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Conserved domains on  [gi|1519312619|ref|NP_872365|]
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transmembrane protease serine 12 precursor [Homo sapiens]

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

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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 ...
78-316 3.15e-82

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: 249.50  E-value: 3.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  78 IIGGTEAQAGAWPWVVSLQIKYGRvlvHVCGGTLVRERWVLTAAHCTKDaSDPLMWTAVIGTNNIHGRYPHTKKIKIKAI 157
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 158 IIHPNFILESYVNDIALFHLKKAVRYNDYIQPICLPfDVFQILDGNTKCFISGWGRTKEEGNATNILQDAEVHYISREMC 237
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519312619 238 NSERSYGGIIPNTSFCAGDEDGAFDTCRGDSGGPLMCYLPeyKRFFVMGITSYGHGCGRRGFPGVYIGPSFYQKWLTEH 316
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
78-316 3.15e-82

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: 249.50  E-value: 3.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  78 IIGGTEAQAGAWPWVVSLQIKYGRvlvHVCGGTLVRERWVLTAAHCTKDaSDPLMWTAVIGTNNIHGRYPHTKKIKIKAI 157
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 158 IIHPNFILESYVNDIALFHLKKAVRYNDYIQPICLPfDVFQILDGNTKCFISGWGRTKEEGNATNILQDAEVHYISREMC 237
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519312619 238 NSERSYGGIIPNTSFCAGDEDGAFDTCRGDSGGPLMCYLPeyKRFFVMGITSYGHGCGRRGFPGVYIGPSFYQKWLTEH 316
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
77-312 6.74e-82

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: 248.75  E-value: 6.74e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619   77 RIIGGTEAQAGAWPWVVSLQIKYGRvlvHVCGGTLVRERWVLTAAHCTKDaSDPLMWTAVIGTNNIhGRYPHTKKIKIKA 156
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDL-SSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  157 IIIHPNFILESYVNDIALFHLKKAVRYNDYIQPICLPfDVFQILDGNTKCFISGWGRTKEE-GNATNILQDAEVHYISRE 235
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLP-SSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519312619  236 MCNSERSYGGIIPNTSFCAGDEDGAFDTCRGDSGGPLMCylpEYKRFFVMGITSYGHGCGRRGFPGVYIGPSFYQKW 312
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC---NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
78-313 2.17e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 200.75  E-value: 2.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  78 IIGGTEAQAGAWPWVVSLQIKYGRvlvHVCGGTLVRERWVLTAAHCTKDASDplmWTAVIGTNNIHGRYPHTKKIKIKAI 157
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 158 IIHPNFILESYVNDIALFHLKKAVRYNDYIQPICLPfDVFQILDGNTKCFISGWGRTKEEGnATNILQDAEVHYISREMC 237
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLP-DASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519312619 238 NSerSYGGIIPNTSFCAGdeDGAFDTCRGDSGGPLMCYLPEykrffVMGITSYGHGCGRRGFPGVYIGPSFYQKWL 313
Cdd:pfam00089 153 RS--AYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
75-316 8.63e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 180.23  E-value: 8.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  75 GSRIIGGTEAQAGAWPWVVSLQIKYGRVlVHVCGGTLVRERWVLTAAHCTKDASDPLMwTAVIGTNNIHGRYPHTKKIKI 154
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 155 KAIiiHPNFILESYVNDIALFHLKKAVrynDYIQPICLPFDVFQILDGNTkcF-ISGWGRTKEE-GNATNILQDAEVHYI 232
Cdd:COG5640   106 IVV--HPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTP--AtVAGWGRTSEGpGSQSGTLRKADVPVV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 233 SREMCNSersYGGIIPNTSFCAGDEDGAFDTCRGDSGGPLmcYLPEYKRFFVMGITSYGHGCGRRGFPGVYIGPSFYQKW 312
Cdd:COG5640   179 SDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPL--VVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                  ....
gi 1519312619 313 LTEH 316
Cdd:COG5640   254 IKST 257
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
78-316 3.15e-82

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: 249.50  E-value: 3.15e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  78 IIGGTEAQAGAWPWVVSLQIKYGRvlvHVCGGTLVRERWVLTAAHCTKDaSDPLMWTAVIGTNNIHGRYPHTKKIKIKAI 157
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGR---HFCGGSLISPRWVLTAAHCVYS-SAPSNYTVRLGSHDLSSNEGGGQVIKVKKV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 158 IIHPNFILESYVNDIALFHLKKAVRYNDYIQPICLPfDVFQILDGNTKCFISGWGRTKEEGNATNILQDAEVHYISREMC 237
Cdd:cd00190    77 IVHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLP-SSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAEC 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519312619 238 NSERSYGGIIPNTSFCAGDEDGAFDTCRGDSGGPLMCYLPeyKRFFVMGITSYGHGCGRRGFPGVYIGPSFYQKWLTEH 316
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN--GRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
77-312 6.74e-82

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: 248.75  E-value: 6.74e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619   77 RIIGGTEAQAGAWPWVVSLQIKYGRvlvHVCGGTLVRERWVLTAAHCTKDaSDPLMWTAVIGTNNIhGRYPHTKKIKIKA 156
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR---HFCGGSLISPRWVLTAAHCVRG-SDPSNIRVRLGSHDL-SSGEEGQVIKVSK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  157 IIIHPNFILESYVNDIALFHLKKAVRYNDYIQPICLPfDVFQILDGNTKCFISGWGRTKEE-GNATNILQDAEVHYISRE 235
Cdd:smart00020  76 VIIHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLP-SSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519312619  236 MCNSERSYGGIIPNTSFCAGDEDGAFDTCRGDSGGPLMCylpEYKRFFVMGITSYGHGCGRRGFPGVYIGPSFYQKW 312
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC---NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228
Trypsin pfam00089
Trypsin;
78-313 2.17e-63

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 200.75  E-value: 2.17e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  78 IIGGTEAQAGAWPWVVSLQIKYGRvlvHVCGGTLVRERWVLTAAHCTKDASDplmWTAVIGTNNIHGRYPHTKKIKIKAI 157
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK---HFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 158 IIHPNFILESYVNDIALFHLKKAVRYNDYIQPICLPfDVFQILDGNTKCFISGWGRTKEEGnATNILQDAEVHYISREMC 237
Cdd:pfam00089  75 IVHPNYNPDTLDNDIALLKLESPVTLGDTVRPICLP-DASSDLPVGTTCTVSGWGNTKTLG-PSDTLQEVTVPVVSRETC 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519312619 238 NSerSYGGIIPNTSFCAGdeDGAFDTCRGDSGGPLMCYLPEykrffVMGITSYGHGCGRRGFPGVYIGPSFYQKWL 313
Cdd:pfam00089 153 RS--AYGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
75-316 8.63e-55

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 180.23  E-value: 8.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619  75 GSRIIGGTEAQAGAWPWVVSLQIKYGRVlVHVCGGTLVRERWVLTAAHCTKDASDPLMwTAVIGTNNIHGRYPHTKKIKI 154
Cdd:COG5640    28 APAIVGGTPATVGEYPWMVALQSSNGPS-GQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGGTVVKVAR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 155 KAIiiHPNFILESYVNDIALFHLKKAVrynDYIQPICLPFDVFQILDGNTkcF-ISGWGRTKEE-GNATNILQDAEVHYI 232
Cdd:COG5640   106 IVV--HPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTP--AtVAGWGRTSEGpGSQSGTLRKADVPVV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 233 SREMCNSersYGGIIPNTSFCAGDEDGAFDTCRGDSGGPLmcYLPEYKRFFVMGITSYGHGCGRRGFPGVYIGPSFYQKW 312
Cdd:COG5640   179 SDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPL--VVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253

                  ....
gi 1519312619 313 LTEH 316
Cdd:COG5640   254 IKST 257
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
105-311 2.55e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 50.45  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 105 HVCGGTLVRERWVLTAAHCTKDASD---PLMWTAVIG-TNNIHGRYPHTkkikikAIIIHPNFILESYVN-DIALFHLKK 179
Cdd:COG3591    12 GVCTGTLIGPNLVLTAGHCVYDGAGggwATNIVFVPGyNGGPYGTATAT------RFRVPPGWVASGDAGyDYALLRLDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312619 180 AVRynDYIQPicLPFDVFQILDGNTKCFISGWGRTKeeGNATNILQDAEVHYISREMCnserSYGGiipntsfcagdedg 259
Cdd:COG3591    86 PLG--DTTGW--LGLAFNDAPLAGEPVTIIGYPGDR--PKDLSLDCSGRVTGVQGNRL----SYDC-------------- 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1519312619 260 afDTCRGDSGGPLmcYLPEYKRFFVMGITSYGHgcGRRGFPGVYIGPSFYQK 311
Cdd:COG3591   142 --DTTGGSSGSPV--LDDSDGGGRVVGVHSAGG--ADRANTGVRLTSAIVAA 187
 
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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