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Conserved domains on  [gi|9910516|ref|NP_064312|]
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kallikrein-4 precursor [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
32-251 7.62e-82

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 244.88  E-value: 7.62e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516   32 IIQGQDCSPHSQPWQAALFSEDG-FFCSGVLVHPQWVLSAAHCLQ----ESYIVGLGLHNLKgSQEPGSRMLEAHLSIQH 106
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYssapSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516  107 PNFNDPSFANDLMLIKLNESVIESNTIRSI--PVATQCPTPGDTCLVSGWGQLK-NGKLPSLLQCVNLSVASEETCRLLY 183
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPIclPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9910516  184 DPVYHL--SMFCAGGGQDQKDSCNGDSGGPIVCNRS----LQGLVSMGQGkCGQPGIPSVYTNLCKFTNWIQTI 251
Cdd:cd00190 160 SYGGTItdNMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
32-251 7.62e-82

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 244.88  E-value: 7.62e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516   32 IIQGQDCSPHSQPWQAALFSEDG-FFCSGVLVHPQWVLSAAHCLQ----ESYIVGLGLHNLKgSQEPGSRMLEAHLSIQH 106
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYssapSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516  107 PNFNDPSFANDLMLIKLNESVIESNTIRSI--PVATQCPTPGDTCLVSGWGQLK-NGKLPSLLQCVNLSVASEETCRLLY 183
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPIclPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9910516  184 DPVYHL--SMFCAGGGQDQKDSCNGDSGGPIVCNRS----LQGLVSMGQGkCGQPGIPSVYTNLCKFTNWIQTI 251
Cdd:cd00190 160 SYGGTItdNMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-248 8.21e-80

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 239.89  E-value: 8.21e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516      31 RIIQGQDCSPHSQPWQAALFSEDG-FFCSGVLVHPQWVLSAAHCLQ----ESYIVGLGLHNLkgSQEPGSRMLEAHLSIQ 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDL--SSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516     106 HPNFNDPSFANDLMLIKLNESVIESNTIRSI--PVATQCPTPGDTCLVSGWGQLKN--GKLPSLLQCVNLSVASEETCRL 181
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPIclPSSNYNVPAGTTCTVSGWGRTSEgaGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9910516     182 LYDPVYHL--SMFCAGGGQDQKDSCNGDSGGPIVCNRS---LQGLVSMGQGkCGQPGIPSVYTNLCKFTNWI 248
Cdd:smart00020 159 AYSGGGAItdNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
32-248 2.43e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 202.67  E-value: 2.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516     32 IIQGQDCSPHSQPWQAAL-FSEDGFFCSGVLVHPQWVLSAAHCL--QESYIVGLGLHNLKgSQEPGSRMLEAHLSIQHPN 108
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516    109 FNDPSFANDLMLIKLNESVIESNTIRSIPVATQCPT--PGDTCLVSGWGQLKNGKLPSLLQCVNLSVASEETCRLLYDPV 186
Cdd:pfam00089  80 YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9910516    187 YHLSMFCAGGGqdQKDSCNGDSGGPIVC-NRSLQGLVSMGQGkCGQPGIPSVYTNLCKFTNWI 248
Cdd:pfam00089 160 VTDTMICAGAG--GKDACQGDSGGPLVCsDGELIGIVSWGYG-CASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-255 2.42e-60

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 191.40  E-value: 2.42e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516    2 MVTARTPWGWFLGCLILEVTGASASSVSSRIIQGQDCSPHSQPWQAALFSEDG---FFCSGVLVHPQWVLSAAHCLQE-- 76
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDGdg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516   77 --SYIVGLGLHNLKGSqepGSRMLEAHLSIQHPNFNDPSFANDLMLIKLNESViesNTIRSIPVAT--QCPTPGDTCLVS 152
Cdd:COG5640  81 psDLRVVIGSTDLSTS---GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATsaDAAAPGTPATVA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516  153 GWGQLKN--GKLPSLLQCVNLSVASEETCRlLYDPVYHLSMFCAGGGQDQKDSCNGDSGGPIVCNRS----LQGLVSMGQ 226
Cdd:COG5640 155 GWGRTSEgpGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGggwvLVGVVSWGG 233
                       250       260
                ....*....|....*....|....*....
gi 9910516  227 GKCGqPGIPSVYTNLCKFTNWIQTIIQTN 255
Cdd:COG5640 234 GPCA-AGYPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
32-251 7.62e-82

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 244.88  E-value: 7.62e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516   32 IIQGQDCSPHSQPWQAALFSEDG-FFCSGVLVHPQWVLSAAHCLQ----ESYIVGLGLHNLKgSQEPGSRMLEAHLSIQH 106
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGrHFCGGSLISPRWVLTAAHCVYssapSNYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516  107 PNFNDPSFANDLMLIKLNESVIESNTIRSI--PVATQCPTPGDTCLVSGWGQLK-NGKLPSLLQCVNLSVASEETCRLLY 183
Cdd:cd00190  80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPIclPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAY 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9910516  184 DPVYHL--SMFCAGGGQDQKDSCNGDSGGPIVCNRS----LQGLVSMGQGkCGQPGIPSVYTNLCKFTNWIQTI 251
Cdd:cd00190 160 SYGGTItdNMLCAGGLEGGKDACQGDSGGPLVCNDNgrgvLVGIVSWGSG-CARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-248 8.21e-80

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 239.89  E-value: 8.21e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516      31 RIIQGQDCSPHSQPWQAALFSEDG-FFCSGVLVHPQWVLSAAHCLQ----ESYIVGLGLHNLkgSQEPGSRMLEAHLSIQ 105
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVRgsdpSNIRVRLGSHDL--SSGEEGQVIKVSKVII 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516     106 HPNFNDPSFANDLMLIKLNESVIESNTIRSI--PVATQCPTPGDTCLVSGWGQLKN--GKLPSLLQCVNLSVASEETCRL 181
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPIclPSSNYNVPAGTTCTVSGWGRTSEgaGSLPDTLQEVNVPIVSNATCRR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9910516     182 LYDPVYHL--SMFCAGGGQDQKDSCNGDSGGPIVCNRS---LQGLVSMGQGkCGQPGIPSVYTNLCKFTNWI 248
Cdd:smart00020 159 AYSGGGAItdNMLCAGGLEGGKDACQGDSGGPLVCNDGrwvLVGIVSWGSG-CARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
32-248 2.43e-65

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 202.67  E-value: 2.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516     32 IIQGQDCSPHSQPWQAAL-FSEDGFFCSGVLVHPQWVLSAAHCL--QESYIVGLGLHNLKgSQEPGSRMLEAHLSIQHPN 108
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVsgASDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516    109 FNDPSFANDLMLIKLNESVIESNTIRSIPVATQCPT--PGDTCLVSGWGQLKNGKLPSLLQCVNLSVASEETCRLLYDPV 186
Cdd:pfam00089  80 YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9910516    187 YHLSMFCAGGGqdQKDSCNGDSGGPIVC-NRSLQGLVSMGQGkCGQPGIPSVYTNLCKFTNWI 248
Cdd:pfam00089 160 VTDTMICAGAG--GKDACQGDSGGPLVCsDGELIGIVSWGYG-CASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-255 2.42e-60

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 191.40  E-value: 2.42e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516    2 MVTARTPWGWFLGCLILEVTGASASSVSSRIIQGQDCSPHSQPWQAALFSEDG---FFCSGVLVHPQWVLSAAHCLQE-- 76
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGpsgQFCGGTLIAPRWVLTAAHCVDGdg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516   77 --SYIVGLGLHNLKGSqepGSRMLEAHLSIQHPNFNDPSFANDLMLIKLNESViesNTIRSIPVAT--QCPTPGDTCLVS 152
Cdd:COG5640  81 psDLRVVIGSTDLSTS---GGTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLATsaDAAAPGTPATVA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516  153 GWGQLKN--GKLPSLLQCVNLSVASEETCRlLYDPVYHLSMFCAGGGQDQKDSCNGDSGGPIVCNRS----LQGLVSMGQ 226
Cdd:COG5640 155 GWGRTSEgpGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGggwvLVGVVSWGG 233
                       250       260
                ....*....|....*....|....*....
gi 9910516  227 GKCGqPGIPSVYTNLCKFTNWIQTIIQTN 255
Cdd:COG5640 234 GPCA-AGYPGVYTRVSAYRDWIKSTAGGL 261
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
54-235 3.32e-08

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 52.37  E-value: 3.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516   54 GFFCSGVLVHPQWVLSAAHCLQ--------ESYIVGLGLHNLKGSQEPGSRMLEahlsiqHPNF-NDPSFANDLMLIKLN 124
Cdd:COG3591  11 GGVCTGTLIGPNLVLTAGHCVYdgagggwaTNIVFVPGYNGGPYGTATATRFRV------PPGWvASGDAGYDYALLRLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910516  125 ESVieSNTIRSIPVATQ-CPTPGDTCLVSGWGQLKNGKLpsllqcvnlsvASEETCRLLYDPVYHLSMFCagggqdqkDS 203
Cdd:COG3591  85 EPL--GDTTGWLGLAFNdAPLAGEPVTIIGYPGDRPKDL-----------SLDCSGRVTGVQGNRLSYDC--------DT 143
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 9910516  204 CNGDSGGPIVCNRSLQ----GLVSMGQGKCGQPGIP 235
Cdd:COG3591 144 TGGSSGSPVLDDSDGGgrvvGVHSAGGADRANTGVR 179
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
206-239 6.42e-03

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 36.52  E-value: 6.42e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 9910516  206 GDSGGPIVCNRSLQGLVSMGQGKCGQPGIPSVYT 239
Cdd:cd21112 145 GDSGGPVFSGTQALGITSGGSGNCGSGGGTSYFQ 178
 
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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