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Conserved domains on  [gi|110625851|ref|NP_898932|]
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transmembrane protease serine 12 isoform 1 precursor [Mus musculus]

Protein Classification

serine protease( domain architecture ID 10076129)

trypsin-like serine protease such as human plasminogen, the precursor of the widely distributed protease plasmin, or granzyme B, a human enzyme necessary for target cell lysis in cell-mediated immune responses

CATH:  2.40.10.10
EC:  3.4.21.-
PubMed:  18259688

Graphical summary

 Zoom to residue level

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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 ...
66-300 1.13e-87

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: 262.98  E-value: 1.13e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851  66 IIGGSQADTGAWPWQVSLQVQDGdilMHVCGGALVRDRWVLTAAHCTKEaRDPLKWRAVMGTNDLTRSPYHSRNIRITDI 145
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGG---RHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851 146 IIPPDFIMETFVNDIALFRLKRAVRYNDYIQPICLPfGVFQKLDQNTACFISGWGRTREEGNGTTILQEAKVHFISREVC 225
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625851 226 SSDQGYSGMIPNTSFCAGHENGTFDSCRGDSGGPLMCYLpeHSRYFVMGITSYGHGCGRRHFPGVYSNPSFFQEW 300
Cdd:cd00190  156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
66-300 1.13e-87

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: 262.98  E-value: 1.13e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851  66 IIGGSQADTGAWPWQVSLQVQDGdilMHVCGGALVRDRWVLTAAHCTKEaRDPLKWRAVMGTNDLTRSPYHSRNIRITDI 145
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGG---RHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851 146 IIPPDFIMETFVNDIALFRLKRAVRYNDYIQPICLPfGVFQKLDQNTACFISGWGRTREEGNGTTILQEAKVHFISREVC 225
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625851 226 SSDQGYSGMIPNTSFCAGHENGTFDSCRGDSGGPLMCYLpeHSRYFVMGITSYGHGCGRRHFPGVYSNPSFFQEW 300
Cdd:cd00190  156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
65-300 1.63e-85

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: 257.22  E-value: 1.63e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851    65 RIIGGSQADTGAWPWQVSLQVQDGDilmHVCGGALVRDRWVLTAAHCTKEaRDPLKWRAVMGTNDLTrSPYHSRNIRITD 144
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLS-SGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851   145 IIIPPDFIMETFVNDIALFRLKRAVRYNDYIQPICLPfGVFQKLDQNTACFISGWGRTREE-GNGTTILQEAKVHFISRE 223
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLP-SSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625851   224 VCSSDQGYSGMIPNTSFCAGHENGTFDSCRGDSGGPLMCylpEHSRYFVMGITSYGHGCGRRHFPGVYSNPSFFQEW 300
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC---NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
53-305 2.36e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.80  E-value: 2.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851  53 GIAPLRGAVEGSRIIGGSQADTGAWPWQVSLQVQDGDIlMHVCGGALVRDRWVLTAAHCTkEARDPLKWRAVMGTNDLTR 132
Cdd:COG5640   18 ALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTDLST 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851 133 SPyhSRNIRITDIIIPPDFIMETFVNDIALFRLKRAVrynDYIQPICLPfGVFQKLDQNTACFISGWGRTREE-GNGTTI 211
Cdd:COG5640   96 SG--GTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLA-TSADAAAPGTPATVAGWGRTSEGpGSQSGT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851 212 LQEAKVHFISREVCssdQGYSGMIPNTSFCAGHENGTFDSCRGDSGGPLmcYLPEHSRYFVMGITSYGHGCGRRHFPGVY 291
Cdd:COG5640  170 LRKADVPVVSDATC---AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPL--VVKDGGGWVLVGVVSWGGGPCAAGYPGVY 244
                        250
                 ....*....|....
gi 110625851 292 SNPSFFQEWMTHYL 305
Cdd:COG5640  245 TRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
66-301 1.08e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 196.12  E-value: 1.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851   66 IIGGSQADTGAWPWQVSLQVQDGdilMHVCGGALVRDRWVLTAAHCtkeARDPLKWRAVMGTNDLTRSPYHSRNIRITDI 145
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG---KHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851  146 IIPPDFIMETFVNDIALFRLKRAVRYNDYIQPICLPfGVFQKLDQNTACFISGWGRTREEGNGTTiLQEAKVHFISREVC 225
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLP-DASSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625851  226 SSDqgYSGMIPNTSFCAGheNGTFDSCRGDSGGPLMCylpehSRYFVMGITSYGHGCGRRHFPGVYSNPSFFQEWM 301
Cdd:pfam00089 153 RSA--YGGTVTDTMICAG--AGGKDACQGDSGGPLVC-----SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
66-300 1.13e-87

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: 262.98  E-value: 1.13e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851  66 IIGGSQADTGAWPWQVSLQVQDGdilMHVCGGALVRDRWVLTAAHCTKEaRDPLKWRAVMGTNDLTRSPYHSRNIRITDI 145
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGG---RHFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851 146 IIPPDFIMETFVNDIALFRLKRAVRYNDYIQPICLPfGVFQKLDQNTACFISGWGRTREEGNGTTILQEAKVHFISREVC 225
Cdd:cd00190   77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625851 226 SSDQGYSGMIPNTSFCAGHENGTFDSCRGDSGGPLMCYLpeHSRYFVMGITSYGHGCGRRHFPGVYSNPSFFQEW 300
Cdd:cd00190  156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDW 228
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
65-300 1.63e-85

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: 257.22  E-value: 1.63e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851    65 RIIGGSQADTGAWPWQVSLQVQDGDilmHVCGGALVRDRWVLTAAHCTKEaRDPLKWRAVMGTNDLTrSPYHSRNIRITD 144
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDLS-SGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851   145 IIIPPDFIMETFVNDIALFRLKRAVRYNDYIQPICLPfGVFQKLDQNTACFISGWGRTREE-GNGTTILQEAKVHFISRE 223
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLP-SSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625851   224 VCSSDQGYSGMIPNTSFCAGHENGTFDSCRGDSGGPLMCylpEHSRYFVMGITSYGHGCGRRHFPGVYSNPSFFQEW 300
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC---NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
53-305 2.36e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 201.80  E-value: 2.36e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851  53 GIAPLRGAVEGSRIIGGSQADTGAWPWQVSLQVQDGDIlMHVCGGALVRDRWVLTAAHCTkEARDPLKWRAVMGTNDLTR 132
Cdd:COG5640   18 ALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCV-DGDGPSDLRVVIGSTDLST 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851 133 SPyhSRNIRITDIIIPPDFIMETFVNDIALFRLKRAVrynDYIQPICLPfGVFQKLDQNTACFISGWGRTREE-GNGTTI 211
Cdd:COG5640   96 SG--GTVVKVARIVVHPDYDPATPGNDIALLKLATPV---PGVAPAPLA-TSADAAAPGTPATVAGWGRTSEGpGSQSGT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851 212 LQEAKVHFISREVCssdQGYSGMIPNTSFCAGHENGTFDSCRGDSGGPLmcYLPEHSRYFVMGITSYGHGCGRRHFPGVY 291
Cdd:COG5640  170 LRKADVPVVSDATC---AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPL--VVKDGGGWVLVGVVSWGGGPCAAGYPGVY 244
                        250
                 ....*....|....
gi 110625851 292 SNPSFFQEWMTHYL 305
Cdd:COG5640  245 TRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
66-301 1.08e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 196.12  E-value: 1.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851   66 IIGGSQADTGAWPWQVSLQVQDGdilMHVCGGALVRDRWVLTAAHCtkeARDPLKWRAVMGTNDLTRSPYHSRNIRITDI 145
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSG---KHFCGGSLISENWVLTAAHC---VSGASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851  146 IIPPDFIMETFVNDIALFRLKRAVRYNDYIQPICLPfGVFQKLDQNTACFISGWGRTREEGNGTTiLQEAKVHFISREVC 225
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLP-DASSDLPVGTTCTVSGWGNTKTLGPSDT-LQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625851  226 SSDqgYSGMIPNTSFCAGheNGTFDSCRGDSGGPLMCylpehSRYFVMGITSYGHGCGRRHFPGVYSNPSFFQEWM 301
Cdd:pfam00089 153 RSA--YGGTVTDTMICAG--AGGKDACQGDSGGPLVC-----SDGELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
93-298 6.13e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 57.76  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851  93 HVCGGALVRDRWVLTAAHC---TKEARDPLKWRAVMGTNDltrSPYhsRNIRITDIIIPPDFIMETFVN-DIALFRLKRA 168
Cdd:COG3591   12 GVCTGTLIGPNLVLTAGHCvydGAGGGWATNIVFVPGYNG---GPY--GTATATRFRVPPGWVASGDAGyDYALLRLDEP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625851 169 VRynDYIQPicLPFGVFQKLDQNTACFISGWGRTReeGNGTTILQEAKVHFISREVCSSDqgysgmipntsfCaghengt 248
Cdd:COG3591   87 LG--DTTGW--LGLAFNDAPLAGEPVTIIGYPGDR--PKDLSLDCSGRVTGVQGNRLSYD------------C------- 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 110625851 249 fDSCRGDSGGPLmcYLPEHSRYFVMGITSYGHgcGRRHFPGVYSNPSFFQ 298
Cdd:COG3591  142 -DTTGGSSGSPV--LDDSDGGGRVVGVHSAGG--ADRANTGVRLTSAIVA 186
 
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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