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Conserved domains on  [gi|1720430249|ref|XP_030099920|]
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hepatocyte growth factor-like protein isoform X4 [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 ...
143-366 2.30e-77

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: 237.94  E-value: 2.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 143 VVGGH---PGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSChePLTGYEVWLGTINQNPQpgEANLQRVPVAKA 219
Cdd:cd00190     1 IVGGSeakIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSN--EGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 220 V------CGPAGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWGE-SIGTSNNTVLHVASMNVISNQECN 292
Cdd:cd00190    77 IvhpnynPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVPIVSNAECK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720430249 293 TKYR--GHIQESEICTQGLVVPVGACEGDYGGPLACYTHDCWVLQGLIIPNRVCARPRWPAIFTRVSVFVDWINKV 366
Cdd:cd00190   157 RAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
143-366 2.30e-77

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: 237.94  E-value: 2.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 143 VVGGH---PGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSChePLTGYEVWLGTINQNPQpgEANLQRVPVAKA 219
Cdd:cd00190     1 IVGGSeakIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSN--EGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 220 V------CGPAGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWGE-SIGTSNNTVLHVASMNVISNQECN 292
Cdd:cd00190    77 IvhpnynPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVPIVSNAECK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720430249 293 TKYR--GHIQESEICTQGLVVPVGACEGDYGGPLACYTHDCWVLQGLIIPNRVCARPRWPAIFTRVSVFVDWINKV 366
Cdd:cd00190   157 RAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
142-363 1.19e-70

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: 220.63  E-value: 1.19e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249  142 RVVGGH---PGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSChePLTGYEVWLGTINQNPQPGEanlQRVPVAK 218
Cdd:smart00020   1 RIVGGSeanIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEEG---QVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249  219 AV------CGPAGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWG--ESIGTSNNTVLHVASMNVISNQE 290
Cdd:smart00020  76 VIihpnynPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720430249  291 CNTKYRG--HIQESEICTQGLVVPVGACEGDYGGPLACyTHDCWVLQGLIIPNRVCARPRWPAIFTRVSVFVDWI 363
Cdd:smart00020 156 CRRAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
143-363 1.08e-50

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 168.77  E-value: 1.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 143 VVGGH---PGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSCHEpltgYEVWLGTINQNPQpgEANLQRVPVAKA 219
Cdd:pfam00089   1 IVGGDeaqPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVLR--EGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 220 VCGP------AGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWGESIGTSNNTVLHVASMNVISNQECNT 293
Cdd:pfam00089  75 IVHPnynpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 294 KYRGHIQESEICTQGlvVPVGACEGDYGGPLACYTHdcwVLQGLIIPNRVCARPRWPAIFTRVSVFVDWI 363
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
142-367 7.07e-40

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 142.10  E-value: 7.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 142 RVVGGHP---GNSPWTVSLRNRQG--QHFCGGSLVKEQWVLTARQCIWSchEPLTGYEVWLGTINQNPQPGeanlQRVPV 216
Cdd:COG5640    30 AIVGGTPatvGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCVDG--DGPSDLRVVIGSTDLSTSGG----TVVKV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 217 AKAVCGP------AGSQLVLLKLERPVilnHHVALICLPPEQYVVPPGTKCEIAGWG---ESIGTSNNTvLHVASMNVIS 287
Cdd:COG5640   104 ARIVVHPdydpatPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGrtsEGPGSQSGT-LRKADVPVVS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 288 NQECNTkYRGHIQESEICTQGLVVPVGACEGDYGGPLACYTHDCWVLQGLI-IPNRVCArPRWPAIFTRVSVFVDWINKV 366
Cdd:COG5640   180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVsWGGGPCA-AGYPGVYTRVSAYRDWIKST 257

                  .
gi 1720430249 367 M 367
Cdd:COG5640   258 A 258
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
143-366 2.30e-77

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: 237.94  E-value: 2.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 143 VVGGH---PGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSChePLTGYEVWLGTINQNPQpgEANLQRVPVAKA 219
Cdd:cd00190     1 IVGGSeakIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS--APSNYTVRLGSHDLSSN--EGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 220 V------CGPAGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWGE-SIGTSNNTVLHVASMNVISNQECN 292
Cdd:cd00190    77 IvhpnynPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRtSEGGPLPDVLQEVNVPIVSNAECK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720430249 293 TKYR--GHIQESEICTQGLVVPVGACEGDYGGPLACYTHDCWVLQGLIIPNRVCARPRWPAIFTRVSVFVDWINKV 366
Cdd:cd00190   157 RAYSygGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
142-363 1.19e-70

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: 220.63  E-value: 1.19e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249  142 RVVGGH---PGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSChePLTGYEVWLGTINQNPQPGEanlQRVPVAK 218
Cdd:smart00020   1 RIVGGSeanIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS--DPSNIRVRLGSHDLSSGEEG---QVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249  219 AV------CGPAGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWG--ESIGTSNNTVLHVASMNVISNQE 290
Cdd:smart00020  76 VIihpnynPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIVSNAT 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720430249  291 CNTKYRG--HIQESEICTQGLVVPVGACEGDYGGPLACyTHDCWVLQGLIIPNRVCARPRWPAIFTRVSVFVDWI 363
Cdd:smart00020 156 CRRAYSGggAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
143-363 1.08e-50

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 168.77  E-value: 1.08e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 143 VVGGH---PGNSPWTVSLRNRQGQHFCGGSLVKEQWVLTARQCIWSCHEpltgYEVWLGTINQNPQpgEANLQRVPVAKA 219
Cdd:pfam00089   1 IVGGDeaqPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASD----VKVVLGAHNIVLR--EGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 220 VCGP------AGSQLVLLKLERPVILNHHVALICLPPEQYVVPPGTKCEIAGWGESIGTSNNTVLHVASMNVISNQECNT 293
Cdd:pfam00089  75 IVHPnynpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 294 KYRGHIQESEICTQGlvVPVGACEGDYGGPLACYTHdcwVLQGLIIPNRVCARPRWPAIFTRVSVFVDWI 363
Cdd:pfam00089 155 AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
142-367 7.07e-40

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 142.10  E-value: 7.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 142 RVVGGHP---GNSPWTVSLRNRQG--QHFCGGSLVKEQWVLTARQCIWSchEPLTGYEVWLGTINQNPQPGeanlQRVPV 216
Cdd:COG5640    30 AIVGGTPatvGEYPWMVALQSSNGpsGQFCGGTLIAPRWVLTAAHCVDG--DGPSDLRVVIGSTDLSTSGG----TVVKV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 217 AKAVCGP------AGSQLVLLKLERPVilnHHVALICLPPEQYVVPPGTKCEIAGWG---ESIGTSNNTvLHVASMNVIS 287
Cdd:COG5640   104 ARIVVHPdydpatPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGrtsEGPGSQSGT-LRKADVPVVS 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720430249 288 NQECNTkYRGHIQESEICTQGLVVPVGACEGDYGGPLACYTHDCWVLQGLI-IPNRVCArPRWPAIFTRVSVFVDWINKV 366
Cdd:COG5640   180 DATCAA-YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVsWGGGPCA-AGYPGVYTRVSAYRDWIKST 257

                  .
gi 1720430249 367 M 367
Cdd:COG5640   258 A 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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