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Conserved domains on  [gi|1958732857|ref|XP_038952287|]
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putative serine protease 47 isoform X9 [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.-
Gene Ontology:  GO:0008236|GO:0008233|GO:0006508|GO:0004252
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 ...
 36-134 4.36e-36

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: 125.47  E-value: 4.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857  36 PFSLQEGEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCRPS 115
Cdd:cd00190   139 PDVLQEVNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP 213

                          90
                  ....*....|....*....
gi 1958732857 116 IYPSVFTRVTYFTDWISQV 134
Cdd:cd00190   214 NYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 36-134 4.36e-36

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: 125.47  E-value: 4.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857  36 PFSLQEGEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCRPS 115
Cdd:cd00190   139 PDVLQEVNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP 213

                          90
                  ....*....|....*....
gi 1958732857 116 IYPSVFTRVTYFTDWISQV 134
Cdd:cd00190   214 NYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 35-131 2.84e-33

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: 118.16  E-value: 2.84e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857   35 PPFSLQEGEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCyHISAWVLVGLASWGLDCRP 114
Cdd:smart00020 139 LPDTLQEVNVPIVSNATCRRAYSGG-----GAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCAR 212

                           90
                   ....*....|....*..
gi 1958732857  115 SIYPSVFTRVTYFTDWI 131
Cdd:smart00020 213 PGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
35-131 6.92e-25

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 96.36  E-value: 6.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857  35 PPFSLQEGEVGIIENEFCNALYGqrlgqsrNYVHEEMLCAGGlsTGKSICRGDSGGPLVCyhiSAWVLVGLASWGLDCRP 114
Cdd:pfam00089 135 PSDTLQEVTVPVVSRETCRSAYG-------GTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCAS 202

                          90
                  ....*....|....*..
gi 1958732857 115 SIYPSVFTRVTYFTDWI 131
Cdd:pfam00089 203 GNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 39-134 4.68e-24

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 95.10  E-value: 4.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857  39 LQEGEVGIIENEFCNALYGqrlgqsrnYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGL-DCRPSiY 117
Cdd:COG5640   170 LRKADVPVVSDATCAAYGG--------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCAAG-Y 240

                          90
                  ....*....|....*..
gi 1958732857 118 PSVFTRVTYFTDWISQV 134
Cdd:COG5640   241 PGVYTRVSAYRDWIKST 257
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 36-134 4.36e-36

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: 125.47  E-value: 4.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857  36 PFSLQEGEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGLDCRPS 115
Cdd:cd00190   139 PDVLQEVNVPIVSNAECKRAYSYG-----GTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARP 213

                          90
                  ....*....|....*....
gi 1958732857 116 IYPSVFTRVTYFTDWISQV 134
Cdd:cd00190   214 NYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 35-131 2.84e-33

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: 118.16  E-value: 2.84e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857   35 PPFSLQEGEVGIIENEFCNALYGQRlgqsrNYVHEEMLCAGGLSTGKSICRGDSGGPLVCyHISAWVLVGLASWGLDCRP 114
Cdd:smart00020 139 LPDTLQEVNVPIVSNATCRRAYSGG-----GAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCAR 212

                           90
                   ....*....|....*..
gi 1958732857  115 SIYPSVFTRVTYFTDWI 131
Cdd:smart00020 213 PGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
35-131 6.92e-25

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 96.36  E-value: 6.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857  35 PPFSLQEGEVGIIENEFCNALYGqrlgqsrNYVHEEMLCAGGlsTGKSICRGDSGGPLVCyhiSAWVLVGLASWGLDCRP 114
Cdd:pfam00089 135 PSDTLQEVTVPVVSRETCRSAYG-------GTVTDTMICAGA--GGKDACQGDSGGPLVC---SDGELIGIVSWGYGCAS 202

                          90
                  ....*....|....*..
gi 1958732857 115 SIYPSVFTRVTYFTDWI 131
Cdd:pfam00089 203 GNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 39-134 4.68e-24

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 95.10  E-value: 4.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958732857  39 LQEGEVGIIENEFCNALYGqrlgqsrnYVHEEMLCAGGLSTGKSICRGDSGGPLVCYHISAWVLVGLASWGL-DCRPSiY 117
Cdd:COG5640   170 LRKADVPVVSDATCAAYGG--------FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGgPCAAG-Y 240

                          90
                  ....*....|....*..
gi 1958732857 118 PSVFTRVTYFTDWISQV 134
Cdd:COG5640   241 PGVYTRVSAYRDWIKST 257
 
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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