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Conserved domains on  [gi|755521206|ref|XP_011249189|]
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kallikrein-13 isoform X2 [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
39-168 1.25e-48

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: 157.44  E-value: 1.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206  39 GGYTCLPHSQPWQAALLIR-GRLLCGGVLVHPKWVLTAAHC----RKDGYTVHLGKHALGRVENGEQAMEVVRSIPHPEY 113
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755521206 114 QVTpthlNHDHDIMLLELKSPVQLSSHVRTLKL-SADDCLPTGTCCRVSGWGTTTS 168
Cdd:cd00190   83 NPS----TYDNDIALLKLKRPVTLSDNVRPICLpSSGYNLPAGTTCTVSGWGRTSE 134
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
39-168 1.25e-48

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: 157.44  E-value: 1.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206  39 GGYTCLPHSQPWQAALLIR-GRLLCGGVLVHPKWVLTAAHC----RKDGYTVHLGKHALGRVENGEQAMEVVRSIPHPEY 113
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755521206 114 QVTpthlNHDHDIMLLELKSPVQLSSHVRTLKL-SADDCLPTGTCCRVSGWGTTTS 168
Cdd:cd00190   83 NPS----TYDNDIALLKLKRPVTLSDNVRPICLpSSGYNLPAGTTCTVSGWGRTSE 134
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
39-174 7.46e-46

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: 150.14  E-value: 7.46e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206    39 GGYTCLPHSQPWQAALLIRG-RLLCGGVLVHPKWVLTAAHC----RKDGYTVHLGKHALgRVENGEQAMEVVRSIPHPEY 113
Cdd:smart00020   4 GGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDL-SSGEEGQVIKVSKVIIHPNY 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755521206   114 QVTpthlNHDHDIMLLELKSPVQLSSHVRTLKL-SADDCLPTGTCCRVSGWGTTTSPQGQAS 174
Cdd:smart00020  83 NPS----TYDNDIALLKLKEPVTLSDNVRPICLpSSNYNVPAGTTCTVSGWGRTSEGAGSLP 140
Trypsin pfam00089
Trypsin;
39-166 4.05e-38

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 130.25  E-value: 4.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206   39 GGYTCLPHSQPWQAALLIR-GRLLCGGVLVHPKWVLTAAHCRKDG--YTVHLGKHALGRVENGEQAMEVVRSIPHPEYqv 115
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY-- 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755521206  116 tpTHLNHDHDIMLLELKSPVQLSSHVRTLKL-SADDCLPTGTCCRVSGWGTT 166
Cdd:pfam00089  81 --NPDTLDNDIALLKLESPVTLGDTVRPICLpDASSDLPVGTTCTVSGWGNT 130
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-174 4.18e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 97.41  E-value: 4.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206   1 MWPLVATIACLTLALSEGISRDyPKILNGTNGTSGflpggytclphSQPWQAALLIRG---RLLCGGVLVHPKWVLTAAH 77
Cdd:COG5640    7 LAALAAAALALALAAAPAADAA-PAIVGGTPATVG-----------EYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206  78 C----RKDGYTVHLGKHALGrvENGEQAMEVVRSIPHPEYQVTPThlnhDHDIMLLELKSPVqlsSHVRTLKL-SADDCL 152
Cdd:COG5640   75 CvdgdGPSDLRVVIGSTDLS--TSGGTVVKVARIVVHPDYDPATP----GNDIALLKLATPV---PGVAPAPLaTSADAA 145
                        170       180
                 ....*....|....*....|..
gi 755521206 153 PTGTCCRVSGWGTTTSPQGQAS 174
Cdd:COG5640  146 APGTPATVAGWGRTSEGPGSQS 167
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
39-168 1.25e-48

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: 157.44  E-value: 1.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206  39 GGYTCLPHSQPWQAALLIR-GRLLCGGVLVHPKWVLTAAHC----RKDGYTVHLGKHALGRVENGEQAMEVVRSIPHPEY 113
Cdd:cd00190    3 GGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNY 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755521206 114 QVTpthlNHDHDIMLLELKSPVQLSSHVRTLKL-SADDCLPTGTCCRVSGWGTTTS 168
Cdd:cd00190   83 NPS----TYDNDIALLKLKRPVTLSDNVRPICLpSSGYNLPAGTTCTVSGWGRTSE 134
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
39-174 7.46e-46

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: 150.14  E-value: 7.46e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206    39 GGYTCLPHSQPWQAALLIRG-RLLCGGVLVHPKWVLTAAHC----RKDGYTVHLGKHALgRVENGEQAMEVVRSIPHPEY 113
Cdd:smart00020   4 GGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDL-SSGEEGQVIKVSKVIIHPNY 82
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755521206   114 QVTpthlNHDHDIMLLELKSPVQLSSHVRTLKL-SADDCLPTGTCCRVSGWGTTTSPQGQAS 174
Cdd:smart00020  83 NPS----TYDNDIALLKLKEPVTLSDNVRPICLpSSNYNVPAGTTCTVSGWGRTSEGAGSLP 140
Trypsin pfam00089
Trypsin;
39-166 4.05e-38

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 130.25  E-value: 4.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206   39 GGYTCLPHSQPWQAALLIR-GRLLCGGVLVHPKWVLTAAHCRKDG--YTVHLGKHALGRVENGEQAMEVVRSIPHPEYqv 115
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGAsdVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY-- 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755521206  116 tpTHLNHDHDIMLLELKSPVQLSSHVRTLKL-SADDCLPTGTCCRVSGWGTT 166
Cdd:pfam00089  81 --NPDTLDNDIALLKLESPVTLGDTVRPICLpDASSDLPVGTTCTVSGWGNT 130
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-174 4.18e-25

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 97.41  E-value: 4.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206   1 MWPLVATIACLTLALSEGISRDyPKILNGTNGTSGflpggytclphSQPWQAALLIRG---RLLCGGVLVHPKWVLTAAH 77
Cdd:COG5640    7 LAALAAAALALALAAAPAADAA-PAIVGGTPATVG-----------EYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206  78 C----RKDGYTVHLGKHALGrvENGEQAMEVVRSIPHPEYQVTPThlnhDHDIMLLELKSPVqlsSHVRTLKL-SADDCL 152
Cdd:COG5640   75 CvdgdGPSDLRVVIGSTDLS--TSGGTVVKVARIVVHPDYDPATP----GNDIALLKLATPV---PGVAPAPLaTSADAA 145
                        170       180
                 ....*....|....*....|..
gi 755521206 153 PTGTCCRVSGWGTTTSPQGQAS 174
Cdd:COG5640  146 APGTPATVAGWGRTSEGPGSQS 167
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
49-141 3.81e-06

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 44.08  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206   49 PWQAALLIRGRLLCGGVLVHPKWVLTAAHCRKDgytVHLGKHALGRVENGEQAMEVVRSiPHPE-YQVTPTHLNHDHDIM 127
Cdd:pfam09342   2 PWIAKVYLDGNMICSGVLIDASWVIVSGSCLRD---TNLRHQYISVVLGGAKTLKSIEG-PYEQiVRVDCRHDIPESEIS 77
                          90
                  ....*....|....
gi 755521206  128 LLELKSPVQLSSHV 141
Cdd:pfam09342  78 LLHLASPASFSNHV 91
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
64-163 8.81e-03

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 35.09  E-value: 8.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755521206   64 GVLVHP-KWVLTAAHCrkdgytvhlgkhaLGRVENGEQAMEVVRSIPHPEYQVTPTHLNHDHDIMLLELKSPvqlSSHVR 142
Cdd:pfam13365   3 GFVVSSdGLVLTNAHV-------------VDDAEEAAVELVSVVLADGREYPATVVARDPDLDLALLRVSGD---GRGLP 66
                          90       100
                  ....*....|....*....|.
gi 755521206  143 TLKLSADDCLPTGTCCRVSGW 163
Cdd:pfam13365  67 PLPLGDSEPLVGGERVYAVGY 87
 
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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