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Conserved domains on  [gi|2392454]
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Chain H, ALPHA-THROMBIN

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 ...
1-253 1.42e-90

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: 267.22  E-value: 1.42e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454    1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454   81 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 160
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454  161 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
gi 2392454  239 FYTHVFRLKKWIQKV 253
Cdd:cd00190 218 VYTRVSSYLDWIQKT 232
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-253 1.42e-90

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: 267.22  E-value: 1.42e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454    1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454   81 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 160
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454  161 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
gi 2392454  239 FYTHVFRLKKWIQKV 253
Cdd:cd00190 218 VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-250 5.68e-88

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: 260.69  E-value: 5.68e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454       1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVekISM 80
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVR------GSDPSNIRVRLGSHDLSSGEEGQ--VIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454      81 LDKIYIHPRYNwKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGNrretwTTSVAEVQPSVL 160
Cdd:smart00020  73 VSKVIIHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP---AGTTCTVSGWGR-----TSEGAGSLPDTL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454     161 QVVNLPLVERPVCKA--STRIRITDNMFCAGYkPGEGKrgDACEGDSGGPFVMKspyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:smart00020 144 QEVNVPIVSNATCRRaySGGGAITDNMLCAGG-LEGGK--DACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPG 217
                          250
                   ....*....|..
gi 2392454     239 FYTHVFRLKKWI 250
Cdd:smart00020 218 VYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-250 1.36e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.18  E-value: 1.36e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454      1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLYPpwdknftvDDLLVRIGKHSRTRYERKVEKISM 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-HFCGGSLISENWVLTAAHCVSGA--------SDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454     81 lDKIYIHPRYNWkENLDRDIALLKLKRPIELSDYIHPVCLPDkqtAAKLLHAGFKGRVTGWGNRRETWTtsvaevqPSVL 160
Cdd:pfam00089  72 -EKIIVHPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPD---ASSDLPVGTTCTVSGWGNTKTLGP-------SDTL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454    161 QVVNLPLVERPVCKASTRIRITDNMFCAGYKpgegkRGDACEGDSGGPFVMKSPYnnrwyQMGIVSWGEGCDRDGKYGFY 240
Cdd:pfam00089 140 QEVTVPVVSRETCRSAYGGTVTDTMICAGAG-----GKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYPGVY 209
                         250
                  ....*....|
gi 2392454    241 THVFRLKKWI 250
Cdd:pfam00089 210 TPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-258 8.03e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 207.96  E-value: 8.03e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454    1 IVEGQDAEVGLSPWQVMLFRKS-PQELLCGASLISDRWVLTAAHCLlyppwdKNFTVDDLLVRIGKHSRTRYERKVEKIs 79
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgPSGQFCGGTLIAPRWVLTAAHCV------DGDGPSDLRVVIGSTDLSTSGGTVVKV- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454   80 mlDKIYIHPRYNWkENLDRDIALLKLKRPIelsDYIHPVCLPDKQTAAKllhAGFKGRVTGWGNRRETWTTsvaevQPSV 159
Cdd:COG5640 104 --ARIVVHPDYDP-ATPGNDIALLKLATPV---PGVAPAPLATSADAAA---PGTPATVAGWGRTSEGPGS-----QSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454  160 LQVVNLPLVERPVCKASTRIrITDNMFCAGYKPGegkRGDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYGF 239
Cdd:COG5640 170 LRKADVPVVSDATCAAYGGF-DGGTMLCAGYPEG---GKDACQGDSGGPLVVKD--GGGWVLVGVVSWGGGPCAAGYPGV 243
                       250
                ....*....|....*....
gi 2392454  240 YTHVFRLKKWIQKVIDRLG 258
Cdd:COG5640 244 YTRVSAYRDWIKSTAGGLG 262
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-253 1.42e-90

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: 267.22  E-value: 1.42e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454    1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454   81 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 160
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454  161 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
gi 2392454  239 FYTHVFRLKKWIQKV 253
Cdd:cd00190 218 VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
1-250 5.68e-88

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: 260.69  E-value: 5.68e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454       1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVekISM 80
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVR------GSDPSNIRVRLGSHDLSSGEEGQ--VIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454      81 LDKIYIHPRYNwKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGNrretwTTSVAEVQPSVL 160
Cdd:smart00020  73 VSKVIIHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP---AGTTCTVSGWGR-----TSEGAGSLPDTL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454     161 QVVNLPLVERPVCKA--STRIRITDNMFCAGYkPGEGKrgDACEGDSGGPFVMKspyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:smart00020 144 QEVNVPIVSNATCRRaySGGGAITDNMLCAGG-LEGGK--DACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPG 217
                          250
                   ....*....|..
gi 2392454     239 FYTHVFRLKKWI 250
Cdd:smart00020 218 VYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-250 1.36e-76

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 231.18  E-value: 1.36e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454      1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLYPpwdknftvDDLLVRIGKHSRTRYERKVEKISM 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-HFCGGSLISENWVLTAAHCVSGA--------SDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454     81 lDKIYIHPRYNWkENLDRDIALLKLKRPIELSDYIHPVCLPDkqtAAKLLHAGFKGRVTGWGNRRETWTtsvaevqPSVL 160
Cdd:pfam00089  72 -EKIIVHPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPD---ASSDLPVGTTCTVSGWGNTKTLGP-------SDTL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454    161 QVVNLPLVERPVCKASTRIRITDNMFCAGYKpgegkRGDACEGDSGGPFVMKSPYnnrwyQMGIVSWGEGCDRDGKYGFY 240
Cdd:pfam00089 140 QEVTVPVVSRETCRSAYGGTVTDTMICAGAG-----GKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYPGVY 209
                         250
                  ....*....|
gi 2392454    241 THVFRLKKWI 250
Cdd:pfam00089 210 TPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-258 8.03e-67

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 207.96  E-value: 8.03e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454    1 IVEGQDAEVGLSPWQVMLFRKS-PQELLCGASLISDRWVLTAAHCLlyppwdKNFTVDDLLVRIGKHSRTRYERKVEKIs 79
Cdd:COG5640  31 IVGGTPATVGEYPWMVALQSSNgPSGQFCGGTLIAPRWVLTAAHCV------DGDGPSDLRVVIGSTDLSTSGGTVVKV- 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454   80 mlDKIYIHPRYNWkENLDRDIALLKLKRPIelsDYIHPVCLPDKQTAAKllhAGFKGRVTGWGNRRETWTTsvaevQPSV 159
Cdd:COG5640 104 --ARIVVHPDYDP-ATPGNDIALLKLATPV---PGVAPAPLATSADAAA---PGTPATVAGWGRTSEGPGS-----QSGT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454  160 LQVVNLPLVERPVCKASTRIrITDNMFCAGYKPGegkRGDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYGF 239
Cdd:COG5640 170 LRKADVPVVSDATCAAYGGF-DGGTMLCAGYPEG---GKDACQGDSGGPLVVKD--GGGWVLVGVVSWGGGPCAAGYPGV 243
                       250
                ....*....|....*....
gi 2392454  240 YTHVFRLKKWIQKVIDRLG 258
Cdd:COG5640 244 YTRVSAYRDWIKSTAGGLG 262
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
27-251 2.07e-10

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.53  E-value: 2.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454   27 LCGASLISDRWVLTAAHCLLYPP---WDKNFTVddllvrigkhsRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALL 103
Cdd:COG3591  13 VCTGTLIGPNLVLTAGHCVYDGAgggWATNIVF-----------VPGYNGGPYGTATATRFRVPPGWVASGDAGYDYALL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454  104 KLKRPIELS-DYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTtsVAEVQPSVLQVvnlplverpvckastririt 182
Cdd:COG3591  82 RLDEPLGDTtGWLGLAFNDAPLAGEPVTIIGYPGDRPKDLSLDCSGR--VTGVQGNRLSY-------------------- 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2392454  183 dnmfcagykpgegkRGDACEGDSGGPFVMKSpyNNRWYQMGIVSWG-EGCDRDGKYGFYTHVFRLKKWIQ 251
Cdd:COG3591 140 --------------DCDTTGGSSGSPVLDDS--DGGGRVVGVHSAGgADRANTGVRLTSAIVAALRAWAS 193
 
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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