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Conserved domains on  [gi|768012287|ref|XP_011525847|]
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kallikrein-4 isoform X1 [Homo sapiens]

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 ...
31-159 7.60e-42

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: 139.33  E-value: 7.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287  31 IINGEDCSPHSQPWQAALVME-NELFCSGVLVHPQWVLSAAHCFQNS----YTIGLGLHSLEaDQEPGSQMVEASLSVRH 105
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768012287 106 PEYNRPLLANDLMLIKLDESVSESDTIRSISIASQ--CPTAGNSCLVSGWGLLANE 159
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEG 135
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-159 7.60e-42

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: 139.33  E-value: 7.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287  31 IINGEDCSPHSQPWQAALVME-NELFCSGVLVHPQWVLSAAHCFQNS----YTIGLGLHSLEaDQEPGSQMVEASLSVRH 105
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768012287 106 PEYNRPLLANDLMLIKLDESVSESDTIRSISIASQ--CPTAGNSCLVSGWGLLANE 159
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEG 135
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-162 4.92e-40

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: 134.73  E-value: 4.92e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287    31 IINGEDCSPHSQPWQAALVMEN-ELFCSGVLVHPQWVLSAAHCFQN----SYTIGLGLHSLEadQEPGSQMVEASLSVRH 105
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdpsNIRVRLGSHDLS--SGEEGQVIKVSKVIIH 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 768012287   106 PEYNRPLLANDLMLIKLDESVSESDTIRSISIAS--QCPTAGNSCLVSGWGLLANECLP 162
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGS 138
Trypsin pfam00089
Trypsin;
31-158 1.66e-33

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 117.93  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287   31 IINGEDCSPHSQPWQAALVME-NELFCSGVLVHPQWVLSAAHCFQN--SYTIGLGLHSLEaDQEPGSQMVEASLSVRHPE 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGasDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768012287  108 YNRPLLANDLMLIKLDESVSESDTIRSISIASQCPT--AGNSCLVSGWGLLAN 158
Cdd:pfam00089  80 YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWGNTKT 132
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-155 1.15e-28

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 106.27  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287   1 MATAGNPWGWFLGYLILGVAGSLVSGSCSQIINGEDCSPHSQPWQAALVMENEL---FCSGVLVHPQWVLSAAHCFQN-- 75
Cdd:COG5640    1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGdg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287  76 --SYTIGLGLHSLEADqepGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRsISIASQCPTAGNSCLVSGW 153
Cdd:COG5640   81 psDLRVVIGSTDLSTS---GGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP-LATSADAAAPGTPATVAGW 156

                 ..
gi 768012287 154 GL 155
Cdd:COG5640  157 GR 158
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
31-159 7.60e-42

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: 139.33  E-value: 7.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287  31 IINGEDCSPHSQPWQAALVME-NELFCSGVLVHPQWVLSAAHCFQNS----YTIGLGLHSLEaDQEPGSQMVEASLSVRH 105
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSapsnYTVRLGSHDLS-SNEGGGQVIKVKKVIVH 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768012287 106 PEYNRPLLANDLMLIKLDESVSESDTIRSISIASQ--CPTAGNSCLVSGWGLLANE 159
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEG 135
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
31-162 4.92e-40

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: 134.73  E-value: 4.92e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287    31 IINGEDCSPHSQPWQAALVMEN-ELFCSGVLVHPQWVLSAAHCFQN----SYTIGLGLHSLEadQEPGSQMVEASLSVRH 105
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGsdpsNIRVRLGSHDLS--SGEEGQVIKVSKVIIH 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 768012287   106 PEYNRPLLANDLMLIKLDESVSESDTIRSISIAS--QCPTAGNSCLVSGWGLLANECLP 162
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGS 138
Trypsin pfam00089
Trypsin;
31-158 1.66e-33

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 117.93  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287   31 IINGEDCSPHSQPWQAALVME-NELFCSGVLVHPQWVLSAAHCFQN--SYTIGLGLHSLEaDQEPGSQMVEASLSVRHPE 107
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGasDVKVVLGAHNIV-LREGGEQKFDVEKIIVHPN 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 768012287  108 YNRPLLANDLMLIKLDESVSESDTIRSISIASQCPT--AGNSCLVSGWGLLAN 158
Cdd:pfam00089  80 YNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDlpVGTTCTVSGWGNTKT 132
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-155 1.15e-28

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 106.27  E-value: 1.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287   1 MATAGNPWGWFLGYLILGVAGSLVSGSCSQIINGEDCSPHSQPWQAALVMENEL---FCSGVLVHPQWVLSAAHCFQN-- 75
Cdd:COG5640    1 MRRRRLLAALAAAALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPsgqFCGGTLIAPRWVLTAAHCVDGdg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287  76 --SYTIGLGLHSLEADqepGSQMVEASLSVRHPEYNRPLLANDLMLIKLDESVSESDTIRsISIASQCPTAGNSCLVSGW 153
Cdd:COG5640   81 psDLRVVIGSTDLSTS---GGTVVKVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP-LATSADAAAPGTPATVAGW 156

                 ..
gi 768012287 154 GL 155
Cdd:COG5640  157 GR 158
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
55-129 8.76e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 35.42  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012287  55 FCSGVLVHPQWVLSAAHCFQNSYTiGLGLHSLEA----DQEPGSQMVEASLSVrHPEY-NRPLLANDLMLIKLDESVSES 129
Cdd:COG3591   13 VCTGTLIGPNLVLTAGHCVYDGAG-GGWATNIVFvpgyNGGPYGTATATRFRV-PPGWvASGDAGYDYALLRLDEPLGDT 90
 
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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