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Conserved domains on  [gi|281427284|ref|NP_699193|]
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inactive serine protease 35 precursor [Homo sapiens]

Protein Classification

trypsin-like serine peptidase( domain architecture ID 10007588)

trypsin-like serine protease catalyzes the cleavage of specific peptide bonds in protein substrates using an active site serine as the nucleophile

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  7845208|7733651
SCOP:  3000114

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
154-403 4.25e-20

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


:

Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 87.42  E-value: 4.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 154 CSGILISPQHVLTAAHCVHDGKDyvkgskklrvgllkmrnksggkkrrgskrsrreasggdqrEGTREHLRERAkgGRRR 233
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAG----------------------------------------GGWATNIVFVP--GYNG 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 234 KKSGrgqriaegrpsfqWTRVKNTHIPKGWARGGMGdatlDYDYALLELKRAHKKKYMELGISPTIKKMPGGMIHFSGFD 313
Cdd:COG3591   52 GPYG-------------TATATRFRVPPGWVASGDA----GYDYALLRLDEPLGDTTGWLGLAFNDAPLAGEPVTIIGYP 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 314 NDRADQL-VYRFCSVSDESNDLLYQYCDAESGSTGSGVYlrlkdpDKKNWKRKIIAVYSGhqwvdvhGVQKDYNVAVRIT 392
Cdd:COG3591  115 GDRPKDLsLDCSGRVTGVQGNRLSYDCDTTGGSSGSPVL------DDSDGGGRVVGVHSA-------GGADRANTGVRLT 181
                        250
                 ....*....|.
gi 281427284 393 PLKYAQICLWI 403
Cdd:COG3591  182 SAIVAALRAWA 192
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
141-187 5.17e-07

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.


The actual alignment was detected with superfamily member cd00190:

Pssm-ID: 473915 [Multi-domain]  Cd Length: 232  Bit Score: 50.35  E-value: 5.17e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 281427284 141 NFPFSTAVKLSTG---CSGILISPQHVLTAAHCVHdgkDYVKGSKKLRVG 187
Cdd:cd00190   11 SFPWQVSLQYTGGrhfCGGSLISPRWVLTAAHCVY---SSAPSNYTVRLG 57
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
154-403 4.25e-20

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 87.42  E-value: 4.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 154 CSGILISPQHVLTAAHCVHDGKDyvkgskklrvgllkmrnksggkkrrgskrsrreasggdqrEGTREHLRERAkgGRRR 233
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAG----------------------------------------GGWATNIVFVP--GYNG 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 234 KKSGrgqriaegrpsfqWTRVKNTHIPKGWARGGMGdatlDYDYALLELKRAHKKKYMELGISPTIKKMPGGMIHFSGFD 313
Cdd:COG3591   52 GPYG-------------TATATRFRVPPGWVASGDA----GYDYALLRLDEPLGDTTGWLGLAFNDAPLAGEPVTIIGYP 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 314 NDRADQL-VYRFCSVSDESNDLLYQYCDAESGSTGSGVYlrlkdpDKKNWKRKIIAVYSGhqwvdvhGVQKDYNVAVRIT 392
Cdd:COG3591  115 GDRPKDLsLDCSGRVTGVQGNRLSYDCDTTGGSSGSPVL------DDSDGGGRVVGVHSA-------GGADRANTGVRLT 181
                        250
                 ....*....|.
gi 281427284 393 PLKYAQICLWI 403
Cdd:COG3591  182 SAIVAALRAWA 192
Trypsin pfam00089
Trypsin;
141-177 8.53e-08

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 52.44  E-value: 8.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 281427284  141 NFPFSTAVKLSTG---CSGILISPQHVLTAAHCVHDGKDY 177
Cdd:pfam00089  11 SFPWQVSLQLSSGkhfCGGSLISENWVLTAAHCVSGASDV 50
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
141-187 5.17e-07

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: 50.35  E-value: 5.17e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 281427284 141 NFPFSTAVKLSTG---CSGILISPQHVLTAAHCVHdgkDYVKGSKKLRVG 187
Cdd:cd00190   11 SFPWQVSLQYTGGrhfCGGSLISPRWVLTAAHCVY---SSAPSNYTVRLG 57
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
140-193 6.16e-07

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 50.42  E-value: 6.16e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 281427284 140 TNFPFSTAVKLSTG-----CSGILISPQHVLTAAHCVHDGKdyvKGSKKLRVGLLKMRN 193
Cdd:COG5640   40 GEYPWMVALQSSNGpsgqfCGGTLIAPRWVLTAAHCVDGDG---PSDLRVVIGSTDLST 95
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
141-173 3.76e-06

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: 47.67  E-value: 3.76e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 281427284   141 NFPFSTAVKLSTG---CSGILISPQHVLTAAHCVHD 173
Cdd:smart00020  12 SFPWQVSLQYGGGrhfCGGSLISPRWVLTAAHCVRG 47
 
Name Accession Description Interval E-value
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
154-403 4.25e-20

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 87.42  E-value: 4.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 154 CSGILISPQHVLTAAHCVHDGKDyvkgskklrvgllkmrnksggkkrrgskrsrreasggdqrEGTREHLRERAkgGRRR 233
Cdd:COG3591   14 CTGTLIGPNLVLTAGHCVYDGAG----------------------------------------GGWATNIVFVP--GYNG 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 234 KKSGrgqriaegrpsfqWTRVKNTHIPKGWARGGMGdatlDYDYALLELKRAHKKKYMELGISPTIKKMPGGMIHFSGFD 313
Cdd:COG3591   52 GPYG-------------TATATRFRVPPGWVASGDA----GYDYALLRLDEPLGDTTGWLGLAFNDAPLAGEPVTIIGYP 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281427284 314 NDRADQL-VYRFCSVSDESNDLLYQYCDAESGSTGSGVYlrlkdpDKKNWKRKIIAVYSGhqwvdvhGVQKDYNVAVRIT 392
Cdd:COG3591  115 GDRPKDLsLDCSGRVTGVQGNRLSYDCDTTGGSSGSPVL------DDSDGGGRVVGVHSA-------GGADRANTGVRLT 181
                        250
                 ....*....|.
gi 281427284 393 PLKYAQICLWI 403
Cdd:COG3591  182 SAIVAALRAWA 192
Trypsin pfam00089
Trypsin;
141-177 8.53e-08

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 52.44  E-value: 8.53e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 281427284  141 NFPFSTAVKLSTG---CSGILISPQHVLTAAHCVHDGKDY 177
Cdd:pfam00089  11 SFPWQVSLQLSSGkhfCGGSLISENWVLTAAHCVSGASDV 50
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
141-187 5.17e-07

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: 50.35  E-value: 5.17e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 281427284 141 NFPFSTAVKLSTG---CSGILISPQHVLTAAHCVHdgkDYVKGSKKLRVG 187
Cdd:cd00190   11 SFPWQVSLQYTGGrhfCGGSLISPRWVLTAAHCVY---SSAPSNYTVRLG 57
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
140-193 6.16e-07

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 50.42  E-value: 6.16e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 281427284 140 TNFPFSTAVKLSTG-----CSGILISPQHVLTAAHCVHDGKdyvKGSKKLRVGLLKMRN 193
Cdd:COG5640   40 GEYPWMVALQSSNGpsgqfCGGTLIAPRWVLTAAHCVDGDG---PSDLRVVIGSTDLST 95
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
141-173 3.76e-06

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: 47.67  E-value: 3.76e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 281427284   141 NFPFSTAVKLSTG---CSGILISPQHVLTAAHCVHD 173
Cdd:smart00020  12 SFPWQVSLQYGGGrhfCGGSLISPRWVLTAAHCVRG 47
 
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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