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Conserved domains on  [gi|7242187|ref|NP_035305|]
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legumain preproprotein [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C13 pfam01650
Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke ...
31-287 7.83e-161

Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke parasite Schistosoma mansoni has at least five Clan CA cysteine peptidases in its digestive tract including cathepsins B (2 isoforms), C, F and L. All have been recombinantly expressed as active enzymes, albeit in various stages of activation. In addition, a Clan CD peptidase, termed asparaginyl endopeptidase or 'legumain' has been identified. This has formerly been characterized as a 'haemoglobinase', but this term is probably incorrect. Two cDNAs have been described for Schistosoma mansoni legumain; one encodes an active enzyme whereas the active site cysteine residue encoded by the second cDNA is substituted by an asparagine residue. Both forms have been recombinantly expressed.


:

Pssm-ID: 396290  Cd Length: 257  Bit Score: 453.67  E-value: 7.83e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187     31 HWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVINRPNGTDVYKGVLKDYTGEDV 110
Cdd:pfam01650   1 LWAVLVAGSNGYYNYRHQADVCHAYQLLKKFGIKDENIIVMMYDDIANNPENPFPGKIFNKPNGTDVYKGVPKDYTGNDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187    111 TPENFLAVLRGDAEAVkgkGSGKVLKSGPRDHVFIYFTDHGATGILVFPN-DDLHVKDLNKTIRYMYEHKMYQKMVFYIE 189
Cdd:pfam01650  81 TPRNFLAVLLGDKSAL---GSGKVLKSGPNDNVFIYFTDHGAPGVLGFPElDYLYAKDLAEALKKMHARGKYKKLVFYVE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187    190 ACESGSMMNHLPDDINVYATTAANPKESSYACYY-DEERGTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSH 268
Cdd:pfam01650 158 ACESGSMFEGLPKDINVYATTAANADESSYGCYCpDPEDGTYLGDLFSVNWMEDSDDHDLSKETLEQQFELVKNRTTGSH 237
                         250
                  ....*....|....*....
gi 7242187    269 VMQYGNKSISTMKVMQFQG 287
Cdd:pfam01650 238 VMQYGDKSLPQLPLSLFQG 256
legumain_C cd21115
C-terminal prodomain of legumain; This family contains the C-terminal propeptide of legumain, ...
311-431 2.02e-53

C-terminal prodomain of legumain; This family contains the C-terminal propeptide of legumain, a lysosomal endopeptidase with a specificity for hydrolysis of asparaginyl bonds. Legumain (also called vacuolar processing enzyme or VPE in plants, and asparaginyl endopeptidase or AEP in animals) is synthesized as a precursor with both N- and C-terminal propeptides. Prolegumain is directed to the lysosome or plant vacuole, where activation occurs at least partially by autolysis. The N-terminal catalytic domain is a cysteine protease from the C13 family. The C-terminal prodomain can be organized into an activation peptide (AP), spanning a helical region, and a C-terminal death domain-like fold, denoted as legumain stabilization and activity modulation (LSAM) domain. The C-terminal prodomain binds over the active site and inhibits the catalytic domain. During activation, the C-terminal prodomain is autocatalytically cleaved. This process is induced by pH changes. Human legumain has been shown to process the tetanus toxin generating the fragments found in class II antigen presentation. Legumain from plant seeds is thought to be responsible for the post-translational processing of seed proteins prior to storage. Legumain is highly expressed in some cancers such as colorectal cancer (CRC) and uveal melanoma (UM); it is associated with poor outcome in CRC and upregulation of legumain is associated with malignant behavior of UM. Thus, legumain may be used as a negative prognostic factor as well as a therapeutic target.


:

Pssm-ID: 411051  Cd Length: 119  Bit Score: 174.02  E-value: 2.02e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187  311 DVPLTILKRKLLRTNDVKESQNLIGQIQQFLDARHVIEKSVHKIVSLLAGFGETAERHLSERTMLTAHDCYQEAVTHFRT 390
Cdd:cd21115   1 DVPLAILKRKLKKANDPEEKEELKKELEKLLQKREFIDETMKKIVKLVTGDEEEAERVLSTRRPLTDLDCYKEVVEHFRT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7242187  391 HCFNWHSvtYEHALRYLYVLANLCEAPYPIDRIEMAMDKVC 431
Cdd:cd21115  81 HCFNLSK--NPYALRHLYVLVNLCEEGYPAERIIAAMDKVC 119
 
Name Accession Description Interval E-value
Peptidase_C13 pfam01650
Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke ...
31-287 7.83e-161

Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke parasite Schistosoma mansoni has at least five Clan CA cysteine peptidases in its digestive tract including cathepsins B (2 isoforms), C, F and L. All have been recombinantly expressed as active enzymes, albeit in various stages of activation. In addition, a Clan CD peptidase, termed asparaginyl endopeptidase or 'legumain' has been identified. This has formerly been characterized as a 'haemoglobinase', but this term is probably incorrect. Two cDNAs have been described for Schistosoma mansoni legumain; one encodes an active enzyme whereas the active site cysteine residue encoded by the second cDNA is substituted by an asparagine residue. Both forms have been recombinantly expressed.


Pssm-ID: 396290  Cd Length: 257  Bit Score: 453.67  E-value: 7.83e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187     31 HWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVINRPNGTDVYKGVLKDYTGEDV 110
Cdd:pfam01650   1 LWAVLVAGSNGYYNYRHQADVCHAYQLLKKFGIKDENIIVMMYDDIANNPENPFPGKIFNKPNGTDVYKGVPKDYTGNDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187    111 TPENFLAVLRGDAEAVkgkGSGKVLKSGPRDHVFIYFTDHGATGILVFPN-DDLHVKDLNKTIRYMYEHKMYQKMVFYIE 189
Cdd:pfam01650  81 TPRNFLAVLLGDKSAL---GSGKVLKSGPNDNVFIYFTDHGAPGVLGFPElDYLYAKDLAEALKKMHARGKYKKLVFYVE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187    190 ACESGSMMNHLPDDINVYATTAANPKESSYACYY-DEERGTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSH 268
Cdd:pfam01650 158 ACESGSMFEGLPKDINVYATTAANADESSYGCYCpDPEDGTYLGDLFSVNWMEDSDDHDLSKETLEQQFELVKNRTTGSH 237
                         250
                  ....*....|....*....
gi 7242187    269 VMQYGNKSISTMKVMQFQG 287
Cdd:pfam01650 238 VMQYGDKSLPQLPLSLFQG 256
legumain_C cd21115
C-terminal prodomain of legumain; This family contains the C-terminal propeptide of legumain, ...
311-431 2.02e-53

C-terminal prodomain of legumain; This family contains the C-terminal propeptide of legumain, a lysosomal endopeptidase with a specificity for hydrolysis of asparaginyl bonds. Legumain (also called vacuolar processing enzyme or VPE in plants, and asparaginyl endopeptidase or AEP in animals) is synthesized as a precursor with both N- and C-terminal propeptides. Prolegumain is directed to the lysosome or plant vacuole, where activation occurs at least partially by autolysis. The N-terminal catalytic domain is a cysteine protease from the C13 family. The C-terminal prodomain can be organized into an activation peptide (AP), spanning a helical region, and a C-terminal death domain-like fold, denoted as legumain stabilization and activity modulation (LSAM) domain. The C-terminal prodomain binds over the active site and inhibits the catalytic domain. During activation, the C-terminal prodomain is autocatalytically cleaved. This process is induced by pH changes. Human legumain has been shown to process the tetanus toxin generating the fragments found in class II antigen presentation. Legumain from plant seeds is thought to be responsible for the post-translational processing of seed proteins prior to storage. Legumain is highly expressed in some cancers such as colorectal cancer (CRC) and uveal melanoma (UM); it is associated with poor outcome in CRC and upregulation of legumain is associated with malignant behavior of UM. Thus, legumain may be used as a negative prognostic factor as well as a therapeutic target.


Pssm-ID: 411051  Cd Length: 119  Bit Score: 174.02  E-value: 2.02e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187  311 DVPLTILKRKLLRTNDVKESQNLIGQIQQFLDARHVIEKSVHKIVSLLAGFGETAERHLSERTMLTAHDCYQEAVTHFRT 390
Cdd:cd21115   1 DVPLAILKRKLKKANDPEEKEELKKELEKLLQKREFIDETMKKIVKLVTGDEEEAERVLSTRRPLTDLDCYKEVVEHFRT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7242187  391 HCFNWHSvtYEHALRYLYVLANLCEAPYPIDRIEMAMDKVC 431
Cdd:cd21115  81 HCFNLSK--NPYALRHLYVLVNLCEEGYPAERIIAAMDKVC 119
GPI8 COG5206
Glycosylphosphatidylinositol transamidase (GPIT), subunit GPI8 [Posttranslational ...
31-254 3.87e-32

Glycosylphosphatidylinositol transamidase (GPIT), subunit GPI8 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227531  Cd Length: 382  Bit Score: 125.47  E-value: 3.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187   31 HWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVI-NRPNGTDVYKGVLK-DYTGE 108
Cdd:COG5206  29 NWAVLLSTSRFWFNYRHMANVLVFYRVVKRLGIPDSQIILMSYDDQACNSRNLFPGSVFnNSDRAGDLYGEDSEiDYSGY 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187  109 DVTPENFLAVLrgDAEAVKGKGSGKVLKSGPRDHVFIYFTDHGATGILVFPN-DDLHVKDLNKTIRYMYEHKMYQKMVFY 187
Cdd:COG5206 109 EVTVEVFIRLL--TARSGENHPKSKRLLTDESSNIFIYMTGHGGDAFLKFQDaEEMTSEDLADAISQLAAKKRYNEILFM 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187  188 IEACESGSMMN--HLPddiNVYATTAANPKESSYACYYDEERGTYLGD---WYSVNWMEDSD----------VEDLTKET 252
Cdd:COG5206 187 IDTCQANALYDksYSP---NVLAVGSSEIGQSSYSHHSDSLIGVAVIDrftYFFLKFLEKIDigskltlqdlLASLNKEP 263

                ..
gi 7242187  253 LH 254
Cdd:COG5206 264 IH 265
 
Name Accession Description Interval E-value
Peptidase_C13 pfam01650
Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke ...
31-287 7.83e-161

Peptidase C13 family; Members of this family are asparaginyl peptidases. The blood fluke parasite Schistosoma mansoni has at least five Clan CA cysteine peptidases in its digestive tract including cathepsins B (2 isoforms), C, F and L. All have been recombinantly expressed as active enzymes, albeit in various stages of activation. In addition, a Clan CD peptidase, termed asparaginyl endopeptidase or 'legumain' has been identified. This has formerly been characterized as a 'haemoglobinase', but this term is probably incorrect. Two cDNAs have been described for Schistosoma mansoni legumain; one encodes an active enzyme whereas the active site cysteine residue encoded by the second cDNA is substituted by an asparagine residue. Both forms have been recombinantly expressed.


Pssm-ID: 396290  Cd Length: 257  Bit Score: 453.67  E-value: 7.83e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187     31 HWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVINRPNGTDVYKGVLKDYTGEDV 110
Cdd:pfam01650   1 LWAVLVAGSNGYYNYRHQADVCHAYQLLKKFGIKDENIIVMMYDDIANNPENPFPGKIFNKPNGTDVYKGVPKDYTGNDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187    111 TPENFLAVLRGDAEAVkgkGSGKVLKSGPRDHVFIYFTDHGATGILVFPN-DDLHVKDLNKTIRYMYEHKMYQKMVFYIE 189
Cdd:pfam01650  81 TPRNFLAVLLGDKSAL---GSGKVLKSGPNDNVFIYFTDHGAPGVLGFPElDYLYAKDLAEALKKMHARGKYKKLVFYVE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187    190 ACESGSMMNHLPDDINVYATTAANPKESSYACYY-DEERGTYLGDWYSVNWMEDSDVEDLTKETLHKQYHLVKSHTNTSH 268
Cdd:pfam01650 158 ACESGSMFEGLPKDINVYATTAANADESSYGCYCpDPEDGTYLGDLFSVNWMEDSDDHDLSKETLEQQFELVKNRTTGSH 237
                         250
                  ....*....|....*....
gi 7242187    269 VMQYGNKSISTMKVMQFQG 287
Cdd:pfam01650 238 VMQYGDKSLPQLPLSLFQG 256
legumain_C cd21115
C-terminal prodomain of legumain; This family contains the C-terminal propeptide of legumain, ...
311-431 2.02e-53

C-terminal prodomain of legumain; This family contains the C-terminal propeptide of legumain, a lysosomal endopeptidase with a specificity for hydrolysis of asparaginyl bonds. Legumain (also called vacuolar processing enzyme or VPE in plants, and asparaginyl endopeptidase or AEP in animals) is synthesized as a precursor with both N- and C-terminal propeptides. Prolegumain is directed to the lysosome or plant vacuole, where activation occurs at least partially by autolysis. The N-terminal catalytic domain is a cysteine protease from the C13 family. The C-terminal prodomain can be organized into an activation peptide (AP), spanning a helical region, and a C-terminal death domain-like fold, denoted as legumain stabilization and activity modulation (LSAM) domain. The C-terminal prodomain binds over the active site and inhibits the catalytic domain. During activation, the C-terminal prodomain is autocatalytically cleaved. This process is induced by pH changes. Human legumain has been shown to process the tetanus toxin generating the fragments found in class II antigen presentation. Legumain from plant seeds is thought to be responsible for the post-translational processing of seed proteins prior to storage. Legumain is highly expressed in some cancers such as colorectal cancer (CRC) and uveal melanoma (UM); it is associated with poor outcome in CRC and upregulation of legumain is associated with malignant behavior of UM. Thus, legumain may be used as a negative prognostic factor as well as a therapeutic target.


Pssm-ID: 411051  Cd Length: 119  Bit Score: 174.02  E-value: 2.02e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187  311 DVPLTILKRKLLRTNDVKESQNLIGQIQQFLDARHVIEKSVHKIVSLLAGFGETAERHLSERTMLTAHDCYQEAVTHFRT 390
Cdd:cd21115   1 DVPLAILKRKLKKANDPEEKEELKKELEKLLQKREFIDETMKKIVKLVTGDEEEAERVLSTRRPLTDLDCYKEVVEHFRT 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7242187  391 HCFNWHSvtYEHALRYLYVLANLCEAPYPIDRIEMAMDKVC 431
Cdd:cd21115  81 HCFNLSK--NPYALRHLYVLVNLCEEGYPAERIIAAMDKVC 119
GPI8 COG5206
Glycosylphosphatidylinositol transamidase (GPIT), subunit GPI8 [Posttranslational ...
31-254 3.87e-32

Glycosylphosphatidylinositol transamidase (GPIT), subunit GPI8 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227531  Cd Length: 382  Bit Score: 125.47  E-value: 3.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187   31 HWVVIVAGSNGWYNYRHQADACHAYQIIHRNGIPDEQIIVMMYDDIANSEENPTPGVVI-NRPNGTDVYKGVLK-DYTGE 108
Cdd:COG5206  29 NWAVLLSTSRFWFNYRHMANVLVFYRVVKRLGIPDSQIILMSYDDQACNSRNLFPGSVFnNSDRAGDLYGEDSEiDYSGY 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187  109 DVTPENFLAVLrgDAEAVKGKGSGKVLKSGPRDHVFIYFTDHGATGILVFPN-DDLHVKDLNKTIRYMYEHKMYQKMVFY 187
Cdd:COG5206 109 EVTVEVFIRLL--TARSGENHPKSKRLLTDESSNIFIYMTGHGGDAFLKFQDaEEMTSEDLADAISQLAAKKRYNEILFM 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7242187  188 IEACESGSMMN--HLPddiNVYATTAANPKESSYACYYDEERGTYLGD---WYSVNWMEDSD----------VEDLTKET 252
Cdd:COG5206 187 IDTCQANALYDksYSP---NVLAVGSSEIGQSSYSHHSDSLIGVAVIDrftYFFLKFLEKIDigskltlqdlLASLNKEP 263

                ..
gi 7242187  253 LH 254
Cdd:COG5206 264 IH 265
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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