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Conserved domains on  [gi|157820687|ref|NP_001102095|]
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probable inactive serine protease 37 precursor [Rattus norvegicus]

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 1.44e-30

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: 112.75  E-value: 1.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  28 PYLAYLKSNFNP--CVGVLIKASWVLAPSHCYLP----NLRVMLGNFKSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLM 101
Cdd:cd00190   13 PWQVSLQYTGGRhfCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687 102 LIKLAKPATFNNKVQVLPIATTN--VRPGTICTLSGldW-SQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSN--HRNSL 176
Cdd:cd00190   93 LLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSG--WgRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGtiTDNML 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820687 177 CVKFGKVfsrifGEVA---------VATVICKNKLQGI--------EVGHFmggdvGIYTNIYSYVPWIEKT 231
Cdd:cd00190  171 CAGGLEG-----GKDAcqgdsggplVCNDNGRGVLVGIvswgsgcaRPNYP-----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 1.44e-30

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: 112.75  E-value: 1.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  28 PYLAYLKSNFNP--CVGVLIKASWVLAPSHCYLP----NLRVMLGNFKSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLM 101
Cdd:cd00190   13 PWQVSLQYTGGRhfCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687 102 LIKLAKPATFNNKVQVLPIATTN--VRPGTICTLSGldW-SQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSN--HRNSL 176
Cdd:cd00190   93 LLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSG--WgRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGtiTDNML 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820687 177 CVKFGKVfsrifGEVA---------VATVICKNKLQGI--------EVGHFmggdvGIYTNIYSYVPWIEKT 231
Cdd:cd00190  171 CAGGLEG-----GKDAcqgdsggplVCNDNGRGVLVGIvswgsgcaRPNYP-----GVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
28-228 3.47e-28

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 106.37  E-value: 3.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687   28 PYLA--YLKSNFNPCVGVLIKASWVLAPSHCYL--PNLRVMLGNFKSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLMLI 103
Cdd:pfam00089  13 PWQVslQLSSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  104 KLAKPATFNNKVQVLPIATTN--VRPGTICTLSGldWSQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSNHRNSLCVKFG 181
Cdd:pfam00089  93 KLESPVTLGDTVRPICLPDASsdLPVGTTCTVSG--WGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGAG 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157820687  182 KVfSRIFGeVAVATVICKNK-LQGIevgHFMGGDV------GIYTNIYSYVPWI 228
Cdd:pfam00089 171 GK-DACQG-DSGGPLVCSDGeLIGI---VSWGYGCasgnypGVYTPVSSYLDWI 219
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-228 3.48e-27

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: 103.91  E-value: 3.48e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687    28 PYLAYLKSNFNP--CVGVLIKASWVLAPSHC----YLPNLRVMLGNFkSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLM 101
Cdd:smart00020  14 PWQVSLQYGGGRhfCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSH-DLSSGEEGQVIKVSKVIIHPNYNPSTYDNDIA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687   102 LIKLAKPATFNNKVQV--LPIATTNVRPGTICTLSGldW--SQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSNH--RNS 175
Cdd:smart00020  93 LLKLKEPVTLSDNVRPicLPSSNYNVPAGTTCTVSG--WgrTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAitDNM 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820687   176 LCVKfgkvfsriFGEVAVAT--------VICKNK---LQGI--------EVGHFmggdvGIYTNIYSYVPWI 228
Cdd:smart00020 171 LCAG--------GLEGGKDAcqgdsggpLVCNDGrwvLVGIvswgsgcaRPGKP-----GVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
27-232 1.13e-16

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 76.61  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  27 APYLAYLKSNFNP----CVGVLIKASWVLAPSHCYLPN----LRVMLGNfkSRVRDGTEQTIYPIQIIRYWNYSHTAPQD 98
Cdd:COG5640   42 YPWMVALQSSNGPsgqfCGGTLIAPRWVLTAAHCVDGDgpsdLRVVIGS--TDLSTSGGTVVKVARIVVHPDYDPATPGN 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  99 DLMLIKLAKPATFnnkVQVLPIATTN--VRPGTICTLSGldW--SQENNGRHPDLRQNLEAPVMTDKDCQkTQQGSNHRN 174
Cdd:COG5640  120 DIALLKLATPVPG---VAPAPLATSAdaAAPGTPATVAG--WgrTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDGGT 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820687 175 SLCVKFGKvfsrifGEV----------AVATVICKNKLQGI---EVGHFMGGDVGIYTNIYSYVPWIEKTT 232
Cdd:COG5640  194 MLCAGYPE------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 1.44e-30

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: 112.75  E-value: 1.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  28 PYLAYLKSNFNP--CVGVLIKASWVLAPSHCYLP----NLRVMLGNFKSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLM 101
Cdd:cd00190   13 PWQVSLQYTGGRhfCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPSTYDNDIA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687 102 LIKLAKPATFNNKVQVLPIATTN--VRPGTICTLSGldW-SQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSN--HRNSL 176
Cdd:cd00190   93 LLKLKRPVTLSDNVRPICLPSSGynLPAGTTCTVSG--WgRTSEGGPLPDVLQEVNVPIVSNAECKRAYSYGGtiTDNML 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820687 177 CVKFGKVfsrifGEVA---------VATVICKNKLQGI--------EVGHFmggdvGIYTNIYSYVPWIEKT 231
Cdd:cd00190  171 CAGGLEG-----GKDAcqgdsggplVCNDNGRGVLVGIvswgsgcaRPNYP-----GVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
28-228 3.47e-28

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 106.37  E-value: 3.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687   28 PYLA--YLKSNFNPCVGVLIKASWVLAPSHCYL--PNLRVMLGNFKSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLMLI 103
Cdd:pfam00089  13 PWQVslQLSSGKHFCGGSLISENWVLTAAHCVSgaSDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYNPDTLDNDIALL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  104 KLAKPATFNNKVQVLPIATTN--VRPGTICTLSGldWSQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSNHRNSLCVKFG 181
Cdd:pfam00089  93 KLESPVTLGDTVRPICLPDASsdLPVGTTCTVSG--WGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGAG 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157820687  182 KVfSRIFGeVAVATVICKNK-LQGIevgHFMGGDV------GIYTNIYSYVPWI 228
Cdd:pfam00089 171 GK-DACQG-DSGGPLVCSDGeLIGI---VSWGYGCasgnypGVYTPVSSYLDWI 219
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-228 3.48e-27

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: 103.91  E-value: 3.48e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687    28 PYLAYLKSNFNP--CVGVLIKASWVLAPSHC----YLPNLRVMLGNFkSRVRDGTEQTIYPIQIIRYWNYSHTAPQDDLM 101
Cdd:smart00020  14 PWQVSLQYGGGRhfCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSH-DLSSGEEGQVIKVSKVIIHPNYNPSTYDNDIA 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687   102 LIKLAKPATFNNKVQV--LPIATTNVRPGTICTLSGldW--SQENNGRHPDLRQNLEAPVMTDKDCQKTQQGSNH--RNS 175
Cdd:smart00020  93 LLKLKEPVTLSDNVRPicLPSSNYNVPAGTTCTVSG--WgrTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGGGAitDNM 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157820687   176 LCVKfgkvfsriFGEVAVAT--------VICKNK---LQGI--------EVGHFmggdvGIYTNIYSYVPWI 228
Cdd:smart00020 171 LCAG--------GLEGGKDAcqgdsggpLVCNDGrwvLVGIvswgsgcaRPGKP-----GVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
27-232 1.13e-16

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 76.61  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  27 APYLAYLKSNFNP----CVGVLIKASWVLAPSHCYLPN----LRVMLGNfkSRVRDGTEQTIYPIQIIRYWNYSHTAPQD 98
Cdd:COG5640   42 YPWMVALQSSNGPsgqfCGGTLIAPRWVLTAAHCVDGDgpsdLRVVIGS--TDLSTSGGTVVKVARIVVHPDYDPATPGN 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687  99 DLMLIKLAKPATFnnkVQVLPIATTN--VRPGTICTLSGldW--SQENNGRHPDLRQNLEAPVMTDKDCQkTQQGSNHRN 174
Cdd:COG5640  120 DIALLKLATPVPG---VAPAPLATSAdaAAPGTPATVAG--WgrTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDGGT 193
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157820687 175 SLCVKFGKvfsrifGEV----------AVATVICKNKLQGI---EVGHFMGGDVGIYTNIYSYVPWIEKTT 232
Cdd:COG5640  194 MLCAGYPE------GGKdacqgdsggpLVVKDGGGWVLVGVvswGGGPCAAGYPGVYTRVSAYRDWIKSTA 258
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
28-115 2.75e-04

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: 39.45  E-value: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157820687   28 PYLA--YLKSNFNpCVGVLIKASWVLAPSHC-YLPNLR-----VMLGNFKSR--VRDGTEQtiypiqiIRYWNYSHTAPQ 97
Cdd:pfam09342   2 PWIAkvYLDGNMI-CSGVLIDASWVIVSGSClRDTNLRhqyisVVLGGAKTLksIEGPYEQ-------IVRVDCRHDIPE 73
                          90
                  ....*....|....*...
gi 157820687   98 DDLMLIKLAKPATFNNKV 115
Cdd:pfam09342  74 SEISLLHLASPASFSNHV 91
 
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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