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Conserved domains on  [gi|10835843|pdb|1FI8|B]
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Chain B, NATURAL KILLER CELL PROTEASE 1

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

 Zoom to residue level

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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 ...
1-224 1.22e-100

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: 291.49  E-value: 1.22e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B        1 IIGGHEAKPHSRPYMAYLQImdeYSGSKKCGGFLIREDFVLTAAHC----SGSKIQVTLGAHNIKEQEKMQQIIPVVKII 76
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B       77 PHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKC-E 155
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECkR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1FI8_B      156 SYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKK----VAAGIVSYGQNDGS--TPRAFTKVSTFLSWIKKT 224
Cdd:cd00190 158 AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARpnYPGVYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-224 1.22e-100

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: 291.49  E-value: 1.22e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B        1 IIGGHEAKPHSRPYMAYLQImdeYSGSKKCGGFLIREDFVLTAAHC----SGSKIQVTLGAHNIKEQEKMQQIIPVVKII 76
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B       77 PHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKC-E 155
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECkR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1FI8_B      156 SYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKK----VAAGIVSYGQNDGS--TPRAFTKVSTFLSWIKKT 224
Cdd:cd00190 158 AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARpnYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-221 1.40e-94

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: 276.10  E-value: 1.40e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B           1 IIGGHEAKPHSRPYMAYLQImdeYSGSKKCGGFLIREDFVLTAAHC----SGSKIQVTLGAHNIKEQEKmQQIIPVVKII 76
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B          77 PHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPM-GKYSDTLQEVELTVQEDQKCE 155
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1FI8_B         156 SYLKNYF-DKANEICAGDPKIKRASFRGDSGGPLVCKK---VAAGIVSYGQN--DGSTPRAFTKVSTFLSWI 221
Cdd:smart00020 158 RAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGcaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-221 2.10e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.64  E-value: 2.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B          1 IIGGHEAKPHSRPYMAYLQIMdeySGSKKCGGFLIREDFVLTAAHC--SGSKIQVTLGAHNIKEQEKMQQIIPVVKIIPH 78
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS---SGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B         79 PAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPmGKYSDTLQEVELTVQEDQKCESYL 158
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKT-LGPSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1FI8_B        159 KNYFdKANEICAGDpkIKRASFRGDSGGPLVCKKV-AAGIVSYGQN--DGSTPRAFTKVSTFLSWI 221
Cdd:pfam00089 157 GGTV-TDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGcaSGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-227 4.13e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 4.13e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B        1 IIGGHEAKPHSRPYMAYLQIMDEYSGSKkCGGFLIREDFVLTAAHC----SGSKIQVTLGAHNIKEQEkmQQIIPVVKII 76
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNGPSGQF-CGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSG--GTVVKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B       77 PHPAYNSKTISNDIMLLKLkskAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGP-MGKYSDTLQEVELTVQEDQKCE 155
Cdd:COG5640 108 VHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDATCA 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1FI8_B      156 SYlkNYFDKANEICAGDPKIKRASFRGDSGGPLVCKK----VAAGIVSYGQND--GSTPRAFTKVSTFLSWIKKTMKK 227
Cdd:COG5640 185 AY--GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDgggwVLVGVVSWGGGPcaAGYPGVYTRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-224 1.22e-100

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: 291.49  E-value: 1.22e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B        1 IIGGHEAKPHSRPYMAYLQImdeYSGSKKCGGFLIREDFVLTAAHC----SGSKIQVTLGAHNIKEQEKMQQIIPVVKII 76
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQY---TGGRHFCGGSLISPRWVLTAAHCvyssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B       77 PHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKC-E 155
Cdd:cd00190  78 VHPNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECkR 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1FI8_B      156 SYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKK----VAAGIVSYGQNDGS--TPRAFTKVSTFLSWIKKT 224
Cdd:cd00190 158 AYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDngrgVLVGIVSWGSGCARpnYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-221 1.40e-94

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: 276.10  E-value: 1.40e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B           1 IIGGHEAKPHSRPYMAYLQImdeYSGSKKCGGFLIREDFVLTAAHC----SGSKIQVTLGAHNIKEQEKmQQIIPVVKII 76
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQY---GGGRHFCGGSLISPRWVLTAAHCvrgsDPSNIRVRLGSHDLSSGEE-GQVIKVSKVI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B          77 PHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPM-GKYSDTLQEVELTVQEDQKCE 155
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGaGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1FI8_B         156 SYLKNYF-DKANEICAGDPKIKRASFRGDSGGPLVCKK---VAAGIVSYGQN--DGSTPRAFTKVSTFLSWI 221
Cdd:smart00020 158 RAYSGGGaITDNMLCAGGLEGGKDACQGDSGGPLVCNDgrwVLVGIVSWGSGcaRPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-221 2.10e-78

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.64  E-value: 2.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B          1 IIGGHEAKPHSRPYMAYLQIMdeySGSKKCGGFLIREDFVLTAAHC--SGSKIQVTLGAHNIKEQEKMQQIIPVVKIIPH 78
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLS---SGKHFCGGSLISENWVLTAAHCvsGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B         79 PAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPmGKYSDTLQEVELTVQEDQKCESYL 158
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKT-LGPSDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1FI8_B        159 KNYFdKANEICAGDpkIKRASFRGDSGGPLVCKKV-AAGIVSYGQN--DGSTPRAFTKVSTFLSWI 221
Cdd:pfam00089 157 GGTV-TDTMICAGA--GGKDACQGDSGGPLVCSDGeLIGIVSWGYGcaSGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-227 4.13e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 194.87  E-value: 4.13e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B        1 IIGGHEAKPHSRPYMAYLQIMDEYSGSKkCGGFLIREDFVLTAAHC----SGSKIQVTLGAHNIKEQEkmQQIIPVVKII 76
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNGPSGQF-CGGTLIAPRWVLTAAHCvdgdGPSDLRVVIGSTDLSTSG--GTVVKVARIV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B       77 PHPAYNSKTISNDIMLLKLkskAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGP-MGKYSDTLQEVELTVQEDQKCE 155
Cdd:COG5640 108 VHPDYDPATPGNDIALLKL---ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDATCA 184
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1FI8_B      156 SYlkNYFDKANEICAGDPKIKRASFRGDSGGPLVCKK----VAAGIVSYGQND--GSTPRAFTKVSTFLSWIKKTMKK 227
Cdd:COG5640 185 AY--GGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDgggwVLVGVVSWGGGPcaAGYPGVYTRVSAYRDWIKSTAGG 260
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
32-189 3.16e-04

Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 39.71  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B         32 GFLIRED-FVLTAAHCSGSKIQVTLGAHNIKEQEKmqQIIPVVKIIPHPAYnsktisnDIMLLKLkskAKRSSAVKPLNL 110
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLADG--REYPATVVARDPDL-------DLALLRV---SGDGRGLPPLPL 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1FI8_B        111 pRRNVKVKPGDVCYVAGWgklgPMGKYSDTLQEVELTVQEDQKCESYLKNYFDkaneiCAGDPkikrasFRGDSGGPLV 189
Cdd:pfam13365  71 -GDSEPLVGGERVYAVGY----PLGGEKLSLSEGIVSGVDEGRDGGDDGRVIQ-----TDAAL------SPGSSGGPVF 133
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
30-206 5.80e-04

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 39.66  E-value: 5.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B       30 CGGFLIREDFVLTAAHC--------SGSKIQVTLGAHNikeqeKMQQIIPVVKIIPHPAY-NSKTISNDIMLLKLKSKAk 100
Cdd:COG3591  14 CTGTLIGPNLVLTAGHCvydgagggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWvASGDAGYDYALLRLDEPL- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1FI8_B      101 rSSAVKPLNLpRRNVKVKPGDVCYVAGWgklgPMGKYSDtlqeveLTVQEDQKCESYLKN--YFDkaneiCAGDPkikra 178
Cdd:COG3591  88 -GDTTGWLGL-AFNDAPLAGEPVTIIGY----PGDRPKD------LSLDCSGRVTGVQGNrlSYD-----CDTTG----- 145
                       170       180       190
                ....*....|....*....|....*....|..
1FI8_B      179 sfrGDSGGPLVCKK----VAAGIVSYGQNDGS 206
Cdd:COG3591 146 ---GSSGSPVLDDSdgggRVVGVHSAGGADRA 174
 
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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