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Conserved domains on  [gi|262527547|sp|P00739|]
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RecName: Full=Haptoglobin-related 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

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 ...
104-344 1.01e-57

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: 186.71  E-value: 1.01e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 183 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 256
Cdd:cd00190   81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 257 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 335
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 262527547 336 SIQHWVQKT 344
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 ...
104-344 1.01e-57

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: 186.71  E-value: 1.01e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 183 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 256
Cdd:cd00190   81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 257 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 335
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 262527547 336 SIQHWVQKT 344
Cdd:cd00190  224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
103-341 3.52e-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: 174.79  E-value: 3.52e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547   103 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 173
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547   174 EIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG--QSDNFKLTDHLKYVMLPVA 246
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547   247 DQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleeDTWYAAGILSFDKSCAVA 326
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 262527547   327 EY-GVYVKVTSIQHWV 341
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
104-341 4.35e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 161.46  E-value: 4.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547  104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547  183 NY----HQVDIGLIKLKQKVLVNERVMPICLPSKN-YAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEG 257
Cdd:pfam00089  79 NYnpdtLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547  258 StcpkwkapkspvgvqpiLNEHTFCVGMskYQEDTCYGDAGSAFAVHDLeedtwYAAGILSFDKSCAVAEY-GVYVKVTS 336
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 262527547  337 IQHWV 341
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 ...
104-344 1.01e-57

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: 186.71  E-value: 1.01e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 183 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 256
Cdd:cd00190   81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547 257 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 335
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 262527547 336 SIQHWVQKT 344
Cdd:cd00190  224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
103-341 3.52e-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: 174.79  E-value: 3.52e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547   103 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 173
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547   174 EIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG--QSDNFKLTDHLKYVMLPVA 246
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547   247 DQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleeDTWYAAGILSFDKSCAVA 326
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 262527547   327 EY-GVYVKVTSIQHWV 341
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
104-341 4.35e-48

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 161.46  E-value: 4.35e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547  104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547  183 NY----HQVDIGLIKLKQKVLVNERVMPICLPSKN-YAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEG 257
Cdd:pfam00089  79 NYnpdtLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 262527547  258 StcpkwkapkspvgvqpiLNEHTFCVGMskYQEDTCYGDAGSAFAVHDLeedtwYAAGILSFDKSCAVAEY-GVYVKVTS 336
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 262527547  337 IQHWV 341
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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