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Conserved domains on  [gi|1034593421|ref|XP_016878364|]
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testisin isoform X1 [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 ...
42-267 5.00e-80

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: 242.18  E-value: 5.00e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYFVS 120
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV--YSSAPSNYTVRLGSH----DLSSNEGGGQVIKVK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 121 NIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAIINN 199
Cdd:cd00190    75 KVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034593421 200 SMCNHLFLKYSFRKDIF---GDM--------GDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFEWIQK 267
Cdd:cd00190   153 AECKRAYSYGGTITDNMlcaGGLeggkdacqGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-267 5.00e-80

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: 242.18  E-value: 5.00e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYFVS 120
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV--YSSAPSNYTVRLGSH----DLSSNEGGGQVIKVK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 121 NIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAIINN 199
Cdd:cd00190    75 KVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034593421 200 SMCNHLFLKYSFRKDIF---GDM--------GDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFEWIQK 267
Cdd:cd00190   153 AECKRAYSYGGTITDNMlcaGGLeggkdacqGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-265 4.33e-78

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: 236.81  E-value: 4.33e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421   41 RIVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetDLSDPSGWMVQFGQltsmpSFWSLQAYYTRYFV 119
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV--RGSDPSNIRVRLGS-----HDLSSGEEGQVIKV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  120 SNIYLSPRY-LGNSPYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeALPSPHTLQEVQVAIIN 198
Cdd:smart00020  74 SKVIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  199 NSMCNHlflKYSFRKDIFGDM--------------GDSGGPLACNKNGlWYQIGVVSWGVGCGRPNRPGVYTNISHHFEW 264
Cdd:smart00020 153 NATCRR---AYSGGGAITDNMlcaggleggkdacqGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 1034593421  265 I 265
Cdd:smart00020 229 I 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-270 5.04e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 176.76  E-value: 5.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  26 AAPLSGpCGRRVITSRIVGGEDAELGRWPWQGSLRLWD---SHVCGVSLLSHRWALTAAHCFETDlsDPSGWMVQFGQLT 102
Cdd:COG5640    16 ALALAA-APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 103 SMPSfwslQAyyTRYFVSNIYLSPRYLGNSP-YDIALVKLSAPVTytkHIQPICLQASTFEFENRTDCWVTGWGYIKEDE 181
Cdd:COG5640    93 LSTS----GG--TVVKVARIVVHPDYDPATPgNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 182 ALPSPhTLQEVQVAIINNSMCNhlflkySFRKDIFGDM--------------GDSGGPLACNKNGLWYQIGVVSWGVGCG 247
Cdd:COG5640   164 GSQSG-TLRKADVPVVSDATCA------AYGGFDGGTMlcagypeggkdacqGDSGGPLVVKDGGGWVLVGVVSWGGGPC 236
                         250       260
                  ....*....|....*....|...
gi 1034593421 248 RPNRPGVYTNISHHFEWIQKLMA 270
Cdd:COG5640   237 AAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
42-265 3.25e-53

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 173.01  E-value: 3.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  42 IVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetdlSDPSGWMVQFGQLTSMPSFWSLQAYYTRYFVS 120
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV----SGASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 121 NIYLSPRYLGNspyDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDEalpSPHTLQEVQVAIINNS 200
Cdd:pfam00089  77 HPNYNPDTLDN---DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034593421 201 MCNHLFLKYSFRKDIFGD-------MGDSGGPLACNKNglwYQIGVVSWGVGCGRPNRPGVYTNISHHFEWI 265
Cdd:pfam00089 151 TCRSAYGGTVTDTMICAGaggkdacQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
42-267 5.00e-80

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: 242.18  E-value: 5.00e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  42 IVGGEDAELGRWPWQGSLRL-WDSHVCGVSLLSHRWALTAAHCFetDLSDPSGWMVQFGQLtsmpSFWSLQAYYTRYFVS 120
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYtGGRHFCGGSLISPRWVLTAAHCV--YSSAPSNYTVRLGSH----DLSSNEGGGQVIKVK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 121 NIYLSPRYLGNS-PYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeaLPSPHTLQEVQVAIINN 199
Cdd:cd00190    75 KVIVHPNYNPSTyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEG--GPLPDVLQEVNVPIVSN 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034593421 200 SMCNHLFLKYSFRKDIF---GDM--------GDSGGPLACNKNGLWYQIGVVSWGVGCGRPNRPGVYTNISHHFEWIQK 267
Cdd:cd00190   153 AECKRAYSYGGTITDNMlcaGGLeggkdacqGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
41-265 4.33e-78

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: 236.81  E-value: 4.33e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421   41 RIVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetDLSDPSGWMVQFGQltsmpSFWSLQAYYTRYFV 119
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV--RGSDPSNIRVRLGS-----HDLSSGEEGQVIKV 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  120 SNIYLSPRY-LGNSPYDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDeALPSPHTLQEVQVAIIN 198
Cdd:smart00020  74 SKVIIHPNYnPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEG-AGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  199 NSMCNHlflKYSFRKDIFGDM--------------GDSGGPLACNKNGlWYQIGVVSWGVGCGRPNRPGVYTNISHHFEW 264
Cdd:smart00020 153 NATCRR---AYSGGGAITDNMlcaggleggkdacqGDSGGPLVCNDGR-WVLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228

                   .
gi 1034593421  265 I 265
Cdd:smart00020 229 I 229
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
26-270 5.04e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 176.76  E-value: 5.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  26 AAPLSGpCGRRVITSRIVGGEDAELGRWPWQGSLRLWD---SHVCGVSLLSHRWALTAAHCFETDlsDPSGWMVQFGQLT 102
Cdd:COG5640    16 ALALAA-APAADAAPAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGD--GPSDLRVVIGSTD 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 103 SMPSfwslQAyyTRYFVSNIYLSPRYLGNSP-YDIALVKLSAPVTytkHIQPICLQASTFEFENRTDCWVTGWGYIKEDE 181
Cdd:COG5640    93 LSTS----GG--TVVKVARIVVHPDYDPATPgNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 182 ALPSPhTLQEVQVAIINNSMCNhlflkySFRKDIFGDM--------------GDSGGPLACNKNGLWYQIGVVSWGVGCG 247
Cdd:COG5640   164 GSQSG-TLRKADVPVVSDATCA------AYGGFDGGTMlcagypeggkdacqGDSGGPLVVKDGGGWVLVGVVSWGGGPC 236
                         250       260
                  ....*....|....*....|...
gi 1034593421 248 RPNRPGVYTNISHHFEWIQKLMA 270
Cdd:COG5640   237 AAGYPGVYTRVSAYRDWIKSTAG 259
Trypsin pfam00089
Trypsin;
42-265 3.25e-53

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 173.01  E-value: 3.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  42 IVGGEDAELGRWPWQGSLRLWD-SHVCGVSLLSHRWALTAAHCFetdlSDPSGWMVQFGQLTSMPSFWSLQAYYTRYFVS 120
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSgKHFCGGSLISENWVLTAAHCV----SGASDVKVVLGAHNIVLREGGEQKFDVEKIIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 121 NIYLSPRYLGNspyDIALVKLSAPVTYTKHIQPICLQASTFEFENRTDCWVTGWGYIKEDEalpSPHTLQEVQVAIINNS 200
Cdd:pfam00089  77 HPNYNPDTLDN---DIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLG---PSDTLQEVTVPVVSRE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034593421 201 MCNHLFLKYSFRKDIFGD-------MGDSGGPLACNKNglwYQIGVVSWGVGCGRPNRPGVYTNISHHFEWI 265
Cdd:pfam00089 151 TCRSAYGGTVTDTMICAGaggkdacQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
70-271 3.67e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.45  E-value: 3.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421  70 SLLSHRWALTAAHCFETDLSD--PSGWMVQFGQLTSMPSFWSlqayYTRYFVSNIYLSPrylGNSPYDIALVKLSAPVTY 147
Cdd:COG3591    17 TLIGPNLVLTAGHCVYDGAGGgwATNIVFVPGYNGGPYGTAT----ATRFRVPPGWVAS---GDAGYDYALLRLDEPLGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034593421 148 TkhIQPICLQASTFEFENRTdcwVTGWGYIKEDealPSPHTLQEV-QVAIINNSmcnhlFLKYSFrkDIFGdmGDSGGPL 226
Cdd:COG3591    90 T--TGWLGLAFNDAPLAGEP---VTIIGYPGDR---PKDLSLDCSgRVTGVQGN-----RLSYDC--DTTG--GSSGSPV 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034593421 227 ACNKNGLWYQIGVVSWGvGCGRPNRpGVYTNiSHHFEWIQKLMAQ 271
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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