NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2392457|pdb|1MKX|H]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.36e-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: 1.36e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H        1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H       81 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 160
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H      161 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
1MKX_H      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 1.36e-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: 1.36e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H        1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H       81 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 160
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H      161 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
1MKX_H      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 5.45e-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 [Multi-domain]  Cd Length: 229  Bit Score: 260.69  E-value: 5.45e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H           1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVekISM 80
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVR------GSDPSNIRVRLGSHDLSSGEEGQ--VIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H          81 LDKIYIHPRYNwKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGNrretwTTSVAEVQPSVL 160
Cdd:smart00020  73 VSKVIIHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP---AGTTCTVSGWGR-----TSEGAGSLPDTL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H         161 QVVNLPLVERPVCKA--STRIRITDNMFCAGYkPGEGKrgDACEGDSGGPFVMKspyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:smart00020 144 QEVNVPIVSNATCRRaySGGGAITDNMLCAGG-LEGGK--DACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPG 217
                          250
                   ....*....|..
1MKX_H         239 FYTHVFRLKKWI 250
Cdd:smart00020 218 VYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-250 1.27e-76

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 1.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H          1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLYPpwdknftvDDLLVRIGKHSRTRYERKVEKISM 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-HFCGGSLISENWVLTAAHCVSGA--------SDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H         81 lDKIYIHPRYNWkENLDRDIALLKLKRPIELSDYIHPVCLPDkqtAAKLLHAGFKGRVTGWGNRRETWTtsvaevqPSVL 160
Cdd:pfam00089  72 -EKIIVHPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPD---ASSDLPVGTTCTVSGWGNTKTLGP-------SDTL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H        161 QVVNLPLVERPVCKASTRIRITDNMFCAGYKpgegkRGDACEGDSGGPFVMKSPYnnrwyQMGIVSWGEGCDRDGKYGFY 240
Cdd:pfam00089 140 QEVTVPVVSRETCRSAYGGTVTDTMICAGAG-----GKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYPGVY 209
                         250
                  ....*....|
1MKX_H        241 THVFRLKKWI 250
Cdd:pfam00089 210 TPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-259 7.75e-29

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 112.66  E-value: 7.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H        1 IVEGQDAEVGLSPWQVMLF---RKSPQELLCGASLISDRWVLTAAHCLlyppwDKN--FTVDDLLVRIGKHSRTRYER-K 74
Cdd:COG5640  33 IIGGSNANAGEYPSLVALVdriSDYVSGTFCGGSKLGGRYVLTAAHCA-----DASspISSDVNRVVVDLNDSSQAERgH 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H       75 VEkismldKIYIHPRYNwKENLDRDIALLKLKRPIEL-SDYIHPVCLPDKQ-----TAAKLLHAGFKGRVTGWGNRretw 148
Cdd:COG5640 108 VR------TIYVHEFYS-PGNLGNDIAVLELARAASLpRVKITSFDASDTFlnsvtTVSPMTNGTFGVTTPSDVPR---- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H      149 ttSVAevQPSVLQVVNLPLVERPVCKASTRIRITDNM------FCAGYKPgegkrGDACEGDSGGPFVMKSpyNNRWYQM 222
Cdd:COG5640 177 --SSP--KGTILHEVAVLFVPLSTCAQYKGCANASDGatgltgFCAGRPP-----KDACQGDSGGPIFHKG--EEGRVQR 245
                       250       260       270
                ....*....|....*....|....*....|....*...
1MKX_H      223 GIVSWGEG-CDRDGKYGFYTHVFRLKKWIQKVIDRLGS 259
Cdd:COG5640 246 GVVSWGDGgCGGTLIPGVYTNVSNYQDWIAAMTNGLSY 283
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
1-253 1.36e-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: 1.36e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H        1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 80
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H       81 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 160
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H      161 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
1MKX_H      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 5.45e-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 [Multi-domain]  Cd Length: 229  Bit Score: 260.69  E-value: 5.45e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H           1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVekISM 80
Cdd:smart00020   2 IVGGSEANIGSFPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVR------GSDPSNIRVRLGSHDLSSGEEGQ--VIK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H          81 LDKIYIHPRYNwKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGNrretwTTSVAEVQPSVL 160
Cdd:smart00020  73 VSKVIIHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP---AGTTCTVSGWGR-----TSEGAGSLPDTL 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H         161 QVVNLPLVERPVCKA--STRIRITDNMFCAGYkPGEGKrgDACEGDSGGPFVMKspyNNRWYQMGIVSWGEGCDRDGKYG 238
Cdd:smart00020 144 QEVNVPIVSNATCRRaySGGGAITDNMLCAGG-LEGGK--DACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKPG 217
                          250
                   ....*....|..
1MKX_H         239 FYTHVFRLKKWI 250
Cdd:smart00020 218 VYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1-250 1.27e-76

Trypsin;


Pssm-ID: 395042 [Multi-domain]  Cd Length: 219  Bit Score: 231.56  E-value: 1.27e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H          1 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLYPpwdknftvDDLLVRIGKHSRTRYERKVEKISM 80
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-HFCGGSLISENWVLTAAHCVSGA--------SDVKVVLGAHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H         81 lDKIYIHPRYNWkENLDRDIALLKLKRPIELSDYIHPVCLPDkqtAAKLLHAGFKGRVTGWGNRRETWTtsvaevqPSVL 160
Cdd:pfam00089  72 -EKIIVHPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPD---ASSDLPVGTTCTVSGWGNTKTLGP-------SDTL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H        161 QVVNLPLVERPVCKASTRIRITDNMFCAGYKpgegkRGDACEGDSGGPFVMKSPYnnrwyQMGIVSWGEGCDRDGKYGFY 240
Cdd:pfam00089 140 QEVTVPVVSRETCRSAYGGTVTDTMICAGAG-----GKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYPGVY 209
                         250
                  ....*....|
1MKX_H        241 THVFRLKKWI 250
Cdd:pfam00089 210 TPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
1-259 7.75e-29

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 112.66  E-value: 7.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H        1 IVEGQDAEVGLSPWQVMLF---RKSPQELLCGASLISDRWVLTAAHCLlyppwDKN--FTVDDLLVRIGKHSRTRYER-K 74
Cdd:COG5640  33 IIGGSNANAGEYPSLVALVdriSDYVSGTFCGGSKLGGRYVLTAAHCA-----DASspISSDVNRVVVDLNDSSQAERgH 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H       75 VEkismldKIYIHPRYNwKENLDRDIALLKLKRPIEL-SDYIHPVCLPDKQ-----TAAKLLHAGFKGRVTGWGNRretw 148
Cdd:COG5640 108 VR------TIYVHEFYS-PGNLGNDIAVLELARAASLpRVKITSFDASDTFlnsvtTVSPMTNGTFGVTTPSDVPR---- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_H      149 ttSVAevQPSVLQVVNLPLVERPVCKASTRIRITDNM------FCAGYKPgegkrGDACEGDSGGPFVMKSpyNNRWYQM 222
Cdd:COG5640 177 --SSP--KGTILHEVAVLFVPLSTCAQYKGCANASDGatgltgFCAGRPP-----KDACQGDSGGPIFHKG--EEGRVQR 245
                       250       260       270
                ....*....|....*....|....*....|....*...
1MKX_H      223 GIVSWGEG-CDRDGKYGFYTHVFRLKKWIQKVIDRLGS 259
Cdd:COG5640 246 GVVSWGDGgCGGTLIPGVYTNVSNYQDWIAAMTNGLSY 283
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH