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Conserved domains on  [gi|11055972|ref|NP_065233|]
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testisin 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 ...
55-294 3.39e-102

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: 299.58  E-value: 3.39e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972  55 IVGGDDAELGRWPWQGSLRV-WGNHLCGATLLNRRWVLTAAHCFQkDNDPFDWTVQFGELTSRPSLWNLQaysnRYQIED 133
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQ----VIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 134 IFLSPKYSEQ-YPNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTGWGAIGEDesLPSPNTLQEVQVAIINNS 212
Cdd:cd00190  76 VIVHPNYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 213 MCNHMYKKPDFRTNiwgDMVCAGTPEGGKDACFGDSGGPLACDQDTVWYQVGVVSWGIGCGRPNRPGVYTNISHHYNWIQ 292
Cdd:cd00190 154 ECKRAYSYGGTITD---NMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 11055972 293 ST 294
Cdd:cd00190 231 KT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
55-294 3.39e-102

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: 299.58  E-value: 3.39e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972  55 IVGGDDAELGRWPWQGSLRV-WGNHLCGATLLNRRWVLTAAHCFQkDNDPFDWTVQFGELTSRPSLWNLQaysnRYQIED 133
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQ----VIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 134 IFLSPKYSEQ-YPNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTGWGAIGEDesLPSPNTLQEVQVAIINNS 212
Cdd:cd00190  76 VIVHPNYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 213 MCNHMYKKPDFRTNiwgDMVCAGTPEGGKDACFGDSGGPLACDQDTVWYQVGVVSWGIGCGRPNRPGVYTNISHHYNWIQ 292
Cdd:cd00190 154 ECKRAYSYGGTITD---NMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 11055972 293 ST 294
Cdd:cd00190 231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
54-291 2.62e-100

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: 294.59  E-value: 2.62e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972     54 RIVGGDDAELGRWPWQGSLRVWGN-HLCGATLLNRRWVLTAAHCFQkDNDPFDWTVQFGELTsrpslWNLQAYSNRYQIE 132
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHD-----LSSGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972    133 DIFLSPKYSEQ-YPNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTGWGAIgEDESLPSPNTLQEVQVAIINN 211
Cdd:smart00020  75 KVIIHPNYNPStYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT-SEGAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972    212 SMCNHMYKKPDFRTNiwgDMVCAGTPEGGKDACFGDSGGPLACdQDTVWYQVGVVSWGIGCGRPNRPGVYTNISHHYNWI 291
Cdd:smart00020 154 ATCRRAYSGGGAITD---NMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
41-295 6.13e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 226.07  E-value: 6.13e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972  41 LLSGPCGHRTIPSRIVGGDDAELGRWPWQGSLRVWG---NHLCGATLLNRRWVLTAAHCFQkDNDPFDWTVQFGELTSRP 117
Cdd:COG5640  17 LALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLST 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 118 SlwnlqaYSNRYQIEDIFLSPKY-SEQYPNDIALLKLSSPVTynnFIQPICLLNSTYKFENRTDCWVTGWGAIGEDESlP 196
Cdd:COG5640  96 S------GGTVVKVARIVVHPDYdPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-S 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 197 SPNTLQEVQVAIINNSMCNhmykkpDFRTNIWGDMVCAGTPEGGKDACFGDSGGPLACDQDTVWYQVGVVSWGIGCGRPN 276
Cdd:COG5640 166 QSGTLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAG 239
                       250
                ....*....|....*....
gi 11055972 277 RPGVYTNISHHYNWIQSTM 295
Cdd:COG5640 240 YPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
55-291 3.84e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 212.30  E-value: 3.84e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972    55 IVGGDDAELGRWPWQGSLRVWGN-HLCGATLLNRRWVLTAAHCFqkdNDPFDWTVQFGELTSRPSlwnlQAYSNRYQIED 133
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLR----EGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972   134 IFLSPKY-SEQYPNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTGWGAIGEDEslpSPNTLQEVQVAIINNS 212
Cdd:pfam00089  74 IIVHPNYnPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11055972   213 MCNHMYKkpdfrTNIWGDMVCAGTpeGGKDACFGDSGGPLACDQDTVwyqVGVVSWGIGCGRPNRPGVYTNISHHYNWI 291
Cdd:pfam00089 151 TCRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDGEL---IGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
55-294 3.39e-102

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: 299.58  E-value: 3.39e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972  55 IVGGDDAELGRWPWQGSLRV-WGNHLCGATLLNRRWVLTAAHCFQkDNDPFDWTVQFGELTSRPSLWNLQaysnRYQIED 133
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQ----VIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 134 IFLSPKYSEQ-YPNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTGWGAIGEDesLPSPNTLQEVQVAIINNS 212
Cdd:cd00190  76 VIVHPNYNPStYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 213 MCNHMYKKPDFRTNiwgDMVCAGTPEGGKDACFGDSGGPLACDQDTVWYQVGVVSWGIGCGRPNRPGVYTNISHHYNWIQ 292
Cdd:cd00190 154 ECKRAYSYGGTITD---NMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                ..
gi 11055972 293 ST 294
Cdd:cd00190 231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
54-291 2.62e-100

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: 294.59  E-value: 2.62e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972     54 RIVGGDDAELGRWPWQGSLRVWGN-HLCGATLLNRRWVLTAAHCFQkDNDPFDWTVQFGELTsrpslWNLQAYSNRYQIE 132
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHD-----LSSGEEGQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972    133 DIFLSPKYSEQ-YPNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTGWGAIgEDESLPSPNTLQEVQVAIINN 211
Cdd:smart00020  75 KVIIHPNYNPStYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRT-SEGAGSLPDTLQEVNVPIVSN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972    212 SMCNHMYKKPDFRTNiwgDMVCAGTPEGGKDACFGDSGGPLACdQDTVWYQVGVVSWGIGCGRPNRPGVYTNISHHYNWI 291
Cdd:smart00020 154 ATCRRAYSGGGAITD---NMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
41-295 6.13e-73

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 226.07  E-value: 6.13e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972  41 LLSGPCGHRTIPSRIVGGDDAELGRWPWQGSLRVWG---NHLCGATLLNRRWVLTAAHCFQkDNDPFDWTVQFGELTSRP 117
Cdd:COG5640  17 LALAAAPAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLST 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 118 SlwnlqaYSNRYQIEDIFLSPKY-SEQYPNDIALLKLSSPVTynnFIQPICLLNSTYKFENRTDCWVTGWGAIGEDESlP 196
Cdd:COG5640  96 S------GGTVVKVARIVVHPDYdPATPGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPG-S 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 197 SPNTLQEVQVAIINNSMCNhmykkpDFRTNIWGDMVCAGTPEGGKDACFGDSGGPLACDQDTVWYQVGVVSWGIGCGRPN 276
Cdd:COG5640 166 QSGTLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAG 239
                       250
                ....*....|....*....
gi 11055972 277 RPGVYTNISHHYNWIQSTM 295
Cdd:COG5640 240 YPGVYTRVSAYRDWIKSTA 258
Trypsin pfam00089
Trypsin;
55-291 3.84e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 212.30  E-value: 3.84e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972    55 IVGGDDAELGRWPWQGSLRVWGN-HLCGATLLNRRWVLTAAHCFqkdNDPFDWTVQFGELTSRPSlwnlQAYSNRYQIED 133
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLR----EGGEQKFDVEK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972   134 IFLSPKY-SEQYPNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTGWGAIGEDEslpSPNTLQEVQVAIINNS 212
Cdd:pfam00089  74 IIVHPNYnPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11055972   213 MCNHMYKkpdfrTNIWGDMVCAGTpeGGKDACFGDSGGPLACDQDTVwyqVGVVSWGIGCGRPNRPGVYTNISHHYNWI 291
Cdd:pfam00089 151 TCRSAYG-----GTVTDTMICAGA--GGKDACQGDSGGPLVCSDGEL---IGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
76-281 6.29e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.85  E-value: 6.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972  76 GNHLCGATLLNRRWVLTAAHCF---QKDNDPFDWTVQFGeltsrpslWNLQAYSnRYQIEDIFLSPKY--SEQYPNDIAL 150
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPG--------YNGGPYG-TATATRFRVPPGWvaSGDAGYDYAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972 151 LKLSSPVTynNFIQPICLLNSTYKFENRTdCWVTGWGAigedeSLPSPNTLQEVQVAiinnsmcnhmykkpdfrTNIWGD 230
Cdd:COG3591  81 LRLDEPLG--DTTGWLGLAFNDAPLAGEP-VTIIGYPG-----DRPKDLSLDCSGRV-----------------TGVQGN 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 11055972 231 MVCAGTpeggkDACFGDSGGPLACDQDTVWYQVGVVSWGiGCGRPNRpGVY 281
Cdd:COG3591 136 RLSYDC-----DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVR 179
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
66-185 1.86e-03

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: 37.53  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11055972    66 WPWQGSLRVWGNHLCGATLLNRRWVLTAAHCFQKDNDPFDW-TVQFGELTSRPSLwnlqaysnRYQIEDIFLSPKYSEQY 144
Cdd:pfam09342   1 WPWIAKVYLDGNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGGAKTLKSI--------EGPYEQIVRVDCRHDIP 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 11055972   145 PNDIALLKLSSPVTYNNFIQPICLLNSTYKFENRTDCWVTG 185
Cdd:pfam09342  73 ESEISLLHLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
 
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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