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Conserved domains on  [gi|2066300703|ref|NP_001382431|]
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serine protease 41 isoform 4 precursor [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 ...
42-181 3.79e-43

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: 146.27  E-value: 3.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703  42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 117
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2066300703 118 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGS 181
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP 137
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-181 3.79e-43

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: 146.27  E-value: 3.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703  42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 117
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2066300703 118 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGS 181
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP 137
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-180 1.11e-41

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: 142.43  E-value: 1.11e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703   42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrpTPWNLRAYSSRYKVQD 120
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGS-----HDLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2066300703  121 IIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSG 180
Cdd:smart00020  76 VIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGA 136
Trypsin pfam00089
Trypsin;
44-181 8.86e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 111.38  E-value: 8.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703  44 GGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFqkhYYPSEWTVQLGELTSRPTpwnlRAYSSRYKVQDII 122
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLR----EGGEQKFDVEKII 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703 123 VNPDALGV-LRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGS 181
Cdd:pfam00089  76 VHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP 135
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
32-186 8.27e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 93.95  E-value: 8.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703  32 ACGHREIHALVAGGVESARGRWPWQASLRLR---RRHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGELTSRPTPwn 108
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSG-- 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2066300703 109 lraySSRYKVQDIIVNPD-ALGVLRNDIALLRLASSVTYNAYIQpicIESSTFNFVHRPDCWVTGWGLISPSGSEAGDR 186
Cdd:COG5640    98 ----GTVVKVARIVVHPDyDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGT 169
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-181 3.79e-43

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: 146.27  E-value: 3.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703  42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrptpWNLRAYSS---RYK 117
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGgRHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGS-------HDLSSNEGggqVIK 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2066300703 118 VQDIIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGS 181
Cdd:cd00190    73 VKKVIVHPNYnPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP 137
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
42-180 1.11e-41

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: 142.43  E-value: 1.11e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703   42 VAGGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGEltsrpTPWNLRAYSSRYKVQD 120
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGS-----HDLSSGEEGQVIKVSK 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2066300703  121 IIVNPDA-LGVLRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSG 180
Cdd:smart00020  76 VIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGA 136
Trypsin pfam00089
Trypsin;
44-181 8.86e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 111.38  E-value: 8.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703  44 GGVESARGRWPWQASLRLRR-RHRCGGSLLSRRWVLSAAHCFqkhYYPSEWTVQLGELTSRPTpwnlRAYSSRYKVQDII 122
Cdd:pfam00089   3 GGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLR----EGGEQKFDVEKII 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703 123 VNPDALGV-LRNDIALLRLASSVTYNAYIQPICIESSTFNFVHRPDCWVTGWGLISPSGS 181
Cdd:pfam00089  76 VHPNYNPDtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP 135
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
32-186 8.27e-23

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 93.95  E-value: 8.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2066300703  32 ACGHREIHALVAGGVESARGRWPWQASLRLR---RRHRCGGSLLSRRWVLSAAHCFQKhYYPSEWTVQLGELTSRPTPwn 108
Cdd:COG5640    21 AAPAADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSG-- 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2066300703 109 lraySSRYKVQDIIVNPD-ALGVLRNDIALLRLASSVTYNAYIQpicIESSTFNFVHRPDCWVTGWGLISPSGSEAGDR 186
Cdd:COG5640    98 ----GTVVKVARIVVHPDyDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTSEGPGSQSGT 169
 
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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