NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720432905|ref|XP_030100509|]
View 

serine protease 44 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
12-177 2.82e-65

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: 200.97  E-value: 2.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  12 VRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSRILQEIEL 91
Cdd:cd00190    69 QVIKVKKVIVHPNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNV 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  92 NIIRHEKCNQILKDIMGniftlVQEGGVC-GYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEV 170
Cdd:cd00190   148 PIVSNAECKRAYSYGGT-----ITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRV 222

                  ....*..
gi 1720432905 171 SYYRDWI 177
Cdd:cd00190   223 SSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
12-177 2.82e-65

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: 200.97  E-value: 2.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  12 VRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSRILQEIEL 91
Cdd:cd00190    69 QVIKVKKVIVHPNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNV 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  92 NIIRHEKCNQILKDIMGniftlVQEGGVC-GYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEV 170
Cdd:cd00190   148 PIVSNAECKRAYSYGGT-----ITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRV 222

                  ....*..
gi 1720432905 171 SYYRDWI 177
Cdd:cd00190   223 SSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
12-177 7.01e-61

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: 189.81  E-value: 7.01e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905   12 VRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKV-LEQGRSSRILQEIE 90
Cdd:smart00020  69 QVIKVSKVIIHPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVN 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905   91 LNIIRHEKCNQILKDImgnifTLVQEGGVC-GYNEKGGDACQGDSGGPLVCEfNKTWVQVGIVSWGLGCGRIGYPGVYTE 169
Cdd:smart00020 148 VPIVSNATCRRAYSGG-----GAITDNMLCaGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTR 221

                   ....*...
gi 1720432905  170 VSYYRDWI 177
Cdd:smart00020 222 VSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-177 4.64e-45

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 150.18  E-value: 4.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905   2 GDADLWSKRPVRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNysvNIQPVCIPEKSFLVQPGTLCWVTGWGKVLE-QG 80
Cdd:COG5640    89 GSTDLSTSGGTVVKVARIVVHPDYDP-ATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPG 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  81 RSSRILQEIELNIIRHEKCNQILKDIMGNIFTLvqeggvcGYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGR 160
Cdd:COG5640   165 SQSGTLRKADVPVVSDATCAAYGGFDGGTMLCA-------GYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCA 237
                         170
                  ....*....|....*..
gi 1720432905 161 IGYPGVYTEVSYYRDWI 177
Cdd:COG5640   238 AGYPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
3-177 1.22e-44

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 147.97  E-value: 1.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905   3 DADLWSKRPVRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRS 82
Cdd:pfam00089  58 NIVLREGGEQKFDVEKIIVHPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  83 SrILQEIELNIIRHEKCNQilkdimgNIFTLVQEGGVCGYnEKGGDACQGDSGGPLVCEFNKtwvQVGIVSWGLGCGRIG 162
Cdd:pfam00089 137 D-TLQEVTVPVVSRETCRS-------AYGGTVTDTMICAG-AGGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGN 204
                         170
                  ....*....|....*
gi 1720432905 163 YPGVYTEVSYYRDWI 177
Cdd:pfam00089 205 YPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
12-177 2.82e-65

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: 200.97  E-value: 2.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  12 VRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRSSRILQEIEL 91
Cdd:cd00190    69 QVIKVKKVIVHPNYNP-STYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNV 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  92 NIIRHEKCNQILKDIMGniftlVQEGGVC-GYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGRIGYPGVYTEV 170
Cdd:cd00190   148 PIVSNAECKRAYSYGGT-----ITDNMLCaGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRV 222

                  ....*..
gi 1720432905 171 SYYRDWI 177
Cdd:cd00190   223 SSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
12-177 7.01e-61

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: 189.81  E-value: 7.01e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905   12 VRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKV-LEQGRSSRILQEIE 90
Cdd:smart00020  69 QVIKVSKVIIHPNYNP-STYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVN 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905   91 LNIIRHEKCNQILKDImgnifTLVQEGGVC-GYNEKGGDACQGDSGGPLVCEfNKTWVQVGIVSWGLGCGRIGYPGVYTE 169
Cdd:smart00020 148 VPIVSNATCRRAYSGG-----GAITDNMLCaGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTR 221

                   ....*...
gi 1720432905  170 VSYYRDWI 177
Cdd:smart00020 222 VSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
2-177 4.64e-45

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 150.18  E-value: 4.64e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905   2 GDADLWSKRPVRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNysvNIQPVCIPEKSFLVQPGTLCWVTGWGKVLE-QG 80
Cdd:COG5640    89 GSTDLSTSGGTVVKVARIVVHPDYDP-ATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEgPG 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  81 RSSRILQEIELNIIRHEKCNQILKDIMGNIFTLvqeggvcGYNEKGGDACQGDSGGPLVCEFNKTWVQVGIVSWGLGCGR 160
Cdd:COG5640   165 SQSGTLRKADVPVVSDATCAAYGGFDGGTMLCA-------GYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCA 237
                         170
                  ....*....|....*..
gi 1720432905 161 IGYPGVYTEVSYYRDWI 177
Cdd:COG5640   238 AGYPGVYTRVSAYRDWI 254
Trypsin pfam00089
Trypsin;
3-177 1.22e-44

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 147.97  E-value: 1.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905   3 DADLWSKRPVRIPVQDIIVHQDFSMmRTVVHDIALVLLAFPVNYSVNIQPVCIPEKSFLVQPGTLCWVTGWGKVLEQGRS 82
Cdd:pfam00089  58 NIVLREGGEQKFDVEKIIVHPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432905  83 SrILQEIELNIIRHEKCNQilkdimgNIFTLVQEGGVCGYnEKGGDACQGDSGGPLVCEFNKtwvQVGIVSWGLGCGRIG 162
Cdd:pfam00089 137 D-TLQEVTVPVVSRETCRS-------AYGGTVTDTMICAG-AGGKDACQGDSGGPLVCSDGE---LIGIVSWGYGCASGN 204
                         170
                  ....*....|....*
gi 1720432905 163 YPGVYTEVSYYRDWI 177
Cdd:pfam00089 205 YPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
128-184 2.18e-03

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 37.73  E-value: 2.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720432905 128 DACQGDSGGPLVCEFNKTWVQVGIVSWglgcgriGYPGVYTEVSYYRDWIIKELSRA 184
Cdd:COG3591   142 DTTGGSSGSPVLDDSDGGGRVVGVHSA-------GGADRANTGVRLTSAIVAALRAW 191
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH