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Conserved domains on  [gi|1622891974|ref|XP_014979905|]
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prostate-specific antigen isoform X3 [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 ...
25-209 5.05e-62

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: 194.03  E-value: 5.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRS----NSVILLGRHNPYYPEDTGQVFQVSHSFPHP 99
Cdd:cd00190     1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974 100 LYNMsllknrylgpgDDSSHDLMLLRLSEPAEITDAVQVLDLPT--WEPELGTTCYASGWGSIEPEEhLTPKKLQCVDLH 177
Cdd:cd00190    81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVP 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622891974 178 IISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTC 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 5.05e-62

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: 194.03  E-value: 5.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRS----NSVILLGRHNPYYPEDTGQVFQVSHSFPHP 99
Cdd:cd00190     1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974 100 LYNMsllknrylgpgDDSSHDLMLLRLSEPAEITDAVQVLDLPT--WEPELGTTCYASGWGSIEPEEhLTPKKLQCVDLH 177
Cdd:cd00190    81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVP 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622891974 178 IISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTC 209
Cdd:cd00190   149 IVSNAECKRAYSYggTITDNMLCAGGLEGGKDAC 182
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-209 1.81e-61

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: 192.51  E-value: 1.81e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974   24 RIVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRSNSV----ILLGRHNPYYPEDtGQVFQVSHSFPH 98
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974   99 PLYNMSLLknrylgpgddsSHDLMLLRLSEPAEITDAVQVLDLPTW--EPELGTTCYASGWGSIEPEEHLTPKKLQCVDL 176
Cdd:smart00020  80 PNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622891974  177 HIISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTC 209
Cdd:smart00020 149 PIVSNATCRRAYSGggAITDNMLCAGGLEGGKDAC 183
Trypsin pfam00089
Trypsin;
25-209 3.64e-49

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 160.69  E-value: 3.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974  25 IVGGWECEKHSQPWQVLVASRGRAV-CGGVLVHPQWVLTAAHCIRSNS--VILLGRHNPYYPEDTGQVFQVSHSFPHPLY 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASdvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974 102 NmsllknrylgpGDDSSHDLMLLRLSEPAEITDAVQVLDLPTWEPEL--GTTCYASGWGSIEPEEhlTPKKLQCVDLHII 179
Cdd:pfam00089  81 N-----------PDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpvGTTCTVSGWGNTKTLG--PSDTLQEVTVPVV 147
                         170       180       190
                  ....*....|....*....|....*....|
gi 1622891974 180 SNDVCAQVHSQKVTKFMLCAGSwmGGKSTC 209
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAGA--GGKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
3-210 6.78e-32

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 117.06  E-value: 6.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974   3 VLVVFLTLSVTWIGAAPlilSRIVGGWECEKHSQPWQVLVASRG---RAVCGGVLVHPQWVLTAAHCIRSNSV----ILL 75
Cdd:COG5640    12 AAALALALAAAPAADAA---PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdlrVVI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974  76 GRHNpyYPEDTGQVFQVSHSFPHPLYNMSllknrylgpgdDSSHDLMLLRLSEPAeitDAVQVLDLPT--WEPELGTTCY 153
Cdd:COG5640    89 GSTD--LSTSGGTVVKVARIVVHPDYDPA-----------TPGNDIALLKLATPV---PGVAPAPLATsaDAAAPGTPAT 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891974 154 ASGWGSIEPEEHLTPKKLQCVDLHIISNDVCAqVHSQKVTKFMLCAGSWMGGKSTCS 210
Cdd:COG5640   153 VAGWGRTSEGPGSQSGTLRKADVPVVSDATCA-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 5.05e-62

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: 194.03  E-value: 5.05e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974  25 IVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRS----NSVILLGRHNPYYPEDTGQVFQVSHSFPHP 99
Cdd:cd00190     1 IVGGSEAKIGSFPWQVsLQYTGGRHFCGGSLISPRWVLTAAHCVYSsapsNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974 100 LYNMsllknrylgpgDDSSHDLMLLRLSEPAEITDAVQVLDLPT--WEPELGTTCYASGWGSIEPEEhLTPKKLQCVDLH 177
Cdd:cd00190    81 NYNP-----------STYDNDIALLKLKRPVTLSDNVRPICLPSsgYNLPAGTTCTVSGWGRTSEGG-PLPDVLQEVNVP 148
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622891974 178 IISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTC 209
Cdd:cd00190   149 IVSNAECKRAYSYggTITDNMLCAGGLEGGKDAC 182
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
24-209 1.81e-61

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: 192.51  E-value: 1.81e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974   24 RIVGGWECEKHSQPWQV-LVASRGRAVCGGVLVHPQWVLTAAHCIRSNSV----ILLGRHNPYYPEDtGQVFQVSHSFPH 98
Cdd:smart00020   1 RIVGGSEANIGSFPWQVsLQYGGGRHFCGGSLISPRWVLTAAHCVRGSDPsnirVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974   99 PLYNMSLLknrylgpgddsSHDLMLLRLSEPAEITDAVQVLDLPTW--EPELGTTCYASGWGSIEPEEHLTPKKLQCVDL 176
Cdd:smart00020  80 PNYNPSTY-----------DNDIALLKLKEPVTLSDNVRPICLPSSnyNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNV 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1622891974  177 HIISNDVCAQVHSQ--KVTKFMLCAGSWMGGKSTC 209
Cdd:smart00020 149 PIVSNATCRRAYSGggAITDNMLCAGGLEGGKDAC 183
Trypsin pfam00089
Trypsin;
25-209 3.64e-49

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 160.69  E-value: 3.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974  25 IVGGWECEKHSQPWQVLVASRGRAV-CGGVLVHPQWVLTAAHCIRSNS--VILLGRHNPYYPEDTGQVFQVSHSFPHPLY 101
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHfCGGSLISENWVLTAAHCVSGASdvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974 102 NmsllknrylgpGDDSSHDLMLLRLSEPAEITDAVQVLDLPTWEPEL--GTTCYASGWGSIEPEEhlTPKKLQCVDLHII 179
Cdd:pfam00089  81 N-----------PDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLpvGTTCTVSGWGNTKTLG--PSDTLQEVTVPVV 147
                         170       180       190
                  ....*....|....*....|....*....|
gi 1622891974 180 SNDVCAQVHSQKVTKFMLCAGSwmGGKSTC 209
Cdd:pfam00089 148 SRETCRSAYGGTVTDTMICAGA--GGKDAC 175
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
3-210 6.78e-32

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 117.06  E-value: 6.78e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974   3 VLVVFLTLSVTWIGAAPlilSRIVGGWECEKHSQPWQVLVASRG---RAVCGGVLVHPQWVLTAAHCIRSNSV----ILL 75
Cdd:COG5640    12 AAALALALAAAPAADAA---PAIVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPsdlrVVI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974  76 GRHNpyYPEDTGQVFQVSHSFPHPLYNMSllknrylgpgdDSSHDLMLLRLSEPAeitDAVQVLDLPT--WEPELGTTCY 153
Cdd:COG5640    89 GSTD--LSTSGGTVVKVARIVVHPDYDPA-----------TPGNDIALLKLATPV---PGVAPAPLATsaDAAAPGTPAT 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622891974 154 ASGWGSIEPEEHLTPKKLQCVDLHIISNDVCAqVHSQKVTKFMLCAGSWMGGKSTCS 210
Cdd:COG5640   153 VAGWGRTSEGPGSQSGTLRKADVPVVSDATCA-AYGGFDGGTMLCAGYPEGGKDACQ 208
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
41-163 3.87e-06

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 46.21  E-value: 3.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622891974  41 LVASRGRAVCGGVLVHPQWVLTAAHCI--------RSNSVILLGRHNPYYPEDTGQVFQVshsfpHPLYNMSllknrylg 112
Cdd:COG3591     5 LETDGGGGVCTGTLIGPNLVLTAGHCVydgagggwATNIVFVPGYNGGPYGTATATRFRV-----PPGWVAS-------- 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622891974 113 pgDDSSHDLMLLRLSEPaeITDAVQVLDL-PTWEPELGTTCYASGWGSIEPE 163
Cdd:COG3591    72 --GDAGYDYALLRLDEP--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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