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Conserved domains on  [gi|1858900755|ref|NP_001371289|]
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haptoglobin-related protein isoform 2 [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 ...
10-224 2.25e-51

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: 166.30  E-value: 2.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755  10 GATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVM 85
Cdd:cd00190    28 GGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPStydnDIALLKLKRPVTLSDNVR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755  86 PICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCV 163
Cdd:cd00190   108 PICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYSY---------------GGTITDNMLCA 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1858900755 164 GMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVTSIQHWVQKT 224
Cdd:cd00190   173 GGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
10-224 2.25e-51

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: 166.30  E-value: 2.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755  10 GATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVM 85
Cdd:cd00190    28 GGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPStydnDIALLKLKRPVTLSDNVR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755  86 PICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCV 163
Cdd:cd00190   108 PICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYSY---------------GGTITDNMLCA 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1858900755 164 GMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVTSIQHWVQKT 224
Cdd:cd00190   173 GGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
10-221 1.16e-45

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: 151.68  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755   10 GATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLVEIEKVVLHPNYHQV----DIGLIKLKQK 77
Cdd:smart00020  29 GGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVIKVSKVIIHPNYNPStydnDIALLKLKEP 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755   78 VLVNERVMPICLPSKNY-AEVGRVGYVSGWG--QSDNFKLTDHLKYVMLPVADQYDCITHYEGstcpkwkapkspvgvQP 154
Cdd:smart00020 100 VTLSDNVRPICLPSSNYnVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIVSNATCRRAYSG---------------GG 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900755  155 ILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleeDTWYAAGILSFDKSCAVAEY-GVYVKVTSIQHWV 221
Cdd:smart00020 165 AITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
2-221 2.16e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 142.97  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755   2 VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHPNY----HQVDIGLIKLKQK 77
Cdd:pfam00089  20 LSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYnpdtLDNDIALLKLESP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755  78 VLVNERVMPICLPSKN-YAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEGStcpkwkapkspvgvqpiL 156
Cdd:pfam00089  98 VTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGT-----------------V 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858900755 157 NEHTFCVGMskYQEDTCYGDAGSAFAVHDLeedtwYAAGILSFDKSCAVAEY-GVYVKVTSIQHWV 221
Cdd:pfam00089 161 TDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSSYLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
10-224 2.25e-51

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: 166.30  E-value: 2.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755  10 GATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVM 85
Cdd:cd00190    28 GGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHPNYNPStydnDIALLKLKRPVTLSDNVR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755  86 PICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCV 163
Cdd:cd00190   108 PICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYSY---------------GGTITDNMLCA 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1858900755 164 GMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVTSIQHWVQKT 224
Cdd:cd00190   173 GGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
10-221 1.16e-45

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: 151.68  E-value: 1.16e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755   10 GATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLVEIEKVVLHPNYHQV----DIGLIKLKQK 77
Cdd:smart00020  29 GGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVIKVSKVIIHPNYNPStydnDIALLKLKEP 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755   78 VLVNERVMPICLPSKNY-AEVGRVGYVSGWG--QSDNFKLTDHLKYVMLPVADQYDCITHYEGstcpkwkapkspvgvQP 154
Cdd:smart00020 100 VTLSDNVRPICLPSSNYnVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIVSNATCRRAYSG---------------GG 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1858900755  155 ILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleeDTWYAAGILSFDKSCAVAEY-GVYVKVTSIQHWV 221
Cdd:smart00020 165 AITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARPGKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
2-221 2.16e-42

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 142.97  E-value: 2.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755   2 VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHPNY----HQVDIGLIKLKQK 77
Cdd:pfam00089  20 LSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHPNYnpdtLDNDIALLKLESP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1858900755  78 VLVNERVMPICLPSKN-YAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEGStcpkwkapkspvgvqpiL 156
Cdd:pfam00089  98 VTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGGT-----------------V 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1858900755 157 NEHTFCVGMskYQEDTCYGDAGSAFAVHDLeedtwYAAGILSFDKSCAVAEY-GVYVKVTSIQHWV 221
Cdd:pfam00089 161 TDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSSYLDWI 219
 
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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