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Conserved domains on  [gi|1634230002|ref|NP_001357332|]
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probable inactive serine protease 37 isoform 1 precursor [Homo sapiens]

Protein Classification

serine protease family protein( domain architecture ID 229414)

trypsin-like serine protease family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tryp_SPc super family cl21584
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-231 1.62e-33

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: 120.46  E-value: 1.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  28 PYLVYLK----SHFnpCVGVLIKPSWVLAPAHCYLP----NLKVMLGNFKSRVRDGTEQTINPIQIVRYWNYSHSAPQDD 99
Cdd:cd00190    13 PWQVSLQytggRHF--CGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002 100 LMLIKLAKPAMLNPKVQPLTLATTN--VRPGTVCLLSGldW-SQENSGRHPDLRQNLEAPVMSDRECQKTEQGKS--HRN 174
Cdd:cd00190    91 IALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSG--WgRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGtiTDN 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634230002 175 SLCVKFVkvfsrifgEVAVAT--------VICKDK----LQGI--------EVGHFmggdvGIYTNVYKYVSWIENT 231
Cdd:cd00190   169 MLCAGGL--------EGGKDAcqgdsggpLVCNDNgrgvLVGIvswgsgcaRPNYP-----GVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-231 1.62e-33

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: 120.46  E-value: 1.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  28 PYLVYLK----SHFnpCVGVLIKPSWVLAPAHCYLP----NLKVMLGNFKSRVRDGTEQTINPIQIVRYWNYSHSAPQDD 99
Cdd:cd00190    13 PWQVSLQytggRHF--CGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002 100 LMLIKLAKPAMLNPKVQPLTLATTN--VRPGTVCLLSGldW-SQENSGRHPDLRQNLEAPVMSDRECQKTEQGKS--HRN 174
Cdd:cd00190    91 IALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSG--WgRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGtiTDN 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634230002 175 SLCVKFVkvfsrifgEVAVAT--------VICKDK----LQGI--------EVGHFmggdvGIYTNVYKYVSWIENT 231
Cdd:cd00190   169 MLCAGGL--------EGGKDAcqgdsggpLVCNDNgrgvLVGIvswgsgcaRPNYP-----GVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
28-228 2.25e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 112.15  E-value: 2.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  28 PYLV--YLKSHFNPCVGVLIKPSWVLAPAHCYL--PNLKVMLGNFKSRVRDGTEQTINPIQIVRYWNYSHSAPQDDLMLI 103
Cdd:pfam00089  13 PWQVslQLSSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002 104 KLAKPAMLNPKVQPLTLATTN--VRPGTVCLLSGldWSQENSGRHPDLRQNLEAPVMSDRECQKTEQGKSHRNSLCVkfv 181
Cdd:pfam00089  93 KLESPVTLGDTVRPICLPDASsdLPVGTTCTVSG--WGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA--- 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1634230002 182 kvfsrifGEVAVAT--------VICKDK-LQGIevgHFMGGDV------GIYTNVYKYVSWI 228
Cdd:pfam00089 168 -------GAGGKDAcqgdsggpLVCSDGeLIGI---VSWGYGCasgnypGVYTPVSSYLDWI 219
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-228 6.99e-30

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: 110.85  E-value: 6.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002   28 PYLVYLK----SHFnpCVGVLIKPSWVLAPAHC----YLPNLKVMLGNFkSRVRDGTEQTINPIQIVRYWNYSHSAPQDD 99
Cdd:smart00020  14 PWQVSLQygggRHF--CGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSH-DLSSGEEGQVIKVSKVIIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  100 LMLIKLAKPAMLNPKVQPLTLATTN--VRPGTVCLLSGldW--SQENSGRHPDLRQNLEAPVMSDRECQKTEQGKSH--R 173
Cdd:smart00020  91 IALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSG--WgrTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAitD 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1634230002  174 NSLCVKfvkvfsriFGEVAVAT--------VICKDK---LQGI--------EVGHFmggdvGIYTNVYKYVSWI 228
Cdd:smart00020 169 NMLCAG--------GLEGGKDAcqgdsggpLVCNDGrwvLVGIvswgsgcaRPGKP-----GVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
27-232 1.74e-20

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 87.01  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  27 APYLVYL------KSHFnpCVGVLIKPSWVLAPAHCYLPN----LKVMLGNfkSRVRDGTEQTINPIQIVRYWNYSHSAP 96
Cdd:COG5640    42 YPWMVALqssngpSGQF--CGGTLIAPRWVLTAAHCVDGDgpsdLRVVIGS--TDLSTSGGTVVKVARIVVHPDYDPATP 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  97 QDDLMLIKLAKPAmlnPKVQPLTLATTN--VRPGTVCLLSGldW--SQENSGRHPDLRQNLEAPVMSDRECQKTEQGKSh 172
Cdd:COG5640   118 GNDIALLKLATPV---PGVAPAPLATSAdaAAPGTPATVAG--WgrTSEGPGSQSGTLRKADVPVVSDATCAAYGGFDG- 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1634230002 173 RNSLCVKFVKvfsrifGEV----------AVATVICKDKLQGI---EVGHFMGGDVGIYTNVYKYVSWIENTA 232
Cdd:COG5640   192 GTMLCAGYPE------GGKdacqgdsggpLVVKDGGGWVLVGVvswGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
28-231 1.62e-33

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: 120.46  E-value: 1.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  28 PYLVYLK----SHFnpCVGVLIKPSWVLAPAHCYLP----NLKVMLGNFKSRVRDGTEQTINPIQIVRYWNYSHSAPQDD 99
Cdd:cd00190    13 PWQVSLQytggRHF--CGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDND 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002 100 LMLIKLAKPAMLNPKVQPLTLATTN--VRPGTVCLLSGldW-SQENSGRHPDLRQNLEAPVMSDRECQKTEQGKS--HRN 174
Cdd:cd00190    91 IALLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSG--WgRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGtiTDN 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1634230002 175 SLCVKFVkvfsrifgEVAVAT--------VICKDK----LQGI--------EVGHFmggdvGIYTNVYKYVSWIENT 231
Cdd:cd00190   169 MLCAGGL--------EGGKDAcqgdsggpLVCNDNgrgvLVGIvswgsgcaRPNYP-----GVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
28-228 2.25e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 112.15  E-value: 2.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  28 PYLV--YLKSHFNPCVGVLIKPSWVLAPAHCYL--PNLKVMLGNFKSRVRDGTEQTINPIQIVRYWNYSHSAPQDDLMLI 103
Cdd:pfam00089  13 PWQVslQLSSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002 104 KLAKPAMLNPKVQPLTLATTN--VRPGTVCLLSGldWSQENSGRHPDLRQNLEAPVMSDRECQKTEQGKSHRNSLCVkfv 181
Cdd:pfam00089  93 KLESPVTLGDTVRPICLPDASsdLPVGTTCTVSG--WGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICA--- 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1634230002 182 kvfsrifGEVAVAT--------VICKDK-LQGIevgHFMGGDV------GIYTNVYKYVSWI 228
Cdd:pfam00089 168 -------GAGGKDAcqgdsggpLVCSDGeLIGI---VSWGYGCasgnypGVYTPVSSYLDWI 219
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-228 6.99e-30

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: 110.85  E-value: 6.99e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002   28 PYLVYLK----SHFnpCVGVLIKPSWVLAPAHC----YLPNLKVMLGNFkSRVRDGTEQTINPIQIVRYWNYSHSAPQDD 99
Cdd:smart00020  14 PWQVSLQygggRHF--CGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSH-DLSSGEEGQVIKVSKVIIHPNYNPSTYDND 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  100 LMLIKLAKPAMLNPKVQPLTLATTN--VRPGTVCLLSGldW--SQENSGRHPDLRQNLEAPVMSDRECQKTEQGKSH--R 173
Cdd:smart00020  91 IALLKLKEPVTLSDNVRPICLPSSNynVPAGTTCTVSG--WgrTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAitD 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1634230002  174 NSLCVKfvkvfsriFGEVAVAT--------VICKDK---LQGI--------EVGHFmggdvGIYTNVYKYVSWI 228
Cdd:smart00020 169 NMLCAG--------GLEGGKDAcqgdsggpLVCNDGrwvLVGIvswgsgcaRPGKP-----GVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
27-232 1.74e-20

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 87.01  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  27 APYLVYL------KSHFnpCVGVLIKPSWVLAPAHCYLPN----LKVMLGNfkSRVRDGTEQTINPIQIVRYWNYSHSAP 96
Cdd:COG5640    42 YPWMVALqssngpSGQF--CGGTLIAPRWVLTAAHCVDGDgpsdLRVVIGS--TDLSTSGGTVVKVARIVVHPDYDPATP 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1634230002  97 QDDLMLIKLAKPAmlnPKVQPLTLATTN--VRPGTVCLLSGldW--SQENSGRHPDLRQNLEAPVMSDRECQKTEQGKSh 172
Cdd:COG5640   118 GNDIALLKLATPV---PGVAPAPLATSAdaAAPGTPATVAG--WgrTSEGPGSQSGTLRKADVPVVSDATCAAYGGFDG- 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1634230002 173 RNSLCVKFVKvfsrifGEV----------AVATVICKDKLQGI---EVGHFMGGDVGIYTNVYKYVSWIENTA 232
Cdd:COG5640   192 GTMLCAGYPE------GGKdacqgdsggpLVVKDGGGWVLVGVvswGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
 
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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