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Conserved domains on  [gi|292158|gb|AAA88079|]
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haptoglobin-like protein [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 10076129)

serine protease such as human cathepsin G with trypsin- and chymotrypsin-like specificity; also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity

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 3.47e-59

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: 190.57  E-value: 3.47e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   183 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 256
Cdd:cd00190  81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   257 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 335
Cdd:cd00190 161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                ....*....
gi 292158   336 SIQDWVQKT 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 3.47e-59

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: 190.57  E-value: 3.47e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   183 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 256
Cdd:cd00190  81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   257 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 335
Cdd:cd00190 161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                ....*....
gi 292158   336 SIQDWVQKT 344
Cdd:cd00190 224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
103-341 1.11e-54

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: 178.64  E-value: 1.11e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158      103 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 173
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158      174 EIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG--QSDNFKLTDHLKYVMLPVA 246
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158      247 DQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleeDTWYAAGILSFDKSCAVA 326
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 292158      327 EY-GVYVKVTSIQDWV 341
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
104-341 6.00e-49

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 163.77  E-value: 6.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158     104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158     183 NY----HQVDIGLIKLKQKVLVNERVMPICLPSKN-YAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEG 257
Cdd:pfam00089  79 NYnpdtLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158     258 StcpkwkapkspvgvqpiLNEHTFCVGMskYQEDTCYGDAGSAFAVHDLeedtwYAAGILSFDKSCAVAEY-GVYVKVTS 336
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 292158     337 IQDWV 341
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
97-348 1.02e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 114.36  E-value: 1.02e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158    97 PANPVQRILGGHLDAKGSFPWQAKMVS---HHNLTTGATLINEQWLLTTAknlflnHsenATAKDIAPTLTLYVG----- 168
Cdd:COG5640  24 AADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAA------H---CVDGDGPSDLRVVIGstdls 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   169 --KKQLVEIEKVVLHPNYHQV----DIGLIKLKQKVlvnERVMPICLP-SKNYAEVGRVGYVSGWGQSDNF--KLTDHLK 239
Cdd:COG5640  95 tsGGTVVKVARIVVHPDYDPAtpgnDIALLKLATPV---PGVAPAPLAtSADAAAPGTPATVAGWGRTSEGpgSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   240 YVMLPVADQYDCiTHYEGstcpkwkapkspvgvqpILNEHTFCVGMSKYQEDTCYGDAGS-AFAVHDleeDTWYAAGILS 318
Cdd:COG5640 172 KADVPVVSDATC-AAYGG-----------------FDGGTMLCAGYPEGGKDACQGDSGGpLVVKDG---GGWVLVGVVS 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 292158   319 F-DKSCAVAEYGVYVKVTSIQDWVQKTIAEN 348
Cdd:COG5640 231 WgGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
104-344 3.47e-59

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: 190.57  E-value: 3.47e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLqYTGGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   183 NYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG-QSDNFKLTDHLKYVMLPVADQYDCITHYE 256
Cdd:cd00190  81 NYNPStydnDIALLKLKRPVTLSDNVRPICLPSSGYnLPAGTTCTVSGWGrTSEGGPLPDVLQEVNVPIVSNAECKRAYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   257 GstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleEDTWYAAGILSFDKSCAVAEY-GVYVKVT 335
Cdd:cd00190 161 Y---------------GGTITDNMLCAGGLEGGKDACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYpGVYTRVS 223

                ....*....
gi 292158   336 SIQDWVQKT 344
Cdd:cd00190 224 SYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
103-341 1.11e-54

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: 178.64  E-value: 1.11e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158      103 RILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTTAKNLFLNHsenatakdiAPTLTLYVG--------KKQLV 173
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLqYGGGRHFCGGSLISPRWVLTAAHCVRGSD---------PSNIRVRLGshdlssgeEGQVI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158      174 EIEKVVLHPNYHQV----DIGLIKLKQKVLVNERVMPICLPSKNY-AEVGRVGYVSGWG--QSDNFKLTDHLKYVMLPVA 246
Cdd:smart00020  72 KVSKVIIHPNYNPStydnDIALLKLKEPVTLSDNVRPICLPSSNYnVPAGTTCTVSGWGrtSEGAGSLPDTLQEVNVPIV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158      247 DQYDCITHYEGstcpkwkapkspvgvQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDleeDTWYAAGILSFDKSCAVA 326
Cdd:smart00020 152 SNATCRRAYSG---------------GGAITDNMLCAGGLEGGKDACQGDSGGPLVCND---GRWVLVGIVSWGSGCARP 213
                          250
                   ....*....|....*.
gi 292158      327 EY-GVYVKVTSIQDWV 341
Cdd:smart00020 214 GKpGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
104-341 6.00e-49

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 163.77  E-value: 6.00e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158     104 ILGGHLDAKGSFPWQAKM-VSHHNLTTGATLINEQWLLTtAKNLFLNHSeNATAKDIAPTLTLYVGKKQLVEIEKVVLHP 182
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLqLSSGKHFCGGSLISENWVLT-AAHCVSGAS-DVKVVLGAHNIVLREGGEQKFDVEKIIVHP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158     183 NY----HQVDIGLIKLKQKVLVNERVMPICLPSKN-YAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEG 257
Cdd:pfam00089  79 NYnpdtLDNDIALLKLESPVTLGDTVRPICLPDASsDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAYGG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158     258 StcpkwkapkspvgvqpiLNEHTFCVGMskYQEDTCYGDAGSAFAVHDLeedtwYAAGILSFDKSCAVAEY-GVYVKVTS 336
Cdd:pfam00089 159 T-----------------VTDTMICAGA--GGKDACQGDSGGPLVCSDG-----ELIGIVSWGYGCASGNYpGVYTPVSS 214

                  ....*
gi 292158     337 IQDWV 341
Cdd:pfam00089 215 YLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
97-348 1.02e-29

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 114.36  E-value: 1.02e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158    97 PANPVQRILGGHLDAKGSFPWQAKMVS---HHNLTTGATLINEQWLLTTAknlflnHsenATAKDIAPTLTLYVG----- 168
Cdd:COG5640  24 AADAAPAIVGGTPATVGEYPWMVALQSsngPSGQFCGGTLIAPRWVLTAA------H---CVDGDGPSDLRVVIGstdls 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   169 --KKQLVEIEKVVLHPNYHQV----DIGLIKLKQKVlvnERVMPICLP-SKNYAEVGRVGYVSGWGQSDNF--KLTDHLK 239
Cdd:COG5640  95 tsGGTVVKVARIVVHPDYDPAtpgnDIALLKLATPV---PGVAPAPLAtSADAAAPGTPATVAGWGRTSEGpgSQSGTLR 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 292158   240 YVMLPVADQYDCiTHYEGstcpkwkapkspvgvqpILNEHTFCVGMSKYQEDTCYGDAGS-AFAVHDleeDTWYAAGILS 318
Cdd:COG5640 172 KADVPVVSDATC-AAYGG-----------------FDGGTMLCAGYPEGGKDACQGDSGGpLVVKDG---GGWVLVGVVS 230
                       250       260       270
                ....*....|....*....|....*....|.
gi 292158   319 F-DKSCAVAEYGVYVKVTSIQDWVQKTIAEN 348
Cdd:COG5640 231 WgGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
 
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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