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Conserved domains on  [gi|71834853|ref|NP_001025218|]
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prostate-specific antigen 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

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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 ...
25-209 1.91e-63

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: 197.50  E-value: 1.91e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQVFQVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853 100 LYDMsllknrflrpgDDSSHDLMLLRLSEPAELTDAVKVMDLPTQ--EPALGTTCYASGWGSIEPEEFLtPKKLQCVDLH 177
Cdd:cd00190  81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190
                ....*....|....*....|....*....|....
gi 71834853 178 VISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTC 209
Cdd:cd00190 149 IVSNAECKRAYSYggTITDNMLCAGGLEGGKDAC 182
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-209 1.91e-63

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: 197.50  E-value: 1.91e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQVFQVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853 100 LYDMsllknrflrpgDDSSHDLMLLRLSEPAELTDAVKVMDLPTQ--EPALGTTCYASGWGSIEPEEFLtPKKLQCVDLH 177
Cdd:cd00190  81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190
                ....*....|....*....|....*....|....
gi 71834853 178 VISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTC 209
Cdd:cd00190 149 IVSNAECKRAYSYggTITDNMLCAGGLEGGKDAC 182
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-209 4.12e-63

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: 196.36  E-value: 4.12e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853     24 RIVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDtGQVFQVSHSFPH 98
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853     99 PLYDMSLLknrflrpgddsSHDLMLLRLSEPAELTDAVKVMDLPT--QEPALGTTCYASGWGSIEPEEFLTPKKLQCVDL 176
Cdd:smart00020  80 PNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 71834853    177 HVISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTC 209
Cdd:smart00020 149 PIVSNATCRRAYSGggAITDNMLCAGGLEGGKDAC 183
Trypsin pfam00089
Trypsin;
25-209 1.03e-50

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 164.54  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853    25 IVGGWECEKHSQPWQVLVASRGRAV-CGGVLVHPQWVLTAAHCIRNKS--VILLGRHSLFHPEDTGQVFQVSHSFPHPLY 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASdvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853   102 DmsllknrflrpGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEP--ALGTTCYASGWGSiePEEFLTPKKLQCVDLHVI 179
Cdd:pfam00089  81 N-----------PDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVV 147
                         170       180       190
                  ....*....|....*....|....*....|
gi 71834853   180 SNDVCAQVHPQKVTKFMLCAGrwTGGKSTC 209
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAG--AGGKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-210 5.04e-33

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 120.14  E-value: 5.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853  23 SRIVGGWECEKHSQPWQVLVASRG---RAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFhpEDTGQVFQVSHS 95
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdlrVVIGSTDLS--TSGGTVVKVARI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853  96 FPHPLYDMSllknrflrpgdDSSHDLMLLRLSEPAELTDAVKVMDlPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVD 175
Cdd:COG5640 107 VVHPDYDPA-----------TPGNDIALLKLATPVPGVAPAPLAT-SADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                       170       180       190
                ....*....|....*....|....*....|....*
gi 71834853 176 LHVISNDVCAqVHPQKVTKFMLCAGRWTGGKSTCS 210
Cdd:COG5640 175 VPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQ 208
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
25-209 1.91e-63

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: 197.50  E-value: 1.91e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDTGQVFQVSHSFPHP 99
Cdd:cd00190   1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSSAPsnytVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853 100 LYDMsllknrflrpgDDSSHDLMLLRLSEPAELTDAVKVMDLPTQ--EPALGTTCYASGWGSIEPEEFLtPKKLQCVDLH 177
Cdd:cd00190  81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSSgyNLPAGTTCTVSGWGRTSEGGPL-PDVLQEVNVP 148
                       170       180       190
                ....*....|....*....|....*....|....
gi 71834853 178 VISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTC 209
Cdd:cd00190 149 IVSNAECKRAYSYggTITDNMLCAGGLEGGKDAC 182
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-209 4.12e-63

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: 196.36  E-value: 4.12e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853     24 RIVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFHPEDtGQVFQVSHSFPH 98
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853     99 PLYDMSLLknrflrpgddsSHDLMLLRLSEPAELTDAVKVMDLPT--QEPALGTTCYASGWGSIEPEEFLTPKKLQCVDL 176
Cdd:smart00020  80 PNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICLPSsnYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 71834853    177 HVISNDVCAQVHPQ--KVTKFMLCAGRWTGGKSTC 209
Cdd:smart00020 149 PIVSNATCRRAYSGggAITDNMLCAGGLEGGKDAC 183
Trypsin pfam00089
Trypsin;
25-209 1.03e-50

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 164.54  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853    25 IVGGWECEKHSQPWQVLVASRGRAV-CGGVLVHPQWVLTAAHCIRNKS--VILLGRHSLFHPEDTGQVFQVSHSFPHPLY 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASdvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853   102 DmsllknrflrpGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEP--ALGTTCYASGWGSiePEEFLTPKKLQCVDLHVI 179
Cdd:pfam00089  81 N-----------PDTLDNDIALLKLESPVTLGDTVRPICLPDASSdlPVGTTCTVSGWGN--TKTLGPSDTLQEVTVPVV 147
                         170       180       190
                  ....*....|....*....|....*....|
gi 71834853   180 SNDVCAQVHPQKVTKFMLCAGrwTGGKSTC 209
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAG--AGGKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
23-210 5.04e-33

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 120.14  E-value: 5.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853  23 SRIVGGWECEKHSQPWQVLVASRG---RAVCGGVLVHPQWVLTAAHCIRNKSV----ILLGRHSLFhpEDTGQVFQVSHS 95
Cdd:COG5640  29 PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdlrVVIGSTDLS--TSGGTVVKVARI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853  96 FPHPLYDMSllknrflrpgdDSSHDLMLLRLSEPAELTDAVKVMDlPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVD 175
Cdd:COG5640 107 VVHPDYDPA-----------TPGNDIALLKLATPVPGVAPAPLAT-SADAAAPGTPATVAGWGRTSEGPGSQSGTLRKAD 174
                       170       180       190
                ....*....|....*....|....*....|....*
gi 71834853 176 LHVISNDVCAqVHPQKVTKFMLCAGRWTGGKSTCS 210
Cdd:COG5640 175 VPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQ 208
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
41-163 8.95e-07

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 47.75  E-value: 8.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71834853  41 LVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHP---EDTGQVFQVSHSFPHPLYDMSllknrflrpgDDS 117
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGWATNIVFVPgynGGPYGTATATRFRVPPGWVAS----------GDA 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 71834853 118 SHDLMLLRLSEPaeLTDAVKVMDL-PTQEPALGTTCYASGWGSIEPE 163
Cdd:COG3591  75 GYDYALLRLDEP--LGDTTGWLGLaFNDAPLAGEPVTIIGYPGDRPK 119
 
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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