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Conserved domains on  [gi|51010989|ref|NP_001003450|]
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chymotrypsin-like elastase family member 1.5 precursor [Danio rerio]

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 ...
30-264 3.84e-84

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: 251.43  E-value: 3.84e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989  30 VVGGEIAKPHSWPWQVSVQIKtlsqdSYTHYCAGTLIRKNYVLTSVHSIFSKY-GSWRVVLGDHDISTDEGTEQYIEVRE 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYT-----GGRHFCGGSLISPRWVLTAAHCVYSSApSNYTVRLGSHDLSSNEGGGQVIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989 109 ITFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQILPHGTPCFTTGWGNTETDGSFSAELKQAYLPVVDHE 188
Cdd:cd00190  76 VIVH--PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51010989 189 TCSQSDWWGSTVKDTMVCGG--DGTMAVCKGDFGGPLSCLVDGKYVVYGIASFmsSEGCNIYKKPTIFTRVSAYVDWI 264
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGglEGGKDACQGDSGGPLVCNDNGRGVLVGIVSW--GSGCARPNYPGVYTRVSSYLDWI 229
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-264 3.84e-84

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: 251.43  E-value: 3.84e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989  30 VVGGEIAKPHSWPWQVSVQIKtlsqdSYTHYCAGTLIRKNYVLTSVHSIFSKY-GSWRVVLGDHDISTDEGTEQYIEVRE 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYT-----GGRHFCGGSLISPRWVLTAAHCVYSSApSNYTVRLGSHDLSSNEGGGQVIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989 109 ITFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQILPHGTPCFTTGWGNTETDGSFSAELKQAYLPVVDHE 188
Cdd:cd00190  76 VIVH--PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51010989 189 TCSQSDWWGSTVKDTMVCGG--DGTMAVCKGDFGGPLSCLVDGKYVVYGIASFmsSEGCNIYKKPTIFTRVSAYVDWI 264
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGglEGGKDACQGDSGGPLVCNDNGRGVLVGIVSW--GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-264 1.51e-78

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: 237.19  E-value: 1.51e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989     29 RVVGGEIAKPHSWPWQVSVQIKtlsqdSYTHYCAGTLIRKNYVLTSVHSIFSKY-GSWRVVLGDHDISTDEGtEQYIEVR 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG-----GGRHFCGGSLISPRWVLTAAHCVRGSDpSNIRVRLGSHDLSSGEE-GQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989    108 EITFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQILPHGTPCFTTGWGNT-ETDGSFSAELKQAYLPVVD 186
Cdd:smart00020  75 KVIIH--PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989    187 HETCSQSDWWGSTVKDTMVCGG--DGTMAVCKGDFGGPLSCLvDGKYVVYGIASFmsSEGCNIYKKPTIFTRVSAYVDWI 264
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGglEGGKDACQGDSGGPLVCN-DGRWVLVGIVSW--GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-264 9.19e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 214.61  E-value: 9.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989    30 VVGGEIAKPHSWPWQVSVQIKTLSqdsytHYCAGTLIRKNYVLTSVHsIFSKYGSWRVVLGDHDISTDEGTEQYIEVREI 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-----HFCGGSLISENWVLTAAH-CVSGASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989   110 TFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQILPHGTPCFTTGWGNTETDGSfSAELKQAYLPVVDHET 189
Cdd:pfam00089  75 IVH--PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51010989   190 CSQSdwWGSTVKDTMVCGGDGTMAVCKGDFGGPLSCLvdGKYVVyGIASFmsSEGCNIYKKPTIFTRVSAYVDWI 264
Cdd:pfam00089 152 CRSA--YGGTVTDTMICAGAGGKDACQGDSGGPLVCS--DGELI-GIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-265 4.68e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 186.01  E-value: 4.68e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989   1 MQRILLLSVLAAFALAEPRYVKDLA-AEERVVGGEIAKPHSWPWQVSVQIktlSQDSYTHYCAGTLIRKNYVLTSVHSIF 79
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAAdAAPAIVGGTPATVGEYPWMVALQS---SNGPSGQFCGGTLIAPRWVLTAAHCVD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989  80 -SKYGSWRVVLGDHDISTDEGTEqyIEVREITFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQIlphGTP 158
Cdd:COG5640  78 gDGPSDLRVVIGSTDLSTSGGTV--VKVARIVVH--PDYDPATPGNDIALLKLATPVPGVAPAPLATSADAAAP---GTP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989 159 CFTTGWGNT-ETDGSFSAELKQAYLPVVDHETCSQsdwWGSTVKDTMVCGG--DGTMAVCKGDFGGPLSCLVDGKYVVYG 235
Cdd:COG5640 151 ATVAGWGRTsEGPGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGypEGGKDACQGDSGGPLVVKDGGGWVLVG 227
                       250       260       270
                ....*....|....*....|....*....|
gi 51010989 236 IASFmsSEGCNIYKKPTIFTRVSAYVDWIT 265
Cdd:COG5640 228 VVSW--GGGPCAAGYPGVYTRVSAYRDWIK 255
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
30-264 3.84e-84

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: 251.43  E-value: 3.84e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989  30 VVGGEIAKPHSWPWQVSVQIKtlsqdSYTHYCAGTLIRKNYVLTSVHSIFSKY-GSWRVVLGDHDISTDEGTEQYIEVRE 108
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYT-----GGRHFCGGSLISPRWVLTAAHCVYSSApSNYTVRLGSHDLSSNEGGGQVIKVKK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989 109 ITFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQILPHGTPCFTTGWGNTETDGSFSAELKQAYLPVVDHE 188
Cdd:cd00190  76 VIVH--PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 51010989 189 TCSQSDWWGSTVKDTMVCGG--DGTMAVCKGDFGGPLSCLVDGKYVVYGIASFmsSEGCNIYKKPTIFTRVSAYVDWI 264
Cdd:cd00190 154 ECKRAYSYGGTITDNMLCAGglEGGKDACQGDSGGPLVCNDNGRGVLVGIVSW--GSGCARPNYPGVYTRVSSYLDWI 229
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
29-264 1.51e-78

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: 237.19  E-value: 1.51e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989     29 RVVGGEIAKPHSWPWQVSVQIKtlsqdSYTHYCAGTLIRKNYVLTSVHSIFSKY-GSWRVVLGDHDISTDEGtEQYIEVR 107
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG-----GGRHFCGGSLISPRWVLTAAHCVRGSDpSNIRVRLGSHDLSSGEE-GQVIKVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989    108 EITFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQILPHGTPCFTTGWGNT-ETDGSFSAELKQAYLPVVD 186
Cdd:smart00020  75 KVIIH--PNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsEGAGSLPDTLQEVNVPIVS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989    187 HETCSQSDWWGSTVKDTMVCGG--DGTMAVCKGDFGGPLSCLvDGKYVVYGIASFmsSEGCNIYKKPTIFTRVSAYVDWI 264
Cdd:smart00020 153 NATCRRAYSGGGAITDNMLCAGglEGGKDACQGDSGGPLVCN-DGRWVLVGIVSW--GSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
30-264 9.19e-70

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 214.61  E-value: 9.19e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989    30 VVGGEIAKPHSWPWQVSVQIKTLSqdsytHYCAGTLIRKNYVLTSVHsIFSKYGSWRVVLGDHDISTDEGTEQYIEVREI 109
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-----HFCGGSLISENWVLTAAH-CVSGASDVKVVLGAHNIVLREGGEQKFDVEKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989   110 TFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQILPHGTPCFTTGWGNTETDGSfSAELKQAYLPVVDHET 189
Cdd:pfam00089  75 IVH--PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRET 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51010989   190 CSQSdwWGSTVKDTMVCGGDGTMAVCKGDFGGPLSCLvdGKYVVyGIASFmsSEGCNIYKKPTIFTRVSAYVDWI 264
Cdd:pfam00089 152 CRSA--YGGTVTDTMICAGAGGKDACQGDSGGPLVCS--DGELI-GIVSW--GYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-265 4.68e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 186.01  E-value: 4.68e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989   1 MQRILLLSVLAAFALAEPRYVKDLA-AEERVVGGEIAKPHSWPWQVSVQIktlSQDSYTHYCAGTLIRKNYVLTSVHSIF 79
Cdd:COG5640   1 MRRRRLLAALAAAALALALAAAPAAdAAPAIVGGTPATVGEYPWMVALQS---SNGPSGQFCGGTLIAPRWVLTAAHCVD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989  80 -SKYGSWRVVLGDHDISTDEGTEqyIEVREITFHaySDLNDVSKGNDVALLKLASDANLNAYVQLAPLPRHKQIlphGTP 158
Cdd:COG5640  78 gDGPSDLRVVIGSTDLSTSGGTV--VKVARIVVH--PDYDPATPGNDIALLKLATPVPGVAPAPLATSADAAAP---GTP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989 159 CFTTGWGNT-ETDGSFSAELKQAYLPVVDHETCSQsdwWGSTVKDTMVCGG--DGTMAVCKGDFGGPLSCLVDGKYVVYG 235
Cdd:COG5640 151 ATVAGWGRTsEGPGSQSGTLRKADVPVVSDATCAA---YGGFDGGTMLCAGypEGGKDACQGDSGGPLVVKDGGGWVLVG 227
                       250       260       270
                ....*....|....*....|....*....|
gi 51010989 236 IASFmsSEGCNIYKKPTIFTRVSAYVDWIT 265
Cdd:COG5640 228 VVSW--GGGPCAAGYPGVYTRVSAYRDWIK 255
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
52-246 2.89e-03

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 37.73  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989  52 LSQDSYTHYCAGTLIRKNYVLTSVHSIFSK-----YGSWRVVLGDHDistdeGTEQYIEVREITFHAYSDlNDVSKGNDV 126
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDGagggwATNIVFVPGYNG-----GPYGTATATRFRVPPGWV-ASGDAGYDY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51010989 127 ALLKLasDANLNAYVQLAPLPRHKQILPhGTPCFTTGWGNtetDGSFSAELkqaylpvvdHETCSQSDWWGSTVkdTMVC 206
Cdd:COG3591  79 ALLRL--DEPLGDTTGWLGLAFNDAPLA-GEPVTIIGYPG---DRPKDLSL---------DCSGRVTGVQGNRL--SYDC 141
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 51010989 207 ggdgtmAVCKGDFGGPLSCLVDGKYVVYGIASFMSSEGCN 246
Cdd:COG3591 142 ------DTTGGSSGSPVLDDSDGGGRVVGVHSAGGADRAN 175
 
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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