVDWRNEGAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNKENNGC 206
Cdd:PTZ00021 249 INyddviKKYKPKDATFDHAKYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSFKNNGC 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  207 GGGKVETAYEFIMNNGGLGTDNDYPYKA-LNGVCEgrLKEDNKNVMIDGYENLPandEAALMKAVAHQPVTAVVDSSSRE 285
Cdd:PTZ00021 329 YGGLIPNAFEDMIELGGLCSEDDYPYVSdTPELCN--IDRCKEKYKIKSYVSIP---EDKFKEAIRFLGPISVSIAVSDD 403
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  286 FQLYESGVFDGTCGTNLNHGVVVVGYGTENGRD----------YWIVKNSRGDTWGEAGYMKMARNIANPRGLCGIAMRA 355
Cdd:PTZ00021 404 FAFYKGGIFDGECGEEPNHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGFIRIETDENGLMKTCSLGTEA 483

                 ....
gi 18413507  356 SYPL 359
Cdd:PTZ00021 484 YVPL 487
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
145-351 2.70e-33

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: 123.92  E-value: 2.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 145 PKSVD----WRNEGAVTEVKDQGLCRSCWAFSTVGA------VEGLNKIvtgeLVTLSEQDLINC-NKENNGCGGGKVET 213
Cdd:cd02620   1 PESFDarekWPNCISIGEIRDQGNCGSCWAFSAVEAfsdrlcIQSNGKE----NVLLSAQDLLSCcSGCGDGCNGGYPDA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 214 AYEFIMNNGgLGTDNDYPY------KALNGVCEGRLKEDNKNVMIDGYE--------------NLPaNDEAALMKAV-AH 272
Cdd:cd02620  77 AWKYLTTTG-VVTGGCQPYtippcgHHPEGPPPCCGTPYCTPKCQDGCEktyeedkhkgksaySVP-SDETDIMKEImTN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 273 QPVTA--VVdssSREFQLYESGVFDGTCGTNLN-HGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKMARNIANprglC 349
Cdd:cd02620 155 GPVQAafTV---YEDFLYYKSGVYQHTSGKQLGgHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILRGSNE----C 227

                ..
gi 18413507 350 GI 351
Cdd:cd02620 228 GI 229
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
144-338 9.50e-32

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 124.09  E-value: 9.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 144 LPKSVDWRNegAVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVT---LSEQDLIN-----CNKENNGCGGGKVETAY 215
Cdd:COG4870   4 LPSSVDLRG--YVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNqarngDGTEGTDDGGSSLRDAL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 216 EFiMNNGGLGTDNDYPYKALNGVCE--GRLKEDNKNVMIDGYENLP----ANDEAALMKAVA-HQPVTAV--VDSSsreF 286
Cdd:COG4870  82 KL-LRWSGVVPESDWPYDDSDFTSQpsAAAYADARNYKIQDYYRLPggggATDLDAIKQALAeGGPVVFGfyVYES---F 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 18413507 287 QLYESGVFDGTCGTNL--NHGVVVVGYGTENGRDYWIVKNSRGDTWGEAGYMKM 338
Cdd:COG4870 158 YNYTGGVYYPTPGDASlgGHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWI 211
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
147-338 2.72e-31

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: 118.00  E-value: 2.72e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 147 SVDWRNEGaVTEVKDQGLCRSCWAFSTVGAVEGLNKIVTG--ELVTLSEQDLIN-----CNKENNGCGGGKVETAYEFIM 219
Cdd:cd02619   1 SVDLRPLR-LTPVKNQGSRGSCWAFASAYALESAYRIKGGedEYVDLSPQYLYIcandeCLGINGSCDGGGPLSALLKLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 220 NNGGLGTDNDYPYKALNGVCEGR--LKEDNKNVMIDGYENLPANDEAALMKAVA-HQPVTAVVDSSSR-----EFQLYES 291
Cdd:cd02619  80 ALKGIPPEEDYPYGAESDGEEPKseAALNAAKVKLKDYRRVLKNNIEDIKEALAkGGPVVAGFDVYSGfdrlkEGIIYEE 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18413507 292 GVFDGTCGTNL-NHGVVVVGYGTEN--GRDYWIVKNSRGDTWGEAGYMKM 338
Cdd:cd02619 160 IVYLLYEDGDLgGHAVVIVGYDDNYveGKGAFIVKNSWGTDWGDNGYGRI 209
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
144-342 4.78e-30

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: 115.20  E-value: 4.78e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 144 LPKSVDWRNEGAV---TEVKDQGL---CRSCWAFSTVGAVEGLNKI---VTGELVTLSEQDLINCNKENNgCGGGKVETA 214
Cdd:cd02698   1 LPKSWDWRNVNGVnyvSPTRNQHIpqyCGSCWAHGSTSALADRINIarkGAWPSVYLSVQVVIDCAGGGS-CHGGDPGGV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 215 YEFIMNNGgLGTDNDYPYKALNGVCE-----GRLKEDNKNVMIDGYENLPAND------EAALMKAVAHQ-PVTAVVDSS 282
Cdd:cd02698  80 YEYAHKHG-IPDETCNPYQAKDGECNpfnrcGTCNPFGECFAIKNYTLYFVSDygsvsgRDKMMAEIYARgPISCGIMAT 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18413507 283 SREFQlYESGVFDGTCGTNL-NHGVVVVGYGT-ENGRDYWIVKNSRGDTWGEAGYMKMARNI 342
Cdd:cd02698 159 EALEN-YTGGVYKEYVQDPLiNHIISVAGWGVdENGVEYWIVRNSWGEPWGERGWFRIVTSS 219
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
144-351 4.26e-29

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: 112.86  E-value: 4.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 144 LPKSVDWRNEGA----VTEVKDQGLCRSCWAFSTVGAVEGLNKIVT------GELVTLSEQDLINCNKENNGCGGGKVET 213
Cdd:cd02621   1 LPKSFDWGDVNNgfnyVSPVRNQGGCGSCYAFASVYALEARIMIASnktdplGQQPILSPQHVLSCSQYSQGCDGGFPFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 214 ----AYEFimnngGLGTDNDYPYKALN-GVCEGRLKEDNKNVMIDGYE--NLPANDEAALMK--AVAHQPVTAVVDSSSr 284
Cdd:cd02621  81 vgkfAEDF-----GIVTEDYFPYTADDdRPCKASPSECRRYYFSDYNYvgGCYGCTNEDEMKweIYRNGPIVVAFEVYS- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507 285 EFQLYESGVFDGTCGTN--------------LNHGVVVVGYGTE--NGRDYWIVKNSRGDTWGEAGYMKMARNIanprGL 348
Cdd:cd02621 155 DFDFYKEGVYHHTDNDEvsdgdndnfnpfelTNHAVLLVGWGEDeiKGEKYWIVKNSWGSSWGEKGYFKIRRGT----NE 230

                ...
gi 18413507 349 CGI 351
Cdd:cd02621 231 CGI 233
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
56-111 1.01e-19

Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 peptidases such as Cathepsin L where it acts as a propeptide. There are also a number of proteins that are composed solely of multiple copies of this domain such as the peptidase inhibitor salarin. This family is classified as I29 by MEROPS. Peptide proteinase inhibitors can be found as single domain proteins or as single or multiple domains within proteins; these are referred to as either simple or compound inhibitors, respectively. In many cases they are synthesised as part of a larger precursor protein, either as a prepropeptide or as an N-terminal domain associated with an inactive peptidase or zymogen. This domain prevents access of the substrate to the active site. Removal of the N-terminal inhibitor domain either by interaction with a second peptidase or by autocatalytic cleavage activates the zymogen. Other inhibitors interact direct with proteinases using a simple noncovalent lock and key mechanism; while yet others use a conformational change-based trapping mechanism that depends on their structural and thermodynamic properties.


Pssm-ID: 214853 [Multi-domain]  Cd Length: 57  Bit Score: 81.91  E-value: 1.01e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18413507     56 FESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNAEN-LSYRLGLNRFADLSLHE 111
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNKKYeHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
56-112 2.65e-18

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: 77.69  E-value: 2.65e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18413507    56 FESWMVKHGKVYDSVAEKERRLTIFEDNLRFITNRNA-ENLSYRLGLNRFADLSLHEY 112
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSnGNVTYKLGLNKFADLTDEEF 58
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
141-342 7.33e-16

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 78.78  E-value: 7.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  141 GDVLPKSVDWRNEGAVT---EVKDQG---LCRSCWAFSTVGAVEGLNKIVT------GELVTLSEQDLINCNKENNGCGG 208
Cdd:PTZ00364 202 GDPPPAAWSWGDVGGASflpAAPPASpgrGCNSSYVEAALAAMMARVMVASnrtdplGQQTFLSARHVLDCSQYGQGCAG 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  209 GKVETAYEFIMNNGGLGTDNDY-PYKALNGV---CEGRLKED----NKNVMIDGYENLPANDEAALMKAVAHQPVTAVV- 279
Cdd:PTZ00364 282 GFPEEVGKFAETFGILTTDSYYiPYDSGDGVeraCKTRRPSRryyfTNYGPLGGYYGAVTDPDEIIWEIYRHGPVPASVy 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  280 --------DSSSREFQLYESGVFDGTCGTN----------LNHGVVVVGYGT-ENGRDYWIVKNSRG--DTWGEAGYMKM 338
Cdd:PTZ00364 362 ansdwyncDENSTEDVRYVSLDDYSTASADrplrhyfasnVNHTVLIIGWGTdENGGDYWLVLDPWGsrRSWCDGGTRKI 441

                 ....
gi 18413507  339 ARNI 342
Cdd:PTZ00364 442 ARGV 445
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
142-340 1.01e-11

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 66.13  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  142 DVLPKSVDW----RNEGAVTEVKDQGLCRSCWAFSTVGAVE-----GLNKIVTGELVT-----LSEQDLINCNKENNGCG 207
Cdd:PTZ00049 379 DELPKNFTWgdpfNNNTREYDVTNQLLCGSCYIASQMYAFKrrieiALTKNLDKKYLNnfddlLSIQTVLSCSFYDQGCN 458
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  208 GGkvetaYEFIMNN----GGLGTDNDYPYKALNGVC-----------------------------EGRLKEDNKNVMIDG 254
Cdd:PTZ00049 459 GG-----FPYLVSKmaklQGIPLDKVFPYTATEQTCpyqvdqsansmngsanlrqinavffssetQSDMHADFEAPISSE 533
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507  255 YENLPAND---------------EAALMKAVAHQ-PVTAVVDSSSrEFQLYESGVFDGT-------CGTNL--------- 302
Cdd:PTZ00049 534 PARWYAKDynyiggcygcnqcngEKIMMNEIYRNgPIVASFEASP-DFYDYADGVYYVEdfpharrCTVDLpkhngvyni 612
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 18413507  303 ------NHGVVVVGYGTE--NGR--DYWIVKNSRGDTWGEAGYMKMAR 340
Cdd:PTZ00049 613 tgwekvNHAIVLVGWGEEeiNGKlyKYWIGRNSWGKNWGKEGYFKIIR 660
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
158-338 9.98e-08

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 53.91  E-value: 9.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   158 EVKDQGLCRSCWAFSTVGAVEGLNKIVTGELVTLSEQDLINCNK--ENNGCGGGKVETAY-EFIMNNGGLGTDNDYPYKA 234
Cdd:PTZ00462  546 QIEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCSKgeHKDRCDEGSNPLEFlQIIEDNGFLPADSNYLYNY 625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   235 --------------LNGVCEGRLKEDNKN--VMIDG-----YENLPANDEaalMKAVAHQPVTAVVDSSSREFQLYESGV 293
Cdd:PTZ00462  626 tkvgedcpdeedhwMNLLDHGKILNHNKKepNSLDGkayraYESEHFHDK---MDAFIKIIKDEIMNKGSVIAYIKAENV 702
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413507   294 ----FDGTCGTNL------NHGVVVVGYGT-----ENGRDYWIVKNSRGDTWGEAGYMKM 338
Cdd:PTZ00462  703 lgyeFNGKKVQNLcgddtaDHAVNIVGYGNyindeDEKKSYWIVRNSWGKYWGDEGYFKV 762
 
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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