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Conserved domains on  [gi|18418684|ref|NP_567983|]
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xylem cysteine peptidase 1 [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;
137-352 6.20e-125

Papain family cysteine protease;


:

Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 357.62  E-value: 6.20e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   137 LPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDtTFNSGCNGGLMDYAFQYIISTG 216
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCD-TFNNGCNGGLPDNAFEYIKKNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   217 GLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALA-HQPVSVAIEASGRDFQFYKGGVFNG-KCGTD 294
Cdd:pfam00112  80 GIVTESDYPYTAKDGTCKFKKSNSKVAKIKGYGDVPYNDEEALQAALAkNGPVSVAIDAYERDFQLYKSGVYKHtECGGE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18418684   295 LDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNTGKpegLCGINKMASYPT 352
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 ...
51-106 5.50e-21

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: 84.99  E-value: 5.50e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18418684     51 FESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRN-NEINSYWLGLNEFADLTHEE 106
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNkKYEHSYKLGVNQFSDLTPEE 57
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
137-352 6.20e-125

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 357.62  E-value: 6.20e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   137 LPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDtTFNSGCNGGLMDYAFQYIISTG 216
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCD-TFNNGCNGGLPDNAFEYIKKNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   217 GLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALA-HQPVSVAIEASGRDFQFYKGGVFNG-KCGTD 294
Cdd:pfam00112  80 GIVTESDYPYTAKDGTCKFKKSNSKVAKIKGYGDVPYNDEEALQAALAkNGPVSVAIDAYERDFQLYKSGVYKHtECGGE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18418684   295 LDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNTGKpegLCGINKMASYPT 352
Cdd:pfam00112 160 LNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNN---ECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
138-351 7.22e-115

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: 331.90  E-value: 7.22e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 138 PKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTFNSGCNGGLMDYAFQYIIStGG 217
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNNGCNGGNPDNAFEYVKN-GG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 218 LHKEDDYPYLMEEGICQEQKEDVeRVTISGYEDVPENDDESLVKALA-HQPVSVAIEASGrDFQFYKGGVFNGKCG--TD 294
Cdd:cd02248  80 LASESDYPYTGKDGTCKYNSSKV-GAKITGYSNVPPGDEEALKAALAnYGPVSVAIDASS-SFQFYKGGIYSGPCCsnTN 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18418684 295 LDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNTgkpeGLCGINKMASYP 351
Cdd:cd02248 158 LNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGS----NLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
137-351 1.18e-90

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 269.07  E-value: 1.18e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684    137 LPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTFNSGCNGGLMDYAFQYIISTG 216
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNCGCNGGLPDNAFEYIKKNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684    217 GLHKEDDYPYlmeegicqeqkedvervtisgyedvpenddeslvkalahqPVSVAIEASgrDFQFYKGGVFNGK-CGTD- 294
Cdd:smart00645  81 GLETESCYPY----------------------------------------TGSVAIDAS--DFQFYKSGIYDHPgCGSGt 118
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684    295 LDHGVAAVGYGSSK--GSDYVIVKNSWGPRWGEKGFIRMKRNTGkpeGLCGIN-KMASYP 351
Cdd:smart00645 119 LDHAVLIVGYGTEVenGKDYWIVKNSWGTDWGENGYFRIARGKN---NECGIEaSVASYP 175
PTZ00021 PTZ00021
falcipain-2; Provisional
50-332 2.04e-79

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 251.23  E-value: 2.04e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   50 LFESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRNNEINS-YWLGLNEFADLTHEEFKGRYLGLAKPQFSRKRQPSAN 128
Cdd:PTZ00021 168 SFYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAHNNKENVlYKKGMNRFGDLSFEEFKKKYLTLKSFDFKSNGKKSPR 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  129 F-RYRDITDLPK---------SVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTfNS 198
Cdd:PTZ00021 248 ViNYDDVIKKYKpkdatfdhaKYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSFK-NN 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  199 GCNGGLMDYAFQYIISTGGLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALAhqPVSVAIEASGrD 278
Cdd:PTZ00021 327 GCYGGLIPNAFEDMIELGGLCSEDDYPYVSDTPELCNIDRCKEKYKIKSYVSIPEDKFKEAIRFLG--PISVSIAVSD-D 403
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18418684  279 FQFYKGGVFNGKCGTDLDHGVAAVGYGSSKGSD----------YVIVKNSWGPRWGEKGFIRMK 332
Cdd:PTZ00021 404 FAFYKGGIFDGECGEEPNHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGFIRIE 467
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
136-332 2.22e-37

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 139.11  E-value: 2.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 136 DLPKSVDWRkkGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSS---LSEQELIDC---DTTFNSGCNGGLMDYAF 209
Cdd:COG4870   3 ALPSSVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNQarnGDGTEGTDDGGSSLRDA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 210 QYIISTGGLHKEDDYPYLMEEGICQ---EQKEDVERVTISGYEDVPENDDESLVKAL-----AHQPVSVAIEASGrDFQF 281
Cdd:COG4870  81 LKLLRWSGVVPESDWPYDDSDFTSQpsaAAYADARNYKIQDYYRLPGGGGATDLDAIkqalaEGGPVVFGFYVYE-SFYN 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18418684 282 YKGGVFNGKCGTDLD--HGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMK 332
Cdd:COG4870 160 YTGGVYYPTPGDASLggHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWIS 212
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
51-106 5.50e-21

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: 84.99  E-value: 5.50e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18418684     51 FESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRN-NEINSYWLGLNEFADLTHEE 106
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNkKYEHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
51-107 2.83e-20

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: 83.08  E-value: 2.83e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18418684    51 FESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRNNEIN-SYWLGLNEFADLTHEEF 107
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGNvTYKLGLNKFADLTDEEF 58
 
Name Accession Description Interval E-value
Peptidase_C1 pfam00112
Papain family cysteine protease;
137-352 6.20e-125

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 357.62  E-value: 6.20e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   137 LPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDtTFNSGCNGGLMDYAFQYIISTG 216
Cdd:pfam00112   1 LPESFDWREKGAVTPVKDQGQCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCD-TFNNGCNGGLPDNAFEYIKKNG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   217 GLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALA-HQPVSVAIEASGRDFQFYKGGVFNG-KCGTD 294
Cdd:pfam00112  80 GIVTESDYPYTAKDGTCKFKKSNSKVAKIKGYGDVPYNDEEALQAALAkNGPVSVAIDAYERDFQLYKSGVYKHtECGGE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18418684   295 LDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNTGKpegLCGINKMASYPT 352
Cdd:pfam00112 160 LNHAVLLVGYGTENGVPYWIVKNSWGTDWGENGYFRIARGVNN---ECGIASEASYPI 214
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
138-351 7.22e-115

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: 331.90  E-value: 7.22e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 138 PKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTFNSGCNGGLMDYAFQYIIStGG 217
Cdd:cd02248   1 PESVDWREKGAVTPVKDQGSCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNNGCNGGNPDNAFEYVKN-GG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 218 LHKEDDYPYLMEEGICQEQKEDVeRVTISGYEDVPENDDESLVKALA-HQPVSVAIEASGrDFQFYKGGVFNGKCG--TD 294
Cdd:cd02248  80 LASESDYPYTGKDGTCKYNSSKV-GAKITGYSNVPPGDEEALKAALAnYGPVSVAIDASS-SFQFYKGGIYSGPCCsnTN 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18418684 295 LDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNTgkpeGLCGINKMASYP 351
Cdd:cd02248 158 LNHAVLLVGYGTENGVDYWIVKNSWGTSWGEKGYIRIARGS----NLCGIASYASYP 210
Pept_C1 smart00645
Papain family cysteine protease;
137-351 1.18e-90

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 269.07  E-value: 1.18e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684    137 LPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTFNSGCNGGLMDYAFQYIISTG 216
Cdd:smart00645   1 LPESFDWRKKGAVTPVKDQGQCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNCGCNGGLPDNAFEYIKKNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684    217 GLHKEDDYPYlmeegicqeqkedvervtisgyedvpenddeslvkalahqPVSVAIEASgrDFQFYKGGVFNGK-CGTD- 294
Cdd:smart00645  81 GLETESCYPY----------------------------------------TGSVAIDAS--DFQFYKSGIYDHPgCGSGt 118
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684    295 LDHGVAAVGYGSSK--GSDYVIVKNSWGPRWGEKGFIRMKRNTGkpeGLCGIN-KMASYP 351
Cdd:smart00645 119 LDHAVLIVGYGTEVenGKDYWIVKNSWGTDWGENGYFRIARGKN---NECGIEaSVASYP 175
PTZ00021 PTZ00021
falcipain-2; Provisional
50-332 2.04e-79

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 251.23  E-value: 2.04e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   50 LFESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRNNEINS-YWLGLNEFADLTHEEFKGRYLGLAKPQFSRKRQPSAN 128
Cdd:PTZ00021 168 SFYLFIKEHGKKYQTPDEMQQRYLSFVENLAKINAHNNKENVlYKKGMNRFGDLSFEEFKKKYLTLKSFDFKSNGKKSPR 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  129 F-RYRDITDLPK---------SVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTfNS 198
Cdd:PTZ00021 248 ViNYDDVIKKYKpkdatfdhaKYDWRLHNGVTPVKDQKNCGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDCSFK-NN 326
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  199 GCNGGLMDYAFQYIISTGGLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALAhqPVSVAIEASGrD 278
Cdd:PTZ00021 327 GCYGGLIPNAFEDMIELGGLCSEDDYPYVSDTPELCNIDRCKEKYKIKSYVSIPEDKFKEAIRFLG--PISVSIAVSD-D 403
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18418684  279 FQFYKGGVFNGKCGTDLDHGVAAVGYGSSKGSD----------YVIVKNSWGPRWGEKGFIRMK 332
Cdd:PTZ00021 404 FAFYKGGIFDGECGEEPNHAVILVGYGMEEIYNsdtkkmekryYYIIKNSWGESWGEKGFIRIE 467
PTZ00200 PTZ00200
cysteine proteinase; Provisional
45-344 3.55e-75

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 238.83  E-value: 3.55e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   45 DKLLElFESWMSEHSKAYKSVEEKVHRFEVFRENLMHI-DQRNNEinSYWLGLNEFADLTHEEFKGRYLGLAKPQFSRKR 123
Cdd:PTZ00200 121 EVYLE-FEEFNKKYNRKHATHAERLNRFLTFRNNYLEVkSHKGDE--PYSKEINKFSDLTEEEFRKLFPVIKVPPKSNST 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  124 QPSANFRYR-------------------DITDLPK----SVDWRKKGAVAPVKDQG-QCGSCWAFSTVAAVEGINQITTG 179
Cdd:PTZ00200 198 SHNNDFKARhvsnptylknlkkakntdeDVKDPSKitgeGLDWRRADAVTKVKDQGlNCGSCWAFSSVGSVESLYKIYRD 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  180 NLSSLSEQELIDCDTtFNSGCNGGLMDYAFQYIiSTGGLHKEDDYPYLMEEGICQEQKEDVerVTISGYEDVPENDdeSL 259
Cdd:PTZ00200 278 KSVDLSEQELVNCDT-KSQGCSGGYPDTALEYV-KNKGLSSSSDVPYLAKDGKCVVSSTKK--VYIDSYLVAKGKD--VL 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  260 VKALAHQPVSVAIEASgRDFQFYKGGVFNGKCGTDLDHGVAAVG--YGSSKGSDYVIVKNSWGPRWGEKGFIRMKRnTGK 337
Cdd:PTZ00200 352 NKSLVISPTVVYIAVS-RELLKYKSGVYNGECGKSLNHAVLLVGegYDEKTKKRYWIIKNSWGTDWGENGYMRLER-TNE 429

                 ....*..
gi 18418684  338 PEGLCGI 344
Cdd:PTZ00200 430 GTDKCGI 436
PTZ00203 PTZ00203
cathepsin L protease; Provisional
50-335 1.24e-69

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 221.50  E-value: 1.24e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   50 LFESWMSEHSKAYKSVEEKVHRFEVFRENL--MHIDQRNNEINSYwlGLNEFADLTHEEFKGRYLGLAKpQFSRKRQPSA 127
Cdd:PTZ00203  37 LFEEFKRTYQRAYGTLTEEQQRLANFERNLelMREHQARNPHARF--GITKFFDLSEAEFAARYLNGAA-YFAAAKQHAG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  128 NFrYR----DITDLPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTfNSGCNGG 203
Cdd:PTZ00203 114 QH-YRkaraDLSAVPDAVDWREKGAVTPVKNQGACGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSCDHV-DNGCGGG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  204 LMDYAFQYIIS--TGGLHKEDDYPYLMEEGI---CQEQKEDVERVTISGYEDVPENDDESLVKALAHQPVSVAIEASGrd 278
Cdd:PTZ00203 192 LMLQAFEWVLRnmNGTVFTEKSYPYVSGNGDvpeCSNSSELAPGARIDGYVSMESSERVMAAWLAKNGPISIAVDASS-- 269
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18418684  279 FQFYKGGVFNGKCGTDLDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNT 335
Cdd:PTZ00203 270 FMSYHSGVLTSCIGEQLNHGVLLVGYNMTGEVPYWVIKNSWGEDWGEKGYVRVTMGV 326
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
140-331 2.18e-38

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: 136.49  E-value: 2.18e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 140 SVDWRKKGaVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSS--LSEQELIDCD----TTFNSGCNGGLMDYAFQYII 213
Cdd:cd02619   1 SVDLRPLR-LTPVKNQGSRGSCWAFASAYALESAYRIKGGEDEYvdLSPQYLYICAndecLGINGSCDGGGPLSALLKLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 214 STGGLHKEDDYPYL---MEEGICQEQKEDVERVTISGYEDVPENDDESLVKALA-HQPVSVAIEASGRDF-----QFYKG 284
Cdd:cd02619  80 ALKGIPPEEDYPYGaesDGEEPKSEAALNAAKVKLKDYRRVLKNNIEDIKEALAkGGPVVAGFDVYSGFDrlkegIIYEE 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 18418684 285 GVFNGKCGTDL-DHGVAAVGYG--SSKGSDYVIVKNSWGPRWGEKGFIRM 331
Cdd:cd02619 160 IVYLLYEDGDLgGHAVVIVGYDdnYVEGKGAFIVKNSWGTDWGDNGYGRI 209
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
136-332 2.22e-37

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 139.11  E-value: 2.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 136 DLPKSVDWRkkGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSS---LSEQELIDC---DTTFNSGCNGGLMDYAF 209
Cdd:COG4870   3 ALPSSVDLR--GYVTPVKDQGSLGSCWAFATAAALESYLKKQAGAPGTsldLSELFLYNQarnGDGTEGTDDGGSSLRDA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 210 QYIISTGGLHKEDDYPYLMEEGICQ---EQKEDVERVTISGYEDVPENDDESLVKAL-----AHQPVSVAIEASGrDFQF 281
Cdd:COG4870  81 LKLLRWSGVVPESDWPYDDSDFTSQpsaAAYADARNYKIQDYYRLPGGGGATDLDAIkqalaEGGPVVFGFYVYE-SFYN 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 18418684 282 YKGGVFNGKCGTDLD--HGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMK 332
Cdd:COG4870 160 YTGGVYYPTPGDASLggHAVAIVGYDDNYSDGAFIIKNSWGTGWGDNGYFWIS 212
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
137-344 5.40e-34

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: 125.58  E-value: 5.40e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 137 LPKSVDWR----KKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSS------LSEQELIDCdTTFNSGCNGGlmd 206
Cdd:cd02621   1 LPKSFDWGdvnnGFNYVSPVRNQGGCGSCYAFASVYALEARIMIASNKTDPlgqqpiLSPQHVLSC-SQYSQGCDGG--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 207 yaFQYIIS----TGGLHKEDDYPYLME-EGICQEQKEDVERVTISGYEDVP---ENDDESLVK--ALAHQPVSVAIEASG 276
Cdd:cd02621  77 --FPFLVGkfaeDFGIVTEDYFPYTADdDRPCKASPSECRRYYFSDYNYVGgcyGCTNEDEMKweIYRNGPIVVAFEVYS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 277 rDFQFYKGGV-----FNGKCGTD---------LDHGVAAVGYGS--SKGSDYVIVKNSWGPRWGEKGFIRMKRNTgkpeG 340
Cdd:cd02621 155 -DFDFYKEGVyhhtdNDEVSDGDndnfnpfelTNHAVLLVGWGEdeIKGEKYWIVKNSWGSSWGEKGYFKIRRGT----N 229

                ....
gi 18418684 341 LCGI 344
Cdd:cd02621 230 ECGI 233
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
138-344 1.06e-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: 124.69  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 138 PKSVDWRKK----GAVAPVKDQGQCGSCWAFSTVAA------VEGINQITTgnlsSLSEQELIDCDTTFNSGCNGGLMDY 207
Cdd:cd02620   1 PESFDAREKwpncISIGEIRDQGNCGSCWAFSAVEAfsdrlcIQSNGKENV----LLSAQDLLSCCSGCGDGCNGGYPDA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 208 AFQYIISTG-------------GLHKEDDYPYLMEEGICQEQKEDVERVTISgyED---------VPENDDESLVKALAH 265
Cdd:cd02620  77 AWKYLTTTGvvtggcqpytippCGHHPEGPPPCCGTPYCTPKCQDGCEKTYE--EDkhkgksaysVPSDETDIMKEIMTN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 266 QPVSVAIEASgRDFQFYKGGVFNGKCGTDLD-HGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRntGKPEglCGI 344
Cdd:cd02620 155 GPVQAAFTVY-EDFLYYKSGVYQHTSGKQLGgHAVKIIGWGVENGVPYWLAANSWGTDWGENGYFRILR--GSNE--CGI 229
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
137-337 7.18e-25

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: 100.95  E-value: 7.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 137 LPKSVDWRKKGAV---APVKDQ---GQCGSCWAFSTVAAV-EGINQITTGNLSS--LSEQELIDCDttfNSG-CNGGLMD 206
Cdd:cd02698   1 LPKSWDWRNVNGVnyvSPTRNQhipQYCGSCWAHGSTSALaDRINIARKGAWPSvyLSVQVVIDCA---GGGsCHGGDPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684 207 YAFQYIISTGgLHKEDDYPYLMEEGICQEQKED--------------------VERVTISGYEDVpenddesLVKALAHQ 266
Cdd:cd02698  78 GVYEYAHKHG-IPDETCNPYQAKDGECNPFNRCgtcnpfgecfaiknytlyfvSDYGSVSGRDKM-------MAEIYARG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18418684 267 PVSVAIEASGRdFQFYKGGVFNGKCGTDL-DHGVAAVGYG-SSKGSDYVIVKNSWGPRWGEKGFIRMKRNTGK 337
Cdd:cd02698 150 PISCGIMATEA-LENYTGGVYKEYVQDPLiNHIISVAGWGvDENGVEYWIVRNSWGEPWGERGWFRIVTSSYK 221
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
51-106 5.50e-21

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: 84.99  E-value: 5.50e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18418684     51 FESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRN-NEINSYWLGLNEFADLTHEE 106
Cdd:smart00848   1 FEQWKKKHGKSYSSEEEEARRFAIFKENLKKIEEHNkKYEHSYKLGVNQFSDLTPEE 57
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
51-107 2.83e-20

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: 83.08  E-value: 2.83e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18418684    51 FESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRNNEIN-SYWLGLNEFADLTHEEF 107
Cdd:pfam08246   1 FDDWMKKYGKSYRSEEEELYRFQIFKENLKRIEEHNSNGNvTYKLGLNKFADLTDEEF 58
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
137-335 3.00e-10

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 61.44  E-value: 3.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  137 LPKSVDWRKKGAVA---PVKDQG---QCGSCWAFSTVAAVEGINQITT------GNLSSLSEQELIDCdTTFNSGCNGGL 204
Cdd:PTZ00364 205 PPAAWSWGDVGGASflpAAPPASpgrGCNSSYVEAALAAMMARVMVASnrtdplGQQTFLSARHVLDC-SQYGQGCAGGF 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  205 MDYAFQYiISTGGLHKEDDY--PYLMEEGICQEQKEDVERV--------TISGYEDVPENDDESLVKALAHQPVSVAIEA 274
Cdd:PTZ00364 284 PEEVGKF-AETFGILTTDSYyiPYDSGDGVERACKTRRPSRryyftnygPLGGYYGAVTDPDEIIWEIYRHGPVPASVYA 362
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  275 sGRDFQFYKGGVFNGKCGT--------------------DLDHGVAAVGYGSSK-GSDYVIVKNSWGPR--WGEKGFIRM 331
Cdd:PTZ00364 363 -NSDWYNCDENSTEDVRYVslddystasadrplrhyfasNVNHTVLIIGWGTDEnGGDYWLVLDPWGSRrsWCDGGTRKI 441

                 ....
gi 18418684  332 KRNT 335
Cdd:PTZ00364 442 ARGV 445
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
133-333 2.34e-09

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 58.81  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  133 DITDLPKSVDW----RKKGAVAPVKDQGQCGSCWAFST---------VAAVEGINQITTGNLSS-LSEQELIDCdTTFNS 198
Cdd:PTZ00049 377 EIDELPKNFTWgdpfNNNTREYDVTNQLLCGSCYIASQmyafkrrieIALTKNLDKKYLNNFDDlLSIQTVLSC-SFYDQ 455
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  199 GCNGGlmdyaFQYIIST----GGLHKEDDYPYLMEEGICQEQKEDV---------------------ERVTISGYEDVPE 253
Cdd:PTZ00049 456 GCNGG-----FPYLVSKmaklQGIPLDKVFPYTATEQTCPYQVDQSansmngsanlrqinavffsseTQSDMHADFEAPI 530
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684  254 NDDES-------------------------LVKALAHQPVSVAIEASgRDFQFYKGGVFNG-------KCGTDL------ 295
Cdd:PTZ00049 531 SSEPArwyakdynyiggcygcnqcngekimMNEIYRNGPIVASFEAS-PDFYDYADGVYYVedfpharRCTVDLpkhngv 609
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18418684  296 ---------DHGVAAVGYGSS----KGSDYVIVKNSWGPRWGEKGFIRMKR 333
Cdd:PTZ00049 610 ynitgwekvNHAIVLVGWGEEeingKLYKYWIGRNSWGKNWGKEGYFKIIR 660
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
152-331 2.27e-08

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 55.84  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   152 VKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDT-TFNSGCNGGLMDYAFQYIISTGG-LHKEDDYPY--- 226
Cdd:PTZ00462  547 IEDQGNCAISWIFASKYHLETIKCMKGYEPHAISALYIANCSKgEHKDRCDEGSNPLEFLQIIEDNGfLPADSNYLYnyt 626
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418684   227 ---------------LMEEG-ICQEQKEDVERVTISGY-----EDVPENDDE--SLVKALAHQPVSVAIEASGRDFQFYK 283
Cdd:PTZ00462  627 kvgedcpdeedhwmnLLDHGkILNHNKKEPNSLDGKAYrayesEHFHDKMDAfiKIIKDEIMNKGSVIAYIKAENVLGYE 706
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18418684   284 ggvFNGK-----CGTDL-DHGVAAVGYGSSKGSD-----YVIVKNSWGPRWGEKGFIRM 331
Cdd:PTZ00462  707 ---FNGKkvqnlCGDDTaDHAVNIVGYGNYINDEdekksYWIVRNSWGKYWGDEGYFKV 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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