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Conserved domains on  [gi|157829726]
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Chain A, Heparin Binding Protein

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

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 ...
1-214 1.93e-73

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  Cd Length: 232  Bit Score: 222.15  E-value: 1.93e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726   1 IVGGRKARPRQFPFLASIQ-NQGRHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRErQSRQTFSISSMSEN 79
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726  80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCR--- 155
Cdd:cd00190   80 pNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKray 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157829726 156 -------PNNVCTGVLTRRGGICNGDGGTPLVCE----GLAHGVASFSLGpCGRG--PDFFTRVALFRDWID 214
Cdd:cd00190  160 syggtitDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPnyPGVYTRVSSYLDWIQ 230
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-214 1.93e-73

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  Cd Length: 232  Bit Score: 222.15  E-value: 1.93e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726   1 IVGGRKARPRQFPFLASIQ-NQGRHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRErQSRQTFSISSMSEN 79
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726  80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCR--- 155
Cdd:cd00190   80 pNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKray 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157829726 156 -------PNNVCTGVLTRRGGICNGDGGTPLVCE----GLAHGVASFSLGpCGRG--PDFFTRVALFRDWID 214
Cdd:cd00190  160 syggtitDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPnyPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-213 2.11e-69

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: 211.77  E-value: 2.11e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726     1 IVGGRKARPRQFPFLASIQNQG-RHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQsrQTFSISSMSEN 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG--QVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726    80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGS-QRSGGRLSRFPRFVNVTVTPEDQCR-- 155
Cdd:smart00020  80 pNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCRra 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157829726   156 --------PNNVCTGVLTRRGGICNGDGGTPLVCE---GLAHGVASFSLGpCGRG--PDFFTRVALFRDWI 213
Cdd:smart00020 160 ysgggaitDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSG-CARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin.
1-213 4.86e-54

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 172.62  E-value: 4.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726    1 IVGGRKARPRQFPFLASIQN-QGRHFCGGALIHARFVMTAASCFQsqNPGVSTVVLGAYDLRRRErQSRQTFSISS-MSE 78
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS--GASDVQVVLGEHNIVLRE-GGEQKFDVAKvIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726   79 NGYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRlSRFPRFVNVTVTPEDQCR--- 155
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAGADLPVGTTCTVSGWGNTKTLGP-PDTLQEVTVPVVSRETCRsay 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157829726  156 -----PNNVCTGvlTRRGGICNGDGGTPLVCE-GLAHGVASFSLGpCGRG--PDFFTRVALFRDWI 213
Cdd:pfam00089 157 ggtvtDTMICAG--AGGKDACQGDSGGPLVCSdGELIGIVSWGYG-CASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-224 1.34e-24

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 99.95  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726   1 IVGGRKARPRQFPFLASIQNQGR-----HFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQTFSISS 75
Cdd:COG5640   33 IIGGSNANAGEYPSLVALVDRISdyvsgTFCGGSKLGGRYVLTAAHCADASSPISSDVNRVVVDLNDSSQAERGHVRTIY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726  76 MSEnGYDPQQNLNDLMLLQLDREANL--------TSSVTILP-----LPLQNATVeaGTRCQVAGWGSQRSGGRLSRfpr 142
Cdd:COG5640  113 VHE-FYSPGNLGNDIAVLELARAASLprvkitsfDASDTFLNsvttvSPMTNGTF--GVTTPSDVPRSSPKGTILHE--- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726 143 fVNVTVTPEDQCRPN--------------NVCTGVLTRRGgiCNGDGGTPLVCEG----LAHGVASFSLGPCGRG--PDF 202
Cdd:COG5640  187 -VAVLFVPLSTCAQYkgcanasdgatgltGFCAGRPPKDA--CQGDSGGPIFHKGeegrVQRGVVSWGDGGCGGTliPGV 263
                        250       260
                 ....*....|....*....|..
gi 157829726 203 FTRVALFRDWIDGVLNNPGPGP 224
Cdd:COG5640  264 YTNVSNYQDWIAAMTNGLSYLQ 285
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-214 1.93e-73

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  Cd Length: 232  Bit Score: 222.15  E-value: 1.93e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726   1 IVGGRKARPRQFPFLASIQ-NQGRHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRErQSRQTFSISSMSEN 79
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726  80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCR--- 155
Cdd:cd00190   80 pNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKray 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157829726 156 -------PNNVCTGVLTRRGGICNGDGGTPLVCE----GLAHGVASFSLGpCGRG--PDFFTRVALFRDWID 214
Cdd:cd00190  160 syggtitDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG-CARPnyPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-213 2.11e-69

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: 211.77  E-value: 2.11e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726     1 IVGGRKARPRQFPFLASIQNQG-RHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQsrQTFSISSMSEN 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG--QVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726    80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGS-QRSGGRLSRFPRFVNVTVTPEDQCR-- 155
Cdd:smart00020  80 pNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCRra 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157829726   156 --------PNNVCTGVLTRRGGICNGDGGTPLVCE---GLAHGVASFSLGpCGRG--PDFFTRVALFRDWI 213
Cdd:smart00020 160 ysgggaitDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSG-CARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin.
1-213 4.86e-54

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 172.62  E-value: 4.86e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726    1 IVGGRKARPRQFPFLASIQN-QGRHFCGGALIHARFVMTAASCFQsqNPGVSTVVLGAYDLRRRErQSRQTFSISS-MSE 78
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS--GASDVQVVLGEHNIVLRE-GGEQKFDVAKvIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726   79 NGYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRlSRFPRFVNVTVTPEDQCR--- 155
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDAGADLPVGTTCTVSGWGNTKTLGP-PDTLQEVTVPVVSRETCRsay 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157829726  156 -----PNNVCTGvlTRRGGICNGDGGTPLVCE-GLAHGVASFSLGpCGRG--PDFFTRVALFRDWI 213
Cdd:pfam00089 157 ggtvtDTMICAG--AGGKDACQGDSGGPLVCSdGELIGIVSWGYG-CASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-224 1.34e-24

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 99.95  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726   1 IVGGRKARPRQFPFLASIQNQGR-----HFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQTFSISS 75
Cdd:COG5640   33 IIGGSNANAGEYPSLVALVDRISdyvsgTFCGGSKLGGRYVLTAAHCADASSPISSDVNRVVVDLNDSSQAERGHVRTIY 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726  76 MSEnGYDPQQNLNDLMLLQLDREANL--------TSSVTILP-----LPLQNATVeaGTRCQVAGWGSQRSGGRLSRfpr 142
Cdd:COG5640  113 VHE-FYSPGNLGNDIAVLELARAASLprvkitsfDASDTFLNsvttvSPMTNGTF--GVTTPSDVPRSSPKGTILHE--- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157829726 143 fVNVTVTPEDQCRPN--------------NVCTGVLTRRGgiCNGDGGTPLVCEG----LAHGVASFSLGPCGRG--PDF 202
Cdd:COG5640  187 -VAVLFVPLSTCAQYkgcanasdgatgltGFCAGRPPKDA--CQGDSGGPIFHKGeegrVQRGVVSWGDGGCGGTliPGV 263
                        250       260
                 ....*....|....*....|..
gi 157829726 203 FTRVALFRDWIDGVLNNPGPGP 224
Cdd:COG5640  264 YTNVSNYQDWIAAMTNGLSYLQ 285
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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