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Conserved domains on  [gi|21614533|ref|NP_659206|]
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testisin isoform 3 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 ...
42-269 1.15e-79

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: 241.03  E-value: 1.15e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533  42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYF 120
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV----YSSAPSNYTVRLGSH----DLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 121 VSNIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAII 199
Cdd:cd00190  73 VKKVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 200 NNSMCNHLFLKYSFRKDIF---GDM--------GDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFEWIQ 268
Cdd:cd00190 151 SNAECKRAYSYGGTITDNMlcaGGLeggkdacqGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                .
gi 21614533 269 K 269
Cdd:cd00190 231 K 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-269 1.15e-79

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: 241.03  E-value: 1.15e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533  42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYF 120
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV----YSSAPSNYTVRLGSH----DLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 121 VSNIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAII 199
Cdd:cd00190  73 VKKVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 200 NNSMCNHLFLKYSFRKDIF---GDM--------GDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFEWIQ 268
Cdd:cd00190 151 SNAECKRAYSYGGTITDNMlcaGGLeggkdacqGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                .
gi 21614533 269 K 269
Cdd:cd00190 231 K 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-267 1.00e-77

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: 236.04  E-value: 1.00e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533     41 RIVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQltsmpSFWSLQAYYTRY 119
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV----RGSDPSNIRVRLGS-----HDLSSGEEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533    120 FVSNIYLSPRY-LGNSPYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeALPSPHTLQEVQVAI 198
Cdd:smart00020  72 KVSKVIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533    199 INNSMCNHlflKYSFRKDIFGDM--------------GDSGGPLACNKNGlWYQIGVVSWGVGCGRPNRPGVYTNISHHF 264
Cdd:smart00020 151 VSNATCRR---AYSGGGAITDNMlcaggleggkdacqGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYL 226

                   ...
gi 21614533    265 EWI 267
Cdd:smart00020 227 DWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-272 1.61e-53

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 175.22  E-value: 1.61e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533  26 AAPLSGpCGRRVITSRIVGGEDAELGRWPWQGSLRLWD---SHVCGVSLLSHRWALTAAHCFETYSdlsdPSGWMVQFGQ 102
Cdd:COG5640  16 ALALAA-APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG----PSDLRVVIGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 103 LTSMPSfwslQAyyTRYFVSNIYLSPRYLGNSP-YDIALVKLSAPVTytkHIQPICLQASTFEFENRTDCWVTGWGYIKE 181
Cdd:COG5640  91 TDLSTS----GG--TVVKVARIVVHPDYDPATPgNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 182 DEALPSPhTLQEVQVAIINNSMCNhlflkySFRKDIFGDM--------------GDSGGPLACNKNGLWYQIGVVSWGVG 247
Cdd:COG5640 162 GPGSQSG-TLRKADVPVVSDATCA------AYGGFDGGTMlcagypeggkdacqGDSGGPLVVKDGGGWVLVGVVSWGGG 234
                       250       260
                ....*....|....*....|....*
gi 21614533 248 CGRPNRPGVYTNISHHFEWIQKLMA 272
Cdd:COG5640 235 PCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
42-267 7.28e-53

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 172.24  E-value: 7.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533    42 IVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetysdlSDPSGWMVQFGQLTSMPSFWSLQAYYTRYF 120
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV------SGASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533   121 VSNIYLSPRYLGNspyDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDEalpSPHTLQEVQVAIIN 200
Cdd:pfam00089  75 IVHPNYNPDTLDN---DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21614533   201 NSMCNHLFLKYSFRKDIFGD-------MGDSGGPLACNKNglwYQIGVVSWGVGCGRPNRPGVYTNISHHFEWI 267
Cdd:pfam00089 149 RETCRSAYGGTVTDTMICAGaggkdacQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-269 1.15e-79

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: 241.03  E-value: 1.15e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533  42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYF 120
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV----YSSAPSNYTVRLGSH----DLSSNEGGGQVIK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 121 VSNIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAII 199
Cdd:cd00190  73 VKKVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 200 NNSMCNHLFLKYSFRKDIF---GDM--------GDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFEWIQ 268
Cdd:cd00190 151 SNAECKRAYSYGGTITDNMlcaGGLeggkdacqGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230

                .
gi 21614533 269 K 269
Cdd:cd00190 231 K 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-267 1.00e-77

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: 236.04  E-value: 1.00e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533     41 RIVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetysDLSDPSGWMVQFGQltsmpSFWSLQAYYTRY 119
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV----RGSDPSNIRVRLGS-----HDLSSGEEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533    120 FVSNIYLSPRY-LGNSPYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeALPSPHTLQEVQVAI 198
Cdd:smart00020  72 KVSKVIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPI 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533    199 INNSMCNHlflKYSFRKDIFGDM--------------GDSGGPLACNKNGlWYQIGVVSWGVGCGRPNRPGVYTNISHHF 264
Cdd:smart00020 151 VSNATCRR---AYSGGGAITDNMlcaggleggkdacqGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYL 226

                   ...
gi 21614533    265 EWI 267
Cdd:smart00020 227 DWI 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-272 1.61e-53

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 175.22  E-value: 1.61e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533  26 AAPLSGpCGRRVITSRIVGGEDAELGRWPWQGSLRLWD---SHVCGVSLLSHRWALTAAHCFETYSdlsdPSGWMVQFGQ 102
Cdd:COG5640  16 ALALAA-APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDG----PSDLRVVIGS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 103 LTSMPSfwslQAyyTRYFVSNIYLSPRYLGNSP-YDIALVKLSAPVTytkHIQPICLQASTFEFENRTDCWVTGWGYIKE 181
Cdd:COG5640  91 TDLSTS----GG--TVVKVARIVVHPDYDPATPgNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 182 DEALPSPhTLQEVQVAIINNSMCNhlflkySFRKDIFGDM--------------GDSGGPLACNKNGLWYQIGVVSWGVG 247
Cdd:COG5640 162 GPGSQSG-TLRKADVPVVSDATCA------AYGGFDGGTMlcagypeggkdacqGDSGGPLVVKDGGGWVLVGVVSWGGG 234
                       250       260
                ....*....|....*....|....*
gi 21614533 248 CGRPNRPGVYTNISHHFEWIQKLMA 272
Cdd:COG5640 235 PCAAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
42-267 7.28e-53

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 172.24  E-value: 7.28e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533    42 IVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetysdlSDPSGWMVQFGQLTSMPSFWSLQAYYTRYF 120
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV------SGASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533   121 VSNIYLSPRYLGNspyDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDEalpSPHTLQEVQVAIIN 200
Cdd:pfam00089  75 IVHPNYNPDTLDN---DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVS 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21614533   201 NSMCNHLFLKYSFRKDIFGD-------MGDSGGPLACNKNglwYQIGVVSWGVGCGRPNRPGVYTNISHHFEWI 267
Cdd:pfam00089 149 RETCRSAYGGTVTDTMICAGaggkdacQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
70-273 8.76e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 60.08  E-value: 8.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533  70 SLLSHRWALTAAHCFETYSDLSDPSGWMVQFGQLTSMPSFWSlqayYTRYFVSNIYLSPrylGNSPYDIALVKLSAPVTY 149
Cdd:COG3591  17 TLIGPNLVLTAGHCVYDGAGGGWATNIVFVPGYNGGPYGTAT----ATRFRVPPGWVAS---GDAGYDYALLRLDEPLGD 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21614533 150 TkhIQPICLQASTFEFENRTdcwVTGWGYIKEDealPSPHTLQEV-QVAIINNSmcnhlFLKYSFrkDIFGdmGDSGGPL 228
Cdd:COG3591  90 T--TGWLGLAFNDAPLAGEP---VTIIGYPGDR---PKDLSLDCSgRVTGVQGN-----RLSYDC--DTTG--GSSGSPV 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 21614533 229 ACNKNGLWYQIGVVSWGvGCGRPNRpGVYTNiSHHFEWIQKLMAQ 273
Cdd:COG3591 153 LDDSDGGGRVVGVHSAG-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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