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Conserved domains on  [gi|3891639|pdb|1KIG|H]
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Chain H, FACTOR XA

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 ...
1-231 6.45e-101

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: 292.64  E-value: 6.45e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H        1 IVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLH--QAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHS 78
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H       79 RFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDwaeATLMTQKTGIVSGFGRTHEKGRLSSTLKMLEVPYVDRSTCK- 157
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1KIG_H      158 -LSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKI 231
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 ...
1-231 6.45e-101

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: 292.64  E-value: 6.45e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H        1 IVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLH--QAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHS 78
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H       79 RFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDwaeATLMTQKTGIVSGFGRTHEKGRLSSTLKMLEVPYVDRSTCK- 157
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1KIG_H      158 -LSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKI 231
Cdd:cd00190 158 aYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-228 1.79e-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: 276.48  E-value: 1.79e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H           1 IVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLH--QAKRFTVRVGDRNTEQEEGNEMaHEVEMTVKHS 78
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEEGQV-IKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H          79 RFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDwaeATLMTQKTGIVSGFGRTHE-KGRLSSTLKMLEVPYVDRSTCK 157
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN---YNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1KIG_H         158 --LSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRfKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWI 228
Cdd:smart00020 158 raYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-228 1.02e-80

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 241.19  E-value: 1.02e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H          1 IVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRF 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H         81 VKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDwaeATLMTQKTGIVSGFGRTHEKGRlSSTLKMLEVPYVDRSTCKLSS 160
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAS---SDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1KIG_H        161 SFTITPNMFCAGYDTQpeDACQGDSGGPHVTRFKdtyFVTGIVSWGEGCARKGKFGVYTKVSNFLKWI 228
Cdd:pfam00089 157 GGTVTDTMICAGAGGK--DACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-234 3.59e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 195.25  E-value: 3.59e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H        1 IVGGRDCAEGECPWQALLVNEE--NEGFCGGTILNEFYVLTAAHCL--HQAKRFTVRVGDRNTEQEEGNEmaHEVEMTVK 76
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVdgDGPSDLRVVIGSTDLSTSGGTV--VKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H       77 HSRFVKETYDFDIAVLRLKTPIRfrrNVAPACLPEKDWAEATlmtQKTGIVSGFGRTHE-KGRLSSTLKMLEVPYVDRST 155
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAP---GTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1KIG_H      156 CKLSSSFtITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKIMKA 234
Cdd:COG5640 183 CAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-231 6.45e-101

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: 292.64  E-value: 6.45e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H        1 IVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLH--QAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHS 78
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYssAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVHP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H       79 RFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDwaeATLMTQKTGIVSGFGRTHEKGRLSSTLKMLEVPYVDRSTCK- 157
Cdd:cd00190  81 NYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSG---YNLPAGTTCTVSGWGRTSEGGPLPDVLQEVNVPIVSNAECKr 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1KIG_H      158 -LSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKI 231
Cdd:cd00190 158 aYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-228 1.79e-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: 276.48  E-value: 1.79e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H           1 IVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLH--QAKRFTVRVGDRNTEQEEGNEMaHEVEMTVKHS 78
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRgsDPSNIRVRLGSHDLSSGEEGQV-IKVSKVIIHP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H          79 RFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDwaeATLMTQKTGIVSGFGRTHE-KGRLSSTLKMLEVPYVDRSTCK 157
Cdd:smart00020  81 NYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSN---YNVPAGTTCTVSGWGRTSEgAGSLPDTLQEVNVPIVSNATCR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1KIG_H         158 --LSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRfKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWI 228
Cdd:smart00020 158 raYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-228 1.02e-80

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 241.19  E-value: 1.02e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H          1 IVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRF 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASDVKVVLGAHNIVLREGGEQKFDVEKIIVHPNY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H         81 VKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDwaeATLMTQKTGIVSGFGRTHEKGRlSSTLKMLEVPYVDRSTCKLSS 160
Cdd:pfam00089  81 NPDTLDNDIALLKLESPVTLGDTVRPICLPDAS---SDLPVGTTCTVSGWGNTKTLGP-SDTLQEVTVPVVSRETCRSAY 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1KIG_H        161 SFTITPNMFCAGYDTQpeDACQGDSGGPHVTRFKdtyFVTGIVSWGEGCARKGKFGVYTKVSNFLKWI 228
Cdd:pfam00089 157 GGTVTDTMICAGAGGK--DACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-234 3.59e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 195.25  E-value: 3.59e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H        1 IVGGRDCAEGECPWQALLVNEE--NEGFCGGTILNEFYVLTAAHCL--HQAKRFTVRVGDRNTEQEEGNEmaHEVEMTVK 76
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgpSGQFCGGTLIAPRWVLTAAHCVdgDGPSDLRVVIGSTDLSTSGGTV--VKVARIVV 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H       77 HSRFVKETYDFDIAVLRLKTPIRfrrNVAPACLPEKDWAEATlmtQKTGIVSGFGRTHE-KGRLSSTLKMLEVPYVDRST 155
Cdd:COG5640 109 HPDYDPATPGNDIALLKLATPVP---GVAPAPLATSADAAAP---GTPATVAGWGRTSEgPGSQSGTLRKADVPVVSDAT 182
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1KIG_H      156 CKLSSSFtITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKIMKA 234
Cdd:COG5640 183 CAAYGGF-DGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
18-206 7.08e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 56.61  E-value: 7.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H       18 LVNEENEGFCGGTILNEFYVLTAAHCLHQ------AKRFTVRVGDRNTEQEEgnemAHEVEMTVKHSRFVKETYDFDIAV 91
Cdd:COG3591   5 LETDGGGGVCTGTLIGPNLVLTAGHCVYDgagggwATNIVFVPGYNGGPYGT----ATATRFRVPPGWVASGDAGYDYAL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIG_H       92 LRLKTPIRFRRNVAPAclpekDWAEATLMTQKTGIVsGFGRTHEKgrlssTLKMlevpyvdRSTCKLSSsftITPNMFca 171
Cdd:COG3591  81 LRLDEPLGDTTGWLGL-----AFNDAPLAGEPVTII-GYPGDRPK-----DLSL-------DCSGRVTG---VQGNRL-- 137
                       170       180       190
                ....*....|....*....|....*....|....*
1KIG_H      172 GYDTqpeDACQGDSGGPHVTRFKDTYFVTGIVSWG 206
Cdd:COG3591 138 SYDC---DTTGGSSGSPVLDDSDGGGRVVGVHSAG 169
 
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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