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Conserved domains on  [gi|1958803037|ref|XP_038939764|]
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serine protease 40 isoform X6 [Rattus norvegicus]

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 ...
72-202 1.25e-40

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: 138.95  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037  72 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYNELSNPSNYSRQMTLSKVIVH 150
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958803037 151 EDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWG 202
Cdd:cd00190    80 PNYNPSTY-DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG 130
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
72-202 1.25e-40

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: 138.95  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037  72 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYNELSNPSNYSRQMTLSKVIVH 150
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958803037 151 EDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWG 202
Cdd:cd00190    80 PNYNPSTY-DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG 130
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
71-226 5.77e-38

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: 132.03  E-value: 5.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037   71 KIYGGSIAKAERWPWQASLIFRG-RHICGAVLIDKNWVASAAHCFkRSLKPSDYRILLGYNELSNPsNYSRQMTLSKVIV 149
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958803037  150 HEDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGmvtdDRSLTFLTGSRRKRQTRLTL 226
Cdd:smart00020  79 HPNYNPSTY-DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPI 150
Trypsin pfam00089
Trypsin;
72-202 3.69e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 111.77  E-value: 3.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037  72 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlkpSDYRILLGYNELSNPSNYSRQMTLSKVIVH 150
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958803037 151 EDYNKLhSQEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWG 202
Cdd:pfam00089  78 PNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG 128
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
54-230 2.08e-26

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 102.81  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037  54 LVAGIVSTVCGKTKFQGKIYGGSIAKAERWPWQASLIFRG---RHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYN 130
Cdd:COG5640    13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGST 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037 131 ELSNPSNYSRqmTLSKVIVHEDYNKlHSQEKDIVLIQLHLPVRYSShifPVCVPDQTTKEPSDESCWISGWGMVTDDRSl 210
Cdd:COG5640    92 DLSTSGGTVV--KVARIVVHPDYDP-ATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG- 164
                         170       180
                  ....*....|....*....|
gi 1958803037 211 tflTGSRRKRQTRLTLTPPS 230
Cdd:COG5640   165 ---SQSGTLRKADVPVVSDA 181
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
72-202 1.25e-40

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: 138.95  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037  72 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYNELSNPSNYSRQMTLSKVIVH 150
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958803037 151 EDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWG 202
Cdd:cd00190    80 PNYNPSTY-DNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWG 130
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
71-226 5.77e-38

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: 132.03  E-value: 5.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037   71 KIYGGSIAKAERWPWQASLIFRG-RHICGAVLIDKNWVASAAHCFkRSLKPSDYRILLGYNELSNPsNYSRQMTLSKVIV 149
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958803037  150 HEDYNKLHSqEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWGmvtdDRSLTFLTGSRRKRQTRLTL 226
Cdd:smart00020  79 HPNYNPSTY-DNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWG----RTSEGAGSLPDTLQEVNVPI 150
Trypsin pfam00089
Trypsin;
72-202 3.69e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 111.77  E-value: 3.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037  72 IYGGSIAKAERWPWQASLIFR-GRHICGAVLIDKNWVASAAHCFKRSlkpSDYRILLGYNELSNPSNYSRQMTLSKVIVH 150
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA---SDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958803037 151 EDYNKLhSQEKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESCWISGWG 202
Cdd:pfam00089  78 PNYNPD-TLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG 128
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
54-230 2.08e-26

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 102.81  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037  54 LVAGIVSTVCGKTKFQGKIYGGSIAKAERWPWQASLIFRG---RHICGAVLIDKNWVASAAHCFKRSlKPSDYRILLGYN 130
Cdd:COG5640    13 AALALALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD-GPSDLRVVIGST 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037 131 ELSNPSNYSRqmTLSKVIVHEDYNKlHSQEKDIVLIQLHLPVRYSShifPVCVPDQTTKEPSDESCWISGWGMVTDDRSl 210
Cdd:COG5640    92 DLSTSGGTVV--KVARIVVHPDYDP-ATPGNDIALLKLATPVPGVA---PAPLATSADAAAPGTPATVAGWGRTSEGPG- 164
                         170       180
                  ....*....|....*....|
gi 1958803037 211 tflTGSRRKRQTRLTLTPPS 230
Cdd:COG5640   165 ---SQSGTLRKADVPVVSDA 181
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
83-196 8.17e-09

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: 52.16  E-value: 8.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958803037  83 WPWQASLIFRGRHICGAVLIDKNWVASAAHCFKR-SLKPSDYRILLGYNE--LSNPSNYSRqmtLSKVIVHEDYnklhsQ 159
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDtNLRHQYISVVLGGAKtlKSIEGPYEQ---IVRVDCRHDI-----P 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1958803037 160 EKDIVLIQLHLPVRYSSHIFPVCVPDQTTKEPSDESC 196
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNENEKDNEC 109
 
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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