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Conserved domains on  [gi|157829823|pdb|1AE5|A]
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Chain A, HEPARIN BINDING PROTEIN

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 2.12e-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 [Multi-domain]  Cd Length: 232  Bit Score: 222.15  E-value: 2.12e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A        1 IVGGRKARPRQFPFLASIQ-NQGRHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRErQSRQTFSISSMSEN 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A       80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCR--- 155
Cdd:cd00190  80 pNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKray 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1AE5_A      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 2.12e-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 [Multi-domain]  Cd Length: 232  Bit Score: 222.15  E-value: 2.12e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A        1 IVGGRKARPRQFPFLASIQ-NQGRHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRErQSRQTFSISSMSEN 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A       80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCR--- 155
Cdd:cd00190  80 pNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKray 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1AE5_A      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 2.32e-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: 2.32e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A           1 IVGGRKARPRQFPFLASIQNQG-RHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQsrQTFSISSMSEN 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG--QVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A          80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGS-QRSGGRLSRFPRFVNVTVTPEDQCR-- 155
Cdd:smart00020  80 pNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCRra 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1AE5_A         156 --------PNNVCTGVLTRRGGICNGDGGTPLVCE---GLAHGVASFSLGpCGRG--PDFFTRVALFRDWI 213
Cdd:smart00020 160 ysgggaitDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSG-CARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-213 1.04e-53

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 171.86  E-value: 1.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A          1 IVGGRKARPRQFPFLASIQN-QGRHFCGGALIHARFVMTAASCFQsqNPGVSTVVLGAYDLRRRErQSRQTFSISS-MSE 78
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS--GASDVKVVLGAHNIVLRE-GGEQKFDVEKiIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A         79 NGYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRlSRFPRFVNVTVTPEDQCR--- 155
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsay 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1AE5_A        156 -----PNNVCTGvlTRRGGICNGDGGTPLVCE-GLAHGVASFSLGpCGRG--PDFFTRVALFRDWI 213
Cdd:pfam00089 157 ggtvtDTMICAG--AGGKDACQGDSGGPLVCSdGELIGIVSWGYG-CASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-221 6.35e-46

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 153.27  E-value: 6.35e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A        1 IVGGRKARPRQFPFLASIQNQG---RHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQtfSISSMS 77
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK--VARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A       78 ENGYDPQQNLNDLMLLQLDREAnltSSVTILPLPLQNATVEAGTRCQVAGWGSQRSG-GRLSRFPRFVNVTVTPEDQCR- 155
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAa 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1AE5_A      156 ------PNNVCTGVLTRRGGICNGDGGTPLV----CEGLAHGVASFSLGPCGRG-PDFFTRVALFRDWIDGVLNNPG 221
Cdd:COG5640 186 yggfdgGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGyPGVYTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-214 2.12e-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 [Multi-domain]  Cd Length: 232  Bit Score: 222.15  E-value: 2.12e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A        1 IVGGRKARPRQFPFLASIQ-NQGRHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRErQSRQTFSISSMSEN 79
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQyTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNE-GGGQVIKVKKVIVH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A       80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTPEDQCR--- 155
Cdd:cd00190  80 pNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKray 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1AE5_A      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 2.32e-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: 2.32e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A           1 IVGGRKARPRQFPFLASIQNQG-RHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQsrQTFSISSMSEN 79
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEEG--QVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A          80 -GYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGS-QRSGGRLSRFPRFVNVTVTPEDQCR-- 155
Cdd:smart00020  80 pNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRtSEGAGSLPDTLQEVNVPIVSNATCRra 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1AE5_A         156 --------PNNVCTGVLTRRGGICNGDGGTPLVCE---GLAHGVASFSLGpCGRG--PDFFTRVALFRDWI 213
Cdd:smart00020 160 ysgggaitDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWGSG-CARPgkPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-213 1.04e-53

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 171.86  E-value: 1.04e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A          1 IVGGRKARPRQFPFLASIQN-QGRHFCGGALIHARFVMTAASCFQsqNPGVSTVVLGAYDLRRRErQSRQTFSISS-MSE 78
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVS--GASDVKVVLGAHNIVLRE-GGEQKFDVEKiIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A         79 NGYDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQRSGGRlSRFPRFVNVTVTPEDQCR--- 155
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRsay 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1AE5_A        156 -----PNNVCTGvlTRRGGICNGDGGTPLVCE-GLAHGVASFSLGpCGRG--PDFFTRVALFRDWI 213
Cdd:pfam00089 157 ggtvtDTMICAG--AGGKDACQGDSGGPLVCSdGELIGIVSWGYG-CASGnyPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-221 6.35e-46

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 153.27  E-value: 6.35e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A        1 IVGGRKARPRQFPFLASIQNQG---RHFCGGALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRRRERQSRQtfSISSMS 77
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK--VARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1AE5_A       78 ENGYDPQQNLNDLMLLQLDREAnltSSVTILPLPLQNATVEAGTRCQVAGWGSQRSG-GRLSRFPRFVNVTVTPEDQCR- 155
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGpGSQSGTLRKADVPVVSDATCAa 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1AE5_A      156 ------PNNVCTGVLTRRGGICNGDGGTPLV----CEGLAHGVASFSLGPCGRG-PDFFTRVALFRDWIDGVLNNPG 221
Cdd:COG5640 186 yggfdgGTMLCAGYPEGGKDACQGDSGGPLVvkdgGGWVLVGVVSWGGGPCAAGyPGVYTRVSAYRDWIKSTAGGLG 262
 
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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