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Conserved domains on  [gi|1622891971|ref|XP_028694357|]
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prostate-specific antigen isoform X2 [Macaca mulatta]

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 ...
103-255 3.27e-38

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: 133.94  E-value: 3.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971 103 CFL---PSNSVILLGRHNPYYPEDTGQVFQVSHSFPHPLYNMsllknrylgpgDDSSHDLMLLRLSEPAEITDAVQVLDL 179
Cdd:cd00190    43 CVYssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNP-----------STYDNDIALLKLKRPVTLSDNVRPICL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971 180 PT--WEPELGTTCYASGWGSIEPEEhLTPKKLQCVDLHIISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTCSaiGDSYG 255
Cdd:cd00190   112 PSsgYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAYSYggTITDNMLCAGGLEGGKDACQ--GDSGG 188
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
103-255 3.27e-38

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: 133.94  E-value: 3.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971 103 CFL---PSNSVILLGRHNPYYPEDTGQVFQVSHSFPHPLYNMsllknrylgpgDDSSHDLMLLRLSEPAEITDAVQVLDL 179
Cdd:cd00190    43 CVYssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNP-----------STYDNDIALLKLKRPVTLSDNVRPICL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971 180 PT--WEPELGTTCYASGWGSIEPEEhLTPKKLQCVDLHIISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTCSaiGDSYG 255
Cdd:cd00190   112 PSsgYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAYSYggTITDNMLCAGGLEGGKDACQ--GDSGG 188
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
103-255 9.42e-37

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: 129.72  E-value: 9.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971  103 CFL---PSNSVILLGRHNPYYPEDtGQVFQVSHSFPHPLYNMSLLknrylgpgddsSHDLMLLRLSEPAEITDAVQVLDL 179
Cdd:smart00020  44 CVRgsdPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHPNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICL 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971  180 PTW--EPELGTTCYASGWGSIEPEEHLTPKKLQCVDLHIISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTCSaiGDSYG 255
Cdd:smart00020 112 PSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGggAITDNMLCAGGLEGGKDACQ--GDSGG 189
Trypsin pfam00089
Trypsin;
99-266 2.33e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 112.92  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971  99 HSCICFLPSNSVIL---------------LGRHNPYYPEDTGQVFQVSHSFPHPLYNmsllknrylgpGDDSSHDLMLLR 163
Cdd:pfam00089  25 HFCGGSLISENWVLtaahcvsgasdvkvvLGAHNIVLREGGEQKFDVEKIIVHPNYN-----------PDTLDNDIALLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971 164 LSEPAEITDAVQVLDLPTWEPEL--GTTCYASGWGSIEPEEhlTPKKLQCVDLHIISNDVCAQVHSQKVTKFMLCAGSwm 241
Cdd:pfam00089  94 LESPVTLGDTVRPICLPDASSDLpvGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA-- 169
                         170       180
                  ....*....|....*....|....*
gi 1622891971 242 GGKSTCSaiGDSYGTVHVSLHSAHG 266
Cdd:pfam00089 170 GGKDACQ--GDSGGPLVCSDGELIG 192
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
103-255 3.27e-38

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: 133.94  E-value: 3.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971 103 CFL---PSNSVILLGRHNPYYPEDTGQVFQVSHSFPHPLYNMsllknrylgpgDDSSHDLMLLRLSEPAEITDAVQVLDL 179
Cdd:cd00190    43 CVYssaPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNP-----------STYDNDIALLKLKRPVTLSDNVRPICL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971 180 PT--WEPELGTTCYASGWGSIEPEEhLTPKKLQCVDLHIISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTCSaiGDSYG 255
Cdd:cd00190   112 PSsgYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVPIVSNAECKRAYSYggTITDNMLCAGGLEGGKDACQ--GDSGG 188
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
103-255 9.42e-37

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: 129.72  E-value: 9.42e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971  103 CFL---PSNSVILLGRHNPYYPEDtGQVFQVSHSFPHPLYNMSLLknrylgpgddsSHDLMLLRLSEPAEITDAVQVLDL 179
Cdd:smart00020  44 CVRgsdPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIHPNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICL 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971  180 PTW--EPELGTTCYASGWGSIEPEEHLTPKKLQCVDLHIISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTCSaiGDSYG 255
Cdd:smart00020 112 PSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNATCRRAYSGggAITDNMLCAGGLEGGKDACQ--GDSGG 189
Trypsin pfam00089
Trypsin;
99-266 2.33e-30

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 112.92  E-value: 2.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971  99 HSCICFLPSNSVIL---------------LGRHNPYYPEDTGQVFQVSHSFPHPLYNmsllknrylgpGDDSSHDLMLLR 163
Cdd:pfam00089  25 HFCGGSLISENWVLtaahcvsgasdvkvvLGAHNIVLREGGEQKFDVEKIIVHPNYN-----------PDTLDNDIALLK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891971 164 LSEPAEITDAVQVLDLPTWEPEL--GTTCYASGWGSIEPEEhlTPKKLQCVDLHIISNDVCAQVHSQKVTKFMLCAGSwm 241
Cdd:pfam00089  94 LESPVTLGDTVRPICLPDASSDLpvGTTCTVSGWGNTKTLG--PSDTLQEVTVPVVSRETCRSAYGGTVTDTMICAGA-- 169
                         170       180
                  ....*....|....*....|....*
gi 1622891971 242 GGKSTCSaiGDSYGTVHVSLHSAHG 266
Cdd:pfam00089 170 GGKDACQ--GDSGGPLVCSDGELIG 192
 
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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