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Conserved domains on  [gi|306845|gb|AAA52647|]
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Hanukah factor serine protease precursor [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 ...
29-254 1.56e-87

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: 259.52  E-value: 1.56e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845    29 IIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845   105 CYDPATREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDrnH 184
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 306845   185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYILLSkKHLNWI 254
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG--CARPNYPGVYTRVS-SYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
29-254 1.56e-87

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: 259.52  E-value: 1.56e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845    29 IIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845   105 CYDPATREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDrnH 184
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 306845   185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYILLSkKHLNWI 254
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG--CARPNYPGVYTRVS-SYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-254 2.40e-82

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: 246.44  E-value: 2.40e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845       28 KIIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPtKQIMLVKKEFPY 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845      104 PCYDPATREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSA-SWSDTLREVNITIIDRKVCndR 182
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATC--R 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306845      183 NHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE---GVFRGVTSFGleNKCGDPRGPGVYILLSkKHLNWI 254
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG--SGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
29-254 1.78e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 208.45  E-value: 1.78e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845      29 IIGGNEVTPHSRPYMVLLSL-DRKTICAGALIAKDWVLTAAHCNLNKRS-QVILGAHSITREEPTKQIMLVKKEFPYPCY 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845     107 DPATREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASwSDTLREVNITIIDRKVCNDRnhyn 186
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA---- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 306845     187 FNPVIGMNMVCAGSlrGGRDSCNGDSGSPLLCEGVF-RGVTSFGleNKCGDPRGPGVYILLSkKHLNWI 254
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGElIGIVSWG--YGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
22-254 2.56e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 175.99  E-value: 2.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845    22 PEDVCEKIIGGNEVTPHSRPYMVLLSLD---RKTICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPTKqiM 95
Cdd:COG5640  24 AADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCvdgDGPSDLRVVIGSTDLSTSGGTV--V 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845    96 LVKKEFPYPCYDPATREGDLKLLQLTEKAKINKYVTilhLPKKGDDVKPGTMCQVAGWGRT-HNSASWSDTLREVNITII 174
Cdd:COG5640 102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVV 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845   175 DRKVCNDRNHYNFNpvigmNMVCAGSLRGGRDSCNGDSGSPLL--CEGVFR--GVTSFGlENKCGdPRGPGVYILLSkKH 250
Cdd:COG5640 179 SDATCAAYGGFDGG-----TMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWG-GGPCA-AGYPGVYTRVS-AY 250

                ....
gi 306845   251 LNWI 254
Cdd:COG5640 251 RDWI 254
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
29-254 1.56e-87

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: 259.52  E-value: 1.56e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845    29 IIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHCNLN---KRSQVILGAHSITREEPTKQIMLVKKEFPYP 104
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRhFCGGSLISPRWVLTAAHCVYSsapSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845   105 CYDPATREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASWSDTLREVNITIIDRKVCNDrnH 184
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKR--A 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 306845   185 YNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE----GVFRGVTSFGLEnkCGDPRGPGVYILLSkKHLNWI 254
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNdngrGVLVGIVSWGSG--CARPNYPGVYTRVS-SYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
28-254 2.40e-82

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: 246.44  E-value: 2.40e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845       28 KIIGGNEVTPHSRPYMVLLSLDRKT-ICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPtKQIMLVKKEFPY 103
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRhFCGGSLISPRWVLTAAHCvrgSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVIIH 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845      104 PCYDPATREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSA-SWSDTLREVNITIIDRKVCndR 182
Cdd:smart00020  80 PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAgSLPDTLQEVNVPIVSNATC--R 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306845      183 NHYNFNPVIGMNMVCAGSLRGGRDSCNGDSGSPLLCE---GVFRGVTSFGleNKCGDPRGPGVYILLSkKHLNWI 254
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNdgrWVLVGIVSWG--SGCARPGKPGVYTRVS-SYLDWI 229
Trypsin pfam00089
Trypsin;
29-254 1.78e-67

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 208.45  E-value: 1.78e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845      29 IIGGNEVTPHSRPYMVLLSL-DRKTICAGALIAKDWVLTAAHCNLNKRS-QVILGAHSITREEPTKQIMLVKKEFPYPCY 106
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLsSGKHFCGGSLISENWVLTAAHCVSGASDvKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845     107 DPATREGDLKLLQLTEKAKINKYVTILHLPKKGDDVKPGTMCQVAGWGRTHNSASwSDTLREVNITIIDRKVCNDRnhyn 186
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSA---- 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 306845     187 FNPVIGMNMVCAGSlrGGRDSCNGDSGSPLLCEGVF-RGVTSFGleNKCGDPRGPGVYILLSkKHLNWI 254
Cdd:pfam00089 156 YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDGElIGIVSWG--YGCASGNYPGVYTPVS-SYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
22-254 2.56e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 175.99  E-value: 2.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845    22 PEDVCEKIIGGNEVTPHSRPYMVLLSLD---RKTICAGALIAKDWVLTAAHC---NLNKRSQVILGAHSITREEPTKqiM 95
Cdd:COG5640  24 AADAAPAIVGGTPATVGEYPWMVALQSSngpSGQFCGGTLIAPRWVLTAAHCvdgDGPSDLRVVIGSTDLSTSGGTV--V 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845    96 LVKKEFPYPCYDPATREGDLKLLQLTEKAKINKYVTilhLPKKGDDVKPGTMCQVAGWGRT-HNSASWSDTLREVNITII 174
Cdd:COG5640 102 KVARIVVHPDYDPATPGNDIALLKLATPVPGVAPAP---LATSADAAAPGTPATVAGWGRTsEGPGSQSGTLRKADVPVV 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306845   175 DRKVCNDRNHYNFNpvigmNMVCAGSLRGGRDSCNGDSGSPLL--CEGVFR--GVTSFGlENKCGdPRGPGVYILLSkKH 250
Cdd:COG5640 179 SDATCAAYGGFDGG-----TMLCAGYPEGGKDACQGDSGGPLVvkDGGGWVlvGVVSWG-GGPCA-AGYPGVYTRVS-AY 250

                ....
gi 306845   251 LNWI 254
Cdd:COG5640 251 RDWI 254
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
45-70 7.51e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 39.66  E-value: 7.51e-04
                        10        20
                ....*....|....*....|....*.
gi 306845    45 LLSLDRKTICAGALIAKDWVLTAAHC 70
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHC 30
 
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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