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Conserved domains on  [gi|5803197|ref|NP_006790|]
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testisin isoform 1 preproprotein [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

 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 ...
42-283 2.07e-92

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: 274.15  E-value: 2.07e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197   42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYF 120
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV----YSSAPSNYTVRLGSH----DLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  121 VSNIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAII 199
Cdd:cd00190  73 VKKVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  200 NNSMCNHlflKYSFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFE 279
Cdd:cd00190 151 SNAECKR---AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                ....
gi 5803197  280 WIQK 283
Cdd:cd00190 228 WIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-283 2.07e-92

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: 274.15  E-value: 2.07e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197   42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYF 120
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV----YSSAPSNYTVRLGSH----DLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  121 VSNIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAII 199
Cdd:cd00190  73 VKKVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  200 NNSMCNHlflKYSFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFE 279
Cdd:cd00190 151 SNAECKR---AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                ....
gi 5803197  280 WIQK 283
Cdd:cd00190 228 WIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-281 1.67e-90

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: 269.16  E-value: 1.67e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197      41 RIVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQltsmpSFWSLQAYYTRY 119
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV----RGSDPSNIRVRLGS-----HDLSSGEEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197     120 FVSNIYLSPRY-LGNSPYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeALPSPHTLQEVQVAI 198
Cdd:smart00020  72 KVSKVIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197     199 INNSMCNHlflKYSFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGlWYQIGVVSWGVGCGRPNRPGVYTNISHHF 278
Cdd:smart00020 151 VSNATCRR---AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYL 226

                   ...
gi 5803197     279 EWI 281
Cdd:smart00020 227 DWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-286 1.21e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 1.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197   26 AAPLSGpCGRRVITSRIVGGEDAELGRWPWQGSLRLWD---SHVCGVSLLSHRWALTAAHCFETYSdlsdPSGWMVQFGQ 102
Cdd:COG5640  16 ALALAA-APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG----PSDLRVVIGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  103 LTSMPSfwslQAyyTRYFVSNIYLSPRYLGNSP-YDIALVKLSAPVTytkHIQPICLQASTFEFENRTDCWVTGWGYIKE 181
Cdd:COG5640  91 TDLSTS----GG--TVVKVARIVVHPDYDPATPgNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  182 DEALPSPhTLQEVQVAIINNSMCNhlflkySFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGLWYQIGVVSWGVG 261
Cdd:COG5640 162 GPGSQSG-TLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGG 234
                       250       260
                ....*....|....*....|....*
gi 5803197  262 CGRPNRPGVYTNISHHFEWIQKLMA 286
Cdd:COG5640 235 PCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
42-281 2.92e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 194.20  E-value: 2.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197     42 IVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetysdlSDPSGWMVQFGQLTSMPSFWSLQAYYTRYF 120
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV------SGASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197    121 VSNIYLSPRYLGNspyDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDEalpSPHTLQEVQVAIIN 200
Cdd:pfam00089  75 IVHPNYNPDTLDN---DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197    201 NSMCNHlflkySFRKDIFGDMVCAGNaqGGKDACFGDSGGPLACNKNglwYQIGVVSWGVGCGRPNRPGVYTNISHHFEW 280
Cdd:pfam00089 149 RETCRS-----AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218

                  .
gi 5803197    281 I 281
Cdd:pfam00089 219 I 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-283 2.07e-92

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: 274.15  E-value: 2.07e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197   42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYF 120
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV----YSSAPSNYTVRLGSH----DLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  121 VSNIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAII 199
Cdd:cd00190  73 VKKVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  200 NNSMCNHlflKYSFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFE 279
Cdd:cd00190 151 SNAECKR---AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLD 227

                ....
gi 5803197  280 WIQK 283
Cdd:cd00190 228 WIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-281 1.67e-90

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: 269.16  E-value: 1.67e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197      41 RIVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQltsmpSFWSLQAYYTRY 119
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV----RGSDPSNIRVRLGS-----HDLSSGEEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197     120 FVSNIYLSPRY-LGNSPYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeALPSPHTLQEVQVAI 198
Cdd:smart00020  72 KVSKVIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197     199 INNSMCNHlflKYSFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGlWYQIGVVSWGVGCGRPNRPGVYTNISHHF 278
Cdd:smart00020 151 VSNATCRR---AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYL 226

                   ...
gi 5803197     279 EWI 281
Cdd:smart00020 227 DWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-286 1.21e-66

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.51  E-value: 1.21e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197   26 AAPLSGpCGRRVITSRIVGGEDAELGRWPWQGSLRLWD---SHVCGVSLLSHRWALTAAHCFETYSdlsdPSGWMVQFGQ 102
Cdd:COG5640  16 ALALAA-APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG----PSDLRVVIGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  103 LTSMPSfwslQAyyTRYFVSNIYLSPRYLGNSP-YDIALVKLSAPVTytkHIQPICLQASTFEFENRTDCWVTGWGYIKE 181
Cdd:COG5640  91 TDLSTS----GG--TVVKVARIVVHPDYDPATPgNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  182 DEALPSPhTLQEVQVAIINNSMCNhlflkySFRKDIFGDMVCAGNAQGGKDACFGDSGGPLACNKNGLWYQIGVVSWGVG 261
Cdd:COG5640 162 GPGSQSG-TLRKADVPVVSDATCA------AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGG 234
                       250       260
                ....*....|....*....|....*
gi 5803197  262 CGRPNRPGVYTNISHHFEWIQKLMA 286
Cdd:COG5640 235 PCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
42-281 2.92e-61

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 194.20  E-value: 2.92e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197     42 IVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetysdlSDPSGWMVQFGQLTSMPSFWSLQAYYTRYF 120
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV------SGASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197    121 VSNIYLSPRYLGNspyDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDEalpSPHTLQEVQVAIIN 200
Cdd:pfam00089  75 IVHPNYNPDTLDN---DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197    201 NSMCNHlflkySFRKDIFGDMVCAGNaqGGKDACFGDSGGPLACNKNglwYQIGVVSWGVGCGRPNRPGVYTNISHHFEW 280
Cdd:pfam00089 149 RETCRS-----AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDW 218

                  .
gi 5803197    281 I 281
Cdd:pfam00089 219 I 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
70-287 4.04e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.15  E-value: 4.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197   70 SLLSHRWALTAAHCFETYSDLSDPSGWMVQFGQLTSMPSFWSlqayYTRYFVSNIYLSPrylGNSPYDIALVKLSAPVTY 149
Cdd:COG3591  17 TLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTAT----ATRFRVPPGWVAS---GDAGYDYALLRLDEPLGD 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5803197  150 TkhIQPICLQASTFEFENRTdcwVTGWGYIKEDealPSPHTLQEV-QVAIINNSmcnhlFLKYSfrkdifgdmvCagnaq 228
Cdd:COG3591  90 T--TGWLGLAFNDAPLAGEP---VTIIGYPGDR---PKDLSLDCSgRVTGVQGN-----RLSYD----------C----- 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5803197  229 ggkDACFGDSGGPLACNKNGLWYQIGVVSWGvGCGRPNRpGVYTNiSHHFEWIQKLMAQ 287
Cdd:COG3591 142 ---DTTGGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVRLT-SAIVAALRAWASA 194
 
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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