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Conserved domains on  [gi|21357391|ref|NP_649608|]
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uncharacterized protein Dmel_CG11459, isoform A [Drosophila melanogaster]

Protein Classification

C1 family peptidase( domain architecture ID 10549616)

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
PubMed:  12887050|11517925
SCOP:  4000859

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
120-334 4.68e-93

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: 275.66  E-value: 4.68e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 120 EGIDWRQYGYISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCVPYPNNGCSGGWVSVAFNYTRDHGI 199
Cdd:cd02248   2 ESVDWREKGAVTPVKDQG-SCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNNGCNGGNPDNAFEYVKNGGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 200 ATKESYPYEPVSGECLWKSDRSAGTLSGYVTLGNYDERELAEVVYNIGPVAVSIDHLHeEFDQYSGGVLSIPACRSKrqD 279
Cdd:cd02248  81 ASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNT--N 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21357391 280 LTHSVLLVGFGTHrKWGDYWIIKNSYGTDWGESGYLKLARNaNNMCGVASLPQYP 334
Cdd:cd02248 158 LNHAVLLVGYGTE-NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
30-85 8.05e-11

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: 56.88  E-value: 8.05e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21357391    30 WDQYKAKYNKQYRN-RDKYHR-ALYEQRVLAVESHNQlylQGKVAFKMGLNKFSD-TDQ 85
Cdd:pfam08246   1 FDDWMKKYGKSYRSeEEELYRfQIFKENLKRIEEHNS---NGNVTYKLGLNKFADlTDE 56
 
Name Accession Description Interval E-value
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
120-334 4.68e-93

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: 275.66  E-value: 4.68e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 120 EGIDWRQYGYISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCVPYPNNGCSGGWVSVAFNYTRDHGI 199
Cdd:cd02248   2 ESVDWREKGAVTPVKDQG-SCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNNGCNGGNPDNAFEYVKNGGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 200 ATKESYPYEPVSGECLWKSDRSAGTLSGYVTLGNYDERELAEVVYNIGPVAVSIDHLHeEFDQYSGGVLSIPACRSKrqD 279
Cdd:cd02248  81 ASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNT--N 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21357391 280 LTHSVLLVGFGTHrKWGDYWIIKNSYGTDWGESGYLKLARNaNNMCGVASLPQYP 334
Cdd:cd02248 158 LNHAVLLVGYGTE-NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Peptidase_C1 pfam00112
Papain family cysteine protease;
120-335 8.86e-79

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 239.75  E-value: 8.86e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   120 EGIDWRQYGYISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCVPYpNNGCSGGWVSVAFNY-TRDHG 198
Cdd:pfam00112   3 ESFDWREKGAVTPVKDQG-QCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTF-NNGCNGGLPDNAFEYiKKNGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   199 IATKESYPYEPVSGECLWKSDRS-AGTLSGYVTLGNYDERELAEVVYNIGPVAVSIDHLHEEFDQYSGGVLSIPACRSKr 277
Cdd:pfam00112  81 IVTESDYPYTAKDGTCKFKKSNSkVAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGGE- 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 21357391   278 qdLTHSVLLVGFGTHRKwGDYWIIKNSYGTDWGESGYLKLARNANNMCGVASLPQYPT 335
Cdd:pfam00112 160 --LNHAVLLVGYGTENG-VPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
Pept_C1 smart00645
Papain family cysteine protease;
120-334 1.25e-60

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 191.64  E-value: 1.25e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391    120 EGIDWRQYGYISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCVPYPNNGCSGGWVSVAFNYTRDH-G 198
Cdd:smart00645   3 ESFDWRKKGAVTPVKDQG-QCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNCGCNGGLPDNAFEYIKKNgG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391    199 IATKESYPYEpvsgeclwksdrsagtlsgyvtlgnyderelaevvynigpVAVSIDhlHEEFDQYSGGVLSIPACRSKrq 278
Cdd:smart00645  82 LETESCYPYT----------------------------------------GSVAID--ASDFQFYKSGIYDHPGCGSG-- 117
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 21357391    279 DLTHSVLLVGFGTHRKWG-DYWIIKNSYGTDWGESGYLKLARNANNMCGV-ASLPQYP 334
Cdd:smart00645 118 TLDHAVLIVGYGTEVENGkDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
PTZ00200 PTZ00200
cysteine proteinase; Provisional
29-336 2.54e-52

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 178.73  E-value: 2.54e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   29 EWDQYKAKYNKQYRNRDKYHRAL--YEQRVLAVESHnqlylQGKVAFKMGLNKFSD-TDQ--RILF---------NYRSS 94
Cdd:PTZ00200 125 EFEEFNKKYNRKHATHAERLNRFltFRNNYLEVKSH-----KGDEPYSKEINKFSDlTEEefRKLFpvikvppksNSTSH 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   95 IPAPLETSTNALTETVNYKR--------YD--QIT-EGIDWRQYGYISPVGDQGTECLSCWAFSTSGVLEAhMAKKYGNL 163
Cdd:PTZ00200 200 NNDFKARHVSNPTYLKNLKKakntdedvKDpsKITgEGLDWRRADAVTKVKDQGLNCGSCWAFSSVGSVES-LYKIYRDK 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  164 -VPLSPKHLVDCvPYPNNGCSGGWVSVAFNYTRDHGIATKESYPYEPVSGECLwKSDRSAGTLSGYVTLGNYDerelaev 242
Cdd:PTZ00200 279 sVDLSEQELVNC-DTKSQGCSGGYPDTALEYVKNKGLSSSSDVPYLAKDGKCV-VSSTKKVYIDSYLVAKGKD------- 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  243 VYN----IGPVAVSIDhLHEEFDQYSGGVLSIPACRSkrqdLTHSVLLVGFGTHRKWGD-YWIIKNSYGTDWGESGYLKL 317
Cdd:PTZ00200 350 VLNkslvISPTVVYIA-VSRELLKYKSGVYNGECGKS----LNHAVLLVGEGYDEKTKKrYWIIKNSWGTDWGENGYMRL 424
                        330       340
                 ....*....|....*....|.
gi 21357391  318 ARN--ANNMCGVASLPQYPTF 336
Cdd:PTZ00200 425 ERTneGTDKCGILTVGLTPVF 445
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
122-314 9.26e-28

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 112.15  E-value: 9.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 122 IDWRQYgyISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNL---VPLSPKHLVDCV----PYPNNGCSGGWVSVAFNYT 194
Cdd:COG4870   8 VDLRGY--VTPVKDQG-SLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQArngdGTEGTDDGGSSLRDALKLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 195 RDHGIATKESYPYEPVS-----GECLWKSDRSAGTLSGYVTLGNYDERELAEV---VYNIGPVAVSIdHLHEEFDQYSGG 266
Cdd:COG4870  85 RWSGVVPESDWPYDDSDftsqpSAAAYADARNYKIQDYYRLPGGGGATDLDAIkqaLAEGGPVVFGF-YVYESFYNYTGG 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21357391 267 VLSipACRSKRQDLTHSVLLVGFgTHRKWGDYWIIKNSYGTDWGESGY 314
Cdd:COG4870 164 VYY--PTPGDASLGGHAVAIVGY-DDNYSDGAFIIKNSWGTGWGDNGY 208
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
30-85 8.05e-11

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: 56.88  E-value: 8.05e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21357391    30 WDQYKAKYNKQYRN-RDKYHR-ALYEQRVLAVESHNQlylQGKVAFKMGLNKFSD-TDQ 85
Cdd:pfam08246   1 FDDWMKKYGKSYRSeEEELYRfQIFKENLKRIEEHNS---NGNVTYKLGLNKFADlTDE 56
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
30-82 1.94e-09

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: 53.02  E-value: 1.94e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 21357391     30 WDQYKAKYNKQYRNRD--KYHRALYEQRVLAVESHNQLYLQGkvaFKMGLNKFSD 82
Cdd:smart00848   1 FEQWKKKHGKSYSSEEeeARRFAIFKENLKKIEEHNKKYEHS---YKLGVNQFSD 52
 
Name Accession Description Interval E-value
Peptidase_C1A cd02248
Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) ...
120-334 4.68e-93

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: 275.66  E-value: 4.68e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 120 EGIDWRQYGYISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCVPYPNNGCSGGWVSVAFNYTRDHGI 199
Cdd:cd02248   2 ESVDWREKGAVTPVKDQG-SCGSCWAFSTVGALEGAYAIKTGKLVSLSEQQLVDCSTSGNNGCNGGNPDNAFEYVKNGGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 200 ATKESYPYEPVSGECLWKSDRSAGTLSGYVTLGNYDERELAEVVYNIGPVAVSIDHLHeEFDQYSGGVLSIPACRSKrqD 279
Cdd:cd02248  81 ASESDYPYTGKDGTCKYNSSKVGAKITGYSNVPPGDEEALKAALANYGPVSVAIDASS-SFQFYKGGIYSGPCCSNT--N 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21357391 280 LTHSVLLVGFGTHrKWGDYWIIKNSYGTDWGESGYLKLARNaNNMCGVASLPQYP 334
Cdd:cd02248 158 LNHAVLLVGYGTE-NGVDYWIVKNSWGTSWGEKGYIRIARG-SNLCGIASYASYP 210
Peptidase_C1 pfam00112
Papain family cysteine protease;
120-335 8.86e-79

Papain family cysteine protease;


Pssm-ID: 425470 [Multi-domain]  Cd Length: 214  Bit Score: 239.75  E-value: 8.86e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   120 EGIDWRQYGYISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCVPYpNNGCSGGWVSVAFNY-TRDHG 198
Cdd:pfam00112   3 ESFDWREKGAVTPVKDQG-QCGSCWAFSAVGALEGRYCIKTGKLVSLSEQQLVDCDTF-NNGCNGGLPDNAFEYiKKNGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   199 IATKESYPYEPVSGECLWKSDRS-AGTLSGYVTLGNYDERELAEVVYNIGPVAVSIDHLHEEFDQYSGGVLSIPACRSKr 277
Cdd:pfam00112  81 IVTESDYPYTAKDGTCKFKKSNSkVAKIKGYGDVPYNDEEALQAALAKNGPVSVAIDAYERDFQLYKSGVYKHTECGGE- 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 21357391   278 qdLTHSVLLVGFGTHRKwGDYWIIKNSYGTDWGESGYLKLARNANNMCGVASLPQYPT 335
Cdd:pfam00112 160 --LNHAVLLVGYGTENG-VPYWIVKNSWGTDWGENGYFRIARGVNNECGIASEASYPI 214
Pept_C1 smart00645
Papain family cysteine protease;
120-334 1.25e-60

Papain family cysteine protease;


Pssm-ID: 214761 [Multi-domain]  Cd Length: 175  Bit Score: 191.64  E-value: 1.25e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391    120 EGIDWRQYGYISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCVPYPNNGCSGGWVSVAFNYTRDH-G 198
Cdd:smart00645   3 ESFDWRKKGAVTPVKDQG-QCGSCWAFSATGALEGRYCIKTGKLVSLSEQQLVDCSGGGNCGCNGGLPDNAFEYIKKNgG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391    199 IATKESYPYEpvsgeclwksdrsagtlsgyvtlgnyderelaevvynigpVAVSIDhlHEEFDQYSGGVLSIPACRSKrq 278
Cdd:smart00645  82 LETESCYPYT----------------------------------------GSVAID--ASDFQFYKSGIYDHPGCGSG-- 117
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 21357391    279 DLTHSVLLVGFGTHRKWG-DYWIIKNSYGTDWGESGYLKLARNANNMCGV-ASLPQYP 334
Cdd:smart00645 118 TLDHAVLIVGYGTEVENGkDYWIVKNSWGTDWGENGYFRIARGKNNECGIeASVASYP 175
PTZ00200 PTZ00200
cysteine proteinase; Provisional
29-336 2.54e-52

cysteine proteinase; Provisional


Pssm-ID: 240310 [Multi-domain]  Cd Length: 448  Bit Score: 178.73  E-value: 2.54e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   29 EWDQYKAKYNKQYRNRDKYHRAL--YEQRVLAVESHnqlylQGKVAFKMGLNKFSD-TDQ--RILF---------NYRSS 94
Cdd:PTZ00200 125 EFEEFNKKYNRKHATHAERLNRFltFRNNYLEVKSH-----KGDEPYSKEINKFSDlTEEefRKLFpvikvppksNSTSH 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   95 IPAPLETSTNALTETVNYKR--------YD--QIT-EGIDWRQYGYISPVGDQGTECLSCWAFSTSGVLEAhMAKKYGNL 163
Cdd:PTZ00200 200 NNDFKARHVSNPTYLKNLKKakntdedvKDpsKITgEGLDWRRADAVTKVKDQGLNCGSCWAFSSVGSVES-LYKIYRDK 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  164 -VPLSPKHLVDCvPYPNNGCSGGWVSVAFNYTRDHGIATKESYPYEPVSGECLwKSDRSAGTLSGYVTLGNYDerelaev 242
Cdd:PTZ00200 279 sVDLSEQELVNC-DTKSQGCSGGYPDTALEYVKNKGLSSSSDVPYLAKDGKCV-VSSTKKVYIDSYLVAKGKD------- 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  243 VYN----IGPVAVSIDhLHEEFDQYSGGVLSIPACRSkrqdLTHSVLLVGFGTHRKWGD-YWIIKNSYGTDWGESGYLKL 317
Cdd:PTZ00200 350 VLNkslvISPTVVYIA-VSRELLKYKSGVYNGECGKS----LNHAVLLVGEGYDEKTKKrYWIIKNSWGTDWGENGYMRL 424
                        330       340
                 ....*....|....*....|.
gi 21357391  318 ARN--ANNMCGVASLPQYPTF 336
Cdd:PTZ00200 425 ERTneGTDKCGILTVGLTPVF 445
PTZ00203 PTZ00203
cathepsin L protease; Provisional
118-331 5.90e-40

cathepsin L protease; Provisional


Pssm-ID: 185513 [Multi-domain]  Cd Length: 348  Bit Score: 143.69  E-value: 5.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  118 ITEGIDWRQYGYISPVGDQGTeCLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCvPYPNNGCSGGWVSVAFNYTRDH 197
Cdd:PTZ00203 126 VPDAVDWREKGAVTPVKNQGA-CGSCWAFSAVGNIESQWAVAGHKLVRLSEQQLVSC-DHVDNGCGGGLMLQAFEWVLRN 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  198 ---GIATKESYPYepVSG-----ECLWKSDRSAGT-LSGYVTLGNyDERELAEVVYNIGPVAVSIDHlhEEFDQYSGGVL 268
Cdd:PTZ00203 204 mngTVFTEKSYPY--VSGngdvpECSNSSELAPGArIDGYVSMES-SERVMAAWLAKNGPISIAVDA--SSFMSYHSGVL 278
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21357391  269 SipACRSKRqdLTHSVLLVGFGthrKWGD--YWIIKNSYGTDWGESGYLKLARNANNmCGVASLP 331
Cdd:PTZ00203 279 T--SCIGEQ--LNHGVLLVGYN---MTGEvpYWVIKNSWGEDWGEKGYVRVTMGVNA-CLLTGYP 335
PTZ00021 PTZ00021
falcipain-2; Provisional
37-317 6.71e-36

falcipain-2; Provisional


Pssm-ID: 240232 [Multi-domain]  Cd Length: 489  Bit Score: 135.67  E-value: 6.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391   37 YNKQYRNRDKY-HRAL-YEQRVLAVESHNQlylQGKVAFKMGLNKFSDTD----QRILFNYRSSipaPLETSTNALTETV 110
Cdd:PTZ00021 176 HGKKYQTPDEMqQRYLsFVENLAKINAHNN---KENVLYKKGMNRFGDLSfeefKKKYLTLKSF---DFKSNGKKSPRVI 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  111 NY----KRYDQITEGID-----WRQYGYISPVGDQGTeCLSCWAFSTSGVLEAHMAKKYGNLVPLSPKHLVDCvPYPNNG 181
Cdd:PTZ00021 250 NYddviKKYKPKDATFDhakydWRLHNGVTPVKDQKN-CGSCWAFSTVGVVESQYAIRKNELVSLSEQELVDC-SFKNNG 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  182 CSGGWVSVAFNYTRD-HGIATKESYPYEPVSGE-CLWKSDRSAGTLSGYVTLgnyDERELAEVVYNIGPVAVSIDhLHEE 259
Cdd:PTZ00021 328 CYGGLIPNAFEDMIElGGLCSEDDYPYVSDTPElCNIDRCKEKYKIKSYVSI---PEDKFKEAIRFLGPISVSIA-VSDD 403
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21357391  260 FDQYSGGVLSIPACRSkrqdLTHSVLLVGFGTHRKWGD---------YWIIKNSYGTDWGESGYLKL 317
Cdd:PTZ00021 404 FAFYKGGIFDGECGEE----PNHAVILVGYGMEEIYNSdtkkmekryYYIIKNSWGESWGEKGFIRI 466
Peptidase_C1A_CathepsinB cd02620
Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial ...
124-326 1.06e-35

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: 129.31  E-value: 1.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 124 WRQYGYISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNL--VPLSPKHLVDCVPYPNNGCSGGWVSVAFNYTRDHGIAT 201
Cdd:cd02620  10 WPNCISIGEIRDQG-NCGSCWAFSAVEAFSDRLCIQSNGKenVLLSAQDLLSCCSGCGDGCNGGYPDAAWKYLTTTGVVT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 202 KESYPY--------------EPVSGEC----------LWKSDRSAGTLSGYVtlgNYDERELAEVVYNIGPVAVSIDhLH 257
Cdd:cd02620  89 GGCQPYtippcghhpegpppCCGTPYCtpkcqdgcekTYEEDKHKGKSAYSV---PSDETDIMKEIMTNGPVQAAFT-VY 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21357391 258 EEFDQYSGGVLSIpacRSKRQDLTHSVLLVGFGTHRKWgDYWIIKNSYGTDWGESGYLKLARNANNmCG 326
Cdd:cd02620 165 EDFLYYKSGVYQH---TSGKQLGGHAVKIIGWGVENGV-PYWLAANSWGTDWGENGYFRILRGSNE-CG 228
Peptidase_C1 cd02619
C1 Peptidase family (MEROPS database nomenclature), also referred to as the papain family; ...
123-317 1.17e-34

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: 126.09  E-value: 1.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 123 DWRQYgYISPVGDQGTeCLSCWAFSTSGVLEAHMAKKYGN--LVPLSPKHLVDCVPY----PNNGCSGGWVSVAFNYT-R 195
Cdd:cd02619   3 DLRPL-RLTPVKNQGS-RGSCWAFASAYALESAYRIKGGEdeYVDLSPQYLYICANDeclgINGSCDGGGPLSALLKLvA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 196 DHGIATKESYPYEPVSGECLWKSDRSAG----TLSGYVTLGNYDERELAEVVYNIGPVAVSIDhLHEEFDQYSGGVLS-- 269
Cdd:cd02619  81 LKGIPPEEDYPYGAESDGEEPKSEAALNaakvKLKDYRRVLKNNIEDIKEALAKGGPVVAGFD-VYSGFDRLKEGIIYee 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21357391 270 IPACRSKRQDL-THSVLLVGFGTHRKWG-DYWIIKNSYGTDWGESGYLKL 317
Cdd:cd02619 160 IVYLLYEDGDLgGHAVVIVGYDDNYVEGkGAFIVKNSWGTDWGDNGYGRI 209
Peptidase_C1A_CathepsinC cd02621
Cathepsin C; also known as Dipeptidyl Peptidase I (DPPI), an atypical papain-like cysteine ...
123-331 5.19e-33

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: 122.49  E-value: 5.19e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 123 DWRQYG----YISPVGDQGTeCLSCWAFSTSGVLEAHMAKKYGNLVP------LSPKHLVDCVPYpNNGCSGGWVSVAFN 192
Cdd:cd02621   6 DWGDVNngfnYVSPVRNQGG-CGSCYAFASVYALEARIMIASNKTDPlgqqpiLSPQHVLSCSQY-SQGCDGGFPFLVGK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 193 YTRDHGIATKESYPYEPVS-GECLWK---SDRSAGTLSGYV--TLGNYDERELAEVVYNIGPVAVSIdHLHEEFDQYSGG 266
Cdd:cd02621  84 FAEDFGIVTEDYFPYTADDdRPCKASpseCRRYYFSDYNYVggCYGCTNEDEMKWEIYRNGPIVVAF-EVYSDFDFYKEG 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21357391 267 VLSIPACRSKRQDL----------THSVLLVGFGT-HRKWGDYWIIKNSYGTDWGESGYLKLARnANNMCGVASLP 331
Cdd:cd02621 163 VYHHTDNDEVSDGDndnfnpfeltNHAVLLVGWGEdEIKGEKYWIVKNSWGSSWGEKGYFKIRR-GTNECGIESQA 237
Peptidase_C1A_CathepsinX cd02698
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase ...
123-321 4.27e-28

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: 109.43  E-value: 4.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 123 DWRQ---YGYISPVGDQ--GTECLSCWAFSTSGVLEAHM--AKK-YGNLVPLSPKHLVDCvpypNNG--CSGGWVSVAFN 192
Cdd:cd02698   6 DWRNvngVNYVSPTRNQhiPQYCGSCWAHGSTSALADRIniARKgAWPSVYLSVQVVIDC----AGGgsCHGGDPGGVYE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 193 YTRDHGIATKESYPYEPVSGEC----------------------LWK-SDRsaGTLSGYvtlgnydERELAEVvYNIGPV 249
Cdd:cd02698  82 YAHKHGIPDETCNPYQAKDGECnpfnrcgtcnpfgecfaiknytLYFvSDY--GSVSGR-------DKMMAEI-YARGPI 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21357391 250 AVSIDhLHEEFDQYSGGVLSIPacrSKRQDLTHSVLLVGFGTHRKWGDYWIIKNSYGTDWGESGYLKLARNA 321
Cdd:cd02698 152 SCGIM-ATEALENYTGGVYKEY---VQDPLINHIISVAGWGVDENGVEYWIVRNSWGEPWGERGWFRIVTSS 219
COG4870 COG4870
Cysteine protease, C1A family [Posttranslational modification, protein turnover, chaperones];
122-314 9.26e-28

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


Pssm-ID: 443898 [Multi-domain]  Cd Length: 426  Bit Score: 112.15  E-value: 9.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 122 IDWRQYgyISPVGDQGtECLSCWAFSTSGVLEAHMAKKYGNL---VPLSPKHLVDCV----PYPNNGCSGGWVSVAFNYT 194
Cdd:COG4870   8 VDLRGY--VTPVKDQG-SLGSCWAFATAAALESYLKKQAGAPgtsLDLSELFLYNQArngdGTEGTDDGGSSLRDALKLL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391 195 RDHGIATKESYPYEPVS-----GECLWKSDRSAGTLSGYVTLGNYDERELAEV---VYNIGPVAVSIdHLHEEFDQYSGG 266
Cdd:COG4870  85 RWSGVVPESDWPYDDSDftsqpSAAAYADARNYKIQDYYRLPGGGGATDLDAIkqaLAEGGPVVFGF-YVYESFYNYTGG 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21357391 267 VLSipACRSKRQDLTHSVLLVGFgTHRKWGDYWIIKNSYGTDWGESGY 314
Cdd:COG4870 164 VYY--PTPGDASLGGHAVAIVGY-DDNYSDGAFIIKNSWGTGWGDNGY 208
PTZ00364 PTZ00364
dipeptidyl-peptidase I precursor; Provisional
116-322 2.67e-17

dipeptidyl-peptidase I precursor; Provisional


Pssm-ID: 240381 [Multi-domain]  Cd Length: 548  Bit Score: 82.63  E-value: 2.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  116 DQITEGIDWRQYG---YISPVGDQ--GTECLSCWAFSTsgvLEAHMAK---------KYGNLVPLSPKHLVDCVPYpNNG 181
Cdd:PTZ00364 203 DPPPAAWSWGDVGgasFLPAAPPAspGRGCNSSYVEAA---LAAMMARvmvasnrtdPLGQQTFLSARHVLDCSQY-GQG 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  182 CSGGWVSVAFNYTRDHGIATKESYPYEPVSGECLWKSDRSAGT-----LSGYVTLGNY-----DERELAEVVYNIGPVAV 251
Cdd:PTZ00364 279 CAGGFPEEVGKFAETFGILTTDSYYIPYDSGDGVERACKTRRPsrryyFTNYGPLGGYygavtDPDEIIWEIYRHGPVPA 358
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  252 SI---------DHLHEE------FDQYSggvlSIPACRSKRQ----DLTHSVLLVGFGTHRKWGDYWIIKNSYGT--DWG 310
Cdd:PTZ00364 359 SVyansdwyncDENSTEdvryvsLDDYS----TASADRPLRHyfasNVNHTVLIIGWGTDENGGDYWLVLDPWGSrrSWC 434
                        250
                 ....*....|..
gi 21357391  311 ESGYLKLARNAN 322
Cdd:PTZ00364 435 DGGTRKIARGVN 446
PTZ00049 PTZ00049
cathepsin C-like protein; Provisional
133-322 1.36e-12

cathepsin C-like protein; Provisional


Pssm-ID: 240244 [Multi-domain]  Cd Length: 693  Bit Score: 68.44  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  133 VGDQGTeCLSCWAFSTSGVLE--------AHMAKKYGNLVP--LSPKHLVDCVPYpNNGCSGGWVSVAFNYTRDHGIATK 202
Cdd:PTZ00049 400 VTNQLL-CGSCYIASQMYAFKrrieialtKNLDKKYLNNFDdlLSIQTVLSCSFY-DQGCNGGFPYLVSKMAKLQGIPLD 477
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  203 ESYPYEPVSGECLWKSDRSAGTLSGYVTL----------------------------------------GNYD------E 236
Cdd:PTZ00049 478 KVFPYTATEQTCPYQVDQSANSMNGSANLrqinavffssetqsdmhadfeapisseparwyakdynyigGCYGcnqcngE 557
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357391  237 RELAEVVYNIGPVAVSIDHLHEEFDqYSGGVL---SIPACRSKRQDLT---------------HSVLLVGFGTHRKWG-- 296
Cdd:PTZ00049 558 KIMMNEIYRNGPIVASFEASPDFYD-YADGVYyveDFPHARRCTVDLPkhngvynitgwekvnHAIVLVGWGEEEINGkl 636
                        250       260
                 ....*....|....*....|....*..
gi 21357391  297 -DYWIIKNSYGTDWGESGYLKLARNAN 322
Cdd:PTZ00049 637 yKYWIGRNSWGKNWGKEGYFKIIRGKN 663
Inhibitor_I29 pfam08246
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
30-85 8.05e-11

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: 56.88  E-value: 8.05e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 21357391    30 WDQYKAKYNKQYRN-RDKYHR-ALYEQRVLAVESHNQlylQGKVAFKMGLNKFSD-TDQ 85
Cdd:pfam08246   1 FDDWMKKYGKSYRSeEEELYRfQIFKENLKRIEEHNS---NGNVTYKLGLNKFADlTDE 56
Inhibitor_I29 smart00848
Cathepsin propeptide inhibitor domain (I29); This domain is found at the N-terminus of some C1 ...
30-82 1.94e-09

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: 53.02  E-value: 1.94e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 21357391     30 WDQYKAKYNKQYRNRD--KYHRALYEQRVLAVESHNQLYLQGkvaFKMGLNKFSD 82
Cdd:smart00848   1 FEQWKKKHGKSYSSEEeeARRFAIFKENLKKIEEHNKKYEHS---YKLGVNQFSD 52
PTZ00462 PTZ00462
Serine-repeat antigen protein; Provisional
273-317 3.07e-04

Serine-repeat antigen protein; Provisional


Pssm-ID: 185641 [Multi-domain]  Cd Length: 1004  Bit Score: 42.74  E-value: 3.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 21357391   273 CRSKRQDltHSVLLVGFGTHRKWGD----YWIIKNSYGTDWGESGYLKL 317
Cdd:PTZ00462  716 CGDDTAD--HAVNIVGYGNYINDEDekksYWIVRNSWGKYWGDEGYFKV 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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