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Conserved domains on  [gi|1370468378|ref|XP_024306019|]
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haptoglobin-related protein isoform X1 [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 ...
110-350 7.33e-58

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: 187.48  E-value: 7.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 110 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 188
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 189 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 262
Cdd:cd00190    81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 263 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 341
Cdd:cd00190   161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                  ....*....
gi 1370468378 342 SIQHWVQKT 350
Cdd:cd00190   224 SYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
110-350 7.33e-58

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: 187.48  E-value: 7.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 110 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 188
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 189 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 262
Cdd:cd00190    81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 263 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 341
Cdd:cd00190   161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                  ....*....
gi 1370468378 342 SIQHWVQKT 350
Cdd:cd00190   224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
109-347 2.74e-53

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: 175.56  E-value: 2.74e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378  109 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 179
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378  180 EIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG--QSDNFKLTDHLKYVMLPVA 252
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378  253 DQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleeDTWYAAGILSFDKSCAVA 332
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 1370468378  333 EY-GVYVKVTSIQHWV 347
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
110-347 3.18e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 161.84  E-value: 3.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 110 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 188
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 189 NY----HQVDIGLIKLKQKVLVNERVMPICLPSKN-YAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEG 263
Cdd:pfam00089  79 NYnpdtLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 264 StcpkwkapkspvgvqpiLNEHTFCVGMskYQEDTCYGDAGSAFAVHDLeedtwYAAGILSFDKSCAVAEY-GVYVKVTS 342
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 1370468378 343 IQHWV 347
Cdd:pfam00089 215 YLDWI 219
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
110-350 7.33e-58

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: 187.48  E-value: 7.33e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 110 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 188
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 189 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 262
Cdd:cd00190    81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 263 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 341
Cdd:cd00190   161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                  ....*....
gi 1370468378 342 SIQHWVQKT 350
Cdd:cd00190   224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
109-347 2.74e-53

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: 175.56  E-value: 2.74e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378  109 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 179
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378  180 EIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG--QSDNFKLTDHLKYVMLPVA 252
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378  253 DQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleeDTWYAAGILSFDKSCAVA 332
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 1370468378  333 EY-GVYVKVTSIQHWV 347
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
110-347 3.18e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 161.84  E-value: 3.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 110 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 188
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 189 NY----HQVDIGLIKLKQKVLVNERVMPICLPSKN-YAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEG 263
Cdd:pfam00089  79 NYnpdtLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370468378 264 StcpkwkapkspvgvqpiLNEHTFCVGMskYQEDTCYGDAGSAFAVHDLeedtwYAAGILSFDKSCAVAEY-GVYVKVTS 342
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 1370468378 343 IQHWV 347
Cdd:pfam00089 215 YLDWI 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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