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Conserved domains on  [gi|545829329|ref|XP_005664416|]
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haptoglobin isoform X1 [Sus scrofa]

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 ...
57-297 3.76e-60

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: 191.34  E-value: 3.76e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  57 IMGGSLDAKGSFPWQAKM-ISHHNLTSGATLINEQWLLTTAKNLRLGHKNDTKAKDIAPTLRLYVGKKQEVEIEKVIFHP 135
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 136 --DNSTV--DIGLIKLKQKVPVNERVMPICLPSKDY-VNVGLVGYVSGWGRNA-NLNFTEHLKYVMLPVADQEKCVQYYE 209
Cdd:cd00190   81 nyNPSTYdnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 210 GstvpekktpkspvgvQPILNEHTFCAGLSKYQEDTCYGDAGSAFAVHdkDDDTWYAAGILSFDKSCRTAEY-GVYVRVT 288
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 545829329 289 SILDWIQTT 297
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 ...
57-297 3.76e-60

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: 191.34  E-value: 3.76e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  57 IMGGSLDAKGSFPWQAKM-ISHHNLTSGATLINEQWLLTTAKNLRLGHKNDTKAKDIAPTLRLYVGKKQEVEIEKVIFHP 135
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 136 --DNSTV--DIGLIKLKQKVPVNERVMPICLPSKDY-VNVGLVGYVSGWGRNA-NLNFTEHLKYVMLPVADQEKCVQYYE 209
Cdd:cd00190   81 nyNPSTYdnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 210 GstvpekktpkspvgvQPILNEHTFCAGLSKYQEDTCYGDAGSAFAVHdkDDDTWYAAGILSFDKSCRTAEY-GVYVRVT 288
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 545829329 289 SILDWIQTT 297
Cdd:cd00190  224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
56-294 6.71e-57

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: 182.88  E-value: 6.71e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329    56 RIMGGSLDAKGSFPWQAKM-ISHHNLTSGATLINEQWLLTTAKNLRLGHKNDtkakdiaptLRLYVG--------KKQEV 126
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329   127 EIEKVIFHPD-NSTV---DIGLIKLKQKVPVNERVMPICLPSKDY-VNVGLVGYVSGWGR--NANLNFTEHLKYVMLPVA 199
Cdd:smart00020  72 KVSKVIIHPNyNPSTydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRtsEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329   200 DQEKCVQYYEGstvpekktpkspvgvQPILNEHTFCAGLSKYQEDTCYGDAGSAFAVHDKdddTWYAAGILSFDKSCRTA 279
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 545829329   280 EY-GVYVRVTSILDWI 294
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
57-294 4.98e-51

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 167.62  E-value: 4.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329   57 IMGGSLDAKGSFPWQAKM-ISHHNLTSGATLINEQWLLTTAKNLRLGHknDTKAKDIAPTLRLYVGKKQEVEIEKVIFHP 135
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  136 ----DNSTVDIGLIKLKQKVPVNERVMPICLPSK-DYVNVGLVGYVSGWGRNANLNFTEHLKYVMLPVADQEKCVQYYEG 210
Cdd:pfam00089  79 nynpDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  211 StvpekktpkspvgvqpiLNEHTFCAGLskYQEDTCYGDAGSAFAVHDKdddtwYAAGILSFDKSCRTAEY-GVYVRVTS 289
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 545829329  290 ILDWI 294
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
50-299 3.41e-34

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 125.15  E-value: 3.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  50 PVDQVQRIMGGSLDAKGSFPWQAKMISHHNLTS---GATLINEQWLLTTAknlrlgH-KNDTKAKDI---APTLRLYVGK 122
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfcGGTLIAPRWVLTAA------HcVDGDGPSDLrvvIGSTDLSTSG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 123 KQEVEIEKVIFHPD----NSTVDIGLIKLKQKVPvneRVMPICLP-SKDYVNVGLVGYVSGWGR--NANLNFTEHLKYVM 195
Cdd:COG5640   98 GTVVKVARIVVHPDydpaTPGNDIALLKLATPVP---GVAPAPLAtSADAAAPGTPATVAGWGRtsEGPGSQSGTLRKAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 196 LPVADQEKCVQYYEgstvpekktpkspvgvqpILNEHTFCAGLSKYQEDTCYGDAGSAFAVhdKDDDTWYAAGILSF-DK 274
Cdd:COG5640  175 VPVVSDATCAAYGG------------------FDGGTMLCAGYPEGGKDACQGDSGGPLVV--KDGGGWVLVGVVSWgGG 234
                        250       260
                 ....*....|....*....|....*
gi 545829329 275 SCRTAEYGVYVRVTSILDWIQTTIA 299
Cdd:COG5640  235 PCAAGYPGVYTRVSAYRDWIKSTAG 259
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
57-297 3.76e-60

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: 191.34  E-value: 3.76e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  57 IMGGSLDAKGSFPWQAKM-ISHHNLTSGATLINEQWLLTTAKNLRLGHKNDTKAKDIAPTLRLYVGKKQEVEIEKVIFHP 135
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 136 --DNSTV--DIGLIKLKQKVPVNERVMPICLPSKDY-VNVGLVGYVSGWGRNA-NLNFTEHLKYVMLPVADQEKCVQYYE 209
Cdd:cd00190   81 nyNPSTYdnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRAYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 210 GstvpekktpkspvgvQPILNEHTFCAGLSKYQEDTCYGDAGSAFAVHdkDDDTWYAAGILSFDKSCRTAEY-GVYVRVT 288
Cdd:cd00190  161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCN--DNGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                 ....*....
gi 545829329 289 SILDWIQTT 297
Cdd:cd00190  224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
56-294 6.71e-57

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: 182.88  E-value: 6.71e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329    56 RIMGGSLDAKGSFPWQAKM-ISHHNLTSGATLINEQWLLTTAKNLRLGHKNDtkakdiaptLRLYVG--------KKQEV 126
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSDPSN---------IRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329   127 EIEKVIFHPD-NSTV---DIGLIKLKQKVPVNERVMPICLPSKDY-VNVGLVGYVSGWGR--NANLNFTEHLKYVMLPVA 199
Cdd:smart00020  72 KVSKVIIHPNyNPSTydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGRtsEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329   200 DQEKCVQYYEGstvpekktpkspvgvQPILNEHTFCAGLSKYQEDTCYGDAGSAFAVHDKdddTWYAAGILSFDKSCRTA 279
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDG---RWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 545829329   280 EY-GVYVRVTSILDWI 294
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
57-294 4.98e-51

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 167.62  E-value: 4.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329   57 IMGGSLDAKGSFPWQAKM-ISHHNLTSGATLINEQWLLTTAKNLRLGHknDTKAKDIAPTLRLYVGKKQEVEIEKVIFHP 135
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLTAAHCVSGAS--DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  136 ----DNSTVDIGLIKLKQKVPVNERVMPICLPSK-DYVNVGLVGYVSGWGRNANLNFTEHLKYVMLPVADQEKCVQYYEG 210
Cdd:pfam00089  79 nynpDTLDNDIALLKLESPVTLGDTVRPICLPDAsSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  211 StvpekktpkspvgvqpiLNEHTFCAGLskYQEDTCYGDAGSAFAVHDKdddtwYAAGILSFDKSCRTAEY-GVYVRVTS 289
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 545829329  290 ILDWI 294
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
50-299 3.41e-34

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 125.15  E-value: 3.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329  50 PVDQVQRIMGGSLDAKGSFPWQAKMISHHNLTS---GATLINEQWLLTTAknlrlgH-KNDTKAKDI---APTLRLYVGK 122
Cdd:COG5640   24 AADAAPAIVGGTPATVGEYPWMVALQSSNGPSGqfcGGTLIAPRWVLTAA------HcVDGDGPSDLrvvIGSTDLSTSG 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 123 KQEVEIEKVIFHPD----NSTVDIGLIKLKQKVPvneRVMPICLP-SKDYVNVGLVGYVSGWGR--NANLNFTEHLKYVM 195
Cdd:COG5640   98 GTVVKVARIVVHPDydpaTPGNDIALLKLATPVP---GVAPAPLAtSADAAAPGTPATVAGWGRtsEGPGSQSGTLRKAD 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545829329 196 LPVADQEKCVQYYEgstvpekktpkspvgvqpILNEHTFCAGLSKYQEDTCYGDAGSAFAVhdKDDDTWYAAGILSF-DK 274
Cdd:COG5640  175 VPVVSDATCAAYGG------------------FDGGTMLCAGYPEGGKDACQGDSGGPLVV--KDGGGWVLVGVVSWgGG 234
                        250       260
                 ....*....|....*....|....*
gi 545829329 275 SCRTAEYGVYVRVTSILDWIQTTIA 299
Cdd:COG5640  235 PCAAGYPGVYTRVSAYRDWIKSTAG 259
 
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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