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Conserved domains on  [gi|2392458|pdb|1MKX|K]
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Chain K, PRETHROMBIN-2

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

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 ...
50-302 6.23e-92

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  Cd Length: 232  Bit Score: 272.61  E-value: 6.23e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K       50 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 129
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      130 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 209
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      210 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 287
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
1MKX_K      288 FYTHVFRLKKWIQKV 302
Cdd:cd00190 218 VYTRVSSYLDWIQKT 232
Thrombin_light pfam09396
Thrombin light chain. Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts ...
3-49 5.17e-29

Thrombin light chain. Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.


:

Pssm-ID: 370463  Cd Length: 47  Bit Score: 105.06  E-value: 5.17e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
1MKX_K          3 EDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR 49
Cdd:pfam09396   1 TEEFQTFFNPRTFGQGEADCGLRPLFEKKSKKDKTEKELLESYIGGR 47
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
50-302 6.23e-92

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  Cd Length: 232  Bit Score: 272.61  E-value: 6.23e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K       50 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 129
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      130 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 209
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      210 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 287
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
1MKX_K      288 FYTHVFRLKKWIQKV 302
Cdd:cd00190 218 VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-299 1.26e-90

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: 269.16  E-value: 1.26e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K          49 RIVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVekIS 128
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVR------GSDPSNIRVRLGSHDLSSGEEGQ--VI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K         129 MLDKIYIHPRYNwKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGNrretwTTSVAEVQPSV 208
Cdd:smart00020  72 KVSKVIIHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP---AGTTCTVSGWGR-----TSEGAGSLPDT 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K         209 LQVVNLPLVERPVCKA--STRIRITDNMFCAGYkPGEGKrgDACEGDSGGPFVMKspyNNRWYQMGIVSWGEGCDRDGKY 286
Cdd:smart00020 143 LQEVNVPIVSNATCRRaySGGGAITDNMLCAGG-LEGGK--DACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKP 216
                          250
                   ....*....|...
1MKX_K         287 GFYTHVFRLKKWI 299
Cdd:smart00020 217 GVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin.
50-299 5.36e-78

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 236.56  E-value: 5.36e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K         50 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLYPpwdknftvDDLLVRIGKHSRTRYERKVEKISM 129
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-HFCGGSLISENWVLTAAHCVSGA--------SDVQVVLGEHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K        130 lDKIYIHPRYNWkENLDRDIALLKLKRPIELSDYIHPVCLPDkqtAAKLLHAGFKGRVTGWGNRRETWTtsvaevqPSVL 209
Cdd:pfam00089  72 -AKVIVHPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPD---AGADLPVGTTCTVSGWGNTKTLGP-------PDTL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K        210 QVVNLPLVERPVCKASTRIRITDNMFCAGYKpgegkRGDACEGDSGGPFVMKSPYnnrwyQMGIVSWGEGCDRDGKYGFY 289
Cdd:pfam00089 140 QEVTVPVVSRETCRSAYGGTVTDTMICAGAG-----GKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYPGVY 209
                         250
                  ....*....|
1MKX_K        290 THVFRLKKWI 299
Cdd:pfam00089 210 TPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
43-308 4.35e-30

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 117.67  E-value: 4.35e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K       43 ESYIEGRIVEGQDAEVGLSPWQVMLF---RKSPQELLCGASLISDRWVLTAAHCLlyppwDKN--FTVDDLLVRIGKHSR 117
Cdd:COG5640  26 ADEVSSRIIGGSNANAGEYPSLVALVdriSDYVSGTFCGGSKLGGRYVLTAAHCA-----DASspISSDVNRVVVDLNDS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      118 TRYER-KVEkismldKIYIHPRYNwKENLDRDIALLKLKRPIEL-SDYIHPVCLPDKQ-----TAAKLLHAGFKGRVTGW 190
Cdd:COG5640 101 SQAERgHVR------TIYVHEFYS-PGNLGNDIAVLELARAASLpRVKITSFDASDTFlnsvtTVSPMTNGTFGVTTPSD 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      191 GNRretwttSVAevQPSVLQVVNLPLVERPVCKASTRIRITDNM------FCAGYKPgegkrGDACEGDSGGPFVMKSpy 264
Cdd:COG5640 174 VPR------SSP--KGTILHEVAVLFVPLSTCAQYKGCANASDGatgltgFCAGRPP-----KDACQGDSGGPIFHKG-- 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
1MKX_K      265 NNRWYQMGIVSWGEG-CDRDGKYGFYTHVFRLKKWIQKVIDRLGS 308
Cdd:COG5640 239 EEGRVQRGVVSWGDGgCGGTLIPGVYTNVSNYQDWIAAMTNGLSY 283
Thrombin_light pfam09396
Thrombin light chain. Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts ...
3-49 5.17e-29

Thrombin light chain. Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.


Pssm-ID: 370463  Cd Length: 47  Bit Score: 105.06  E-value: 5.17e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
1MKX_K          3 EDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR 49
Cdd:pfam09396   1 TEEFQTFFNPRTFGQGEADCGLRPLFEKKSKKDKTEKELLESYIGGR 47
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
50-302 6.23e-92

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  Cd Length: 232  Bit Score: 272.61  E-value: 6.23e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K       50 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVEKISm 129
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYTGGR-HFCGGSLISPRWVLTAAHCVY------SSAPSNYTVRLGSHDLSSNEGGGQVIK- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      130 LDKIYIHPRYNWKeNLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGnrretwTTSVAEVQPSVL 209
Cdd:cd00190  73 VKKVIVHPNYNPS-TYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLP---AGTTCTVSGWG------RTSEGGPLPDVL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      210 QVVNLPLVERPVCKASTR--IRITDNMFCAGYKPGeGKrgDACEGDSGGPFVMKSpyNNRWYQMGIVSWGEGCDRDGKYG 287
Cdd:cd00190 143 QEVNVPIVSNAECKRAYSygGTITDNMLCAGGLEG-GK--DACQGDSGGPLVCND--NGRGVLVGIVSWGSGCARPNYPG 217
                       250
                ....*....|....*
1MKX_K      288 FYTHVFRLKKWIQKV 302
Cdd:cd00190 218 VYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
49-299 1.26e-90

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: 269.16  E-value: 1.26e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K          49 RIVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLyppwdkNFTVDDLLVRIGKHSRTRYERKVekIS 128
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGR-HFCGGSLISPRWVLTAAHCVR------GSDPSNIRVRLGSHDLSSGEEGQ--VI 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K         129 MLDKIYIHPRYNwKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKllhAGFKGRVTGWGNrretwTTSVAEVQPSV 208
Cdd:smart00020  72 KVSKVIIHPNYN-PSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVP---AGTTCTVSGWGR-----TSEGAGSLPDT 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K         209 LQVVNLPLVERPVCKA--STRIRITDNMFCAGYkPGEGKrgDACEGDSGGPFVMKspyNNRWYQMGIVSWGEGCDRDGKY 286
Cdd:smart00020 143 LQEVNVPIVSNATCRRaySGGGAITDNMLCAGG-LEGGK--DACQGDSGGPLVCN---DGRWVLVGIVSWGSGCARPGKP 216
                          250
                   ....*....|...
1MKX_K         287 GFYTHVFRLKKWI 299
Cdd:smart00020 217 GVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin.
50-299 5.36e-78

Trypsin.


Pssm-ID: 365866  Cd Length: 219  Bit Score: 236.56  E-value: 5.36e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K         50 IVEGQDAEVGLSPWQVMLFRKSPQeLLCGASLISDRWVLTAAHCLLYPpwdknftvDDLLVRIGKHSRTRYERKVEKISM 129
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGK-HFCGGSLISENWVLTAAHCVSGA--------SDVQVVLGEHNIVLREGGEQKFDV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K        130 lDKIYIHPRYNWkENLDRDIALLKLKRPIELSDYIHPVCLPDkqtAAKLLHAGFKGRVTGWGNRRETWTtsvaevqPSVL 209
Cdd:pfam00089  72 -AKVIVHPNYNP-DTLDNDIALLKLESPVTLGDTVRPICLPD---AGADLPVGTTCTVSGWGNTKTLGP-------PDTL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K        210 QVVNLPLVERPVCKASTRIRITDNMFCAGYKpgegkRGDACEGDSGGPFVMKSPYnnrwyQMGIVSWGEGCDRDGKYGFY 289
Cdd:pfam00089 140 QEVTVPVVSRETCRSAYGGTVTDTMICAGAG-----GKDACQGDSGGPLVCSDGE-----LIGIVSWGYGCASGNYPGVY 209
                         250
                  ....*....|
1MKX_K        290 THVFRLKKWI 299
Cdd:pfam00089 210 TPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
43-308 4.35e-30

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


Pssm-ID: 227927 [Multi-domain]  Cd Length: 413  Bit Score: 117.67  E-value: 4.35e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K       43 ESYIEGRIVEGQDAEVGLSPWQVMLF---RKSPQELLCGASLISDRWVLTAAHCLlyppwDKN--FTVDDLLVRIGKHSR 117
Cdd:COG5640  26 ADEVSSRIIGGSNANAGEYPSLVALVdriSDYVSGTFCGGSKLGGRYVLTAAHCA-----DASspISSDVNRVVVDLNDS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      118 TRYER-KVEkismldKIYIHPRYNwKENLDRDIALLKLKRPIEL-SDYIHPVCLPDKQ-----TAAKLLHAGFKGRVTGW 190
Cdd:COG5640 101 SQAERgHVR------TIYVHEFYS-PGNLGNDIAVLELARAASLpRVKITSFDASDTFlnsvtTVSPMTNGTFGVTTPSD 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MKX_K      191 GNRretwttSVAevQPSVLQVVNLPLVERPVCKASTRIRITDNM------FCAGYKPgegkrGDACEGDSGGPFVMKSpy 264
Cdd:COG5640 174 VPR------SSP--KGTILHEVAVLFVPLSTCAQYKGCANASDGatgltgFCAGRPP-----KDACQGDSGGPIFHKG-- 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
1MKX_K      265 NNRWYQMGIVSWGEG-CDRDGKYGFYTHVFRLKKWIQKVIDRLGS 308
Cdd:COG5640 239 EEGRVQRGVVSWGDGgCGGTLIPGVYTNVSNYQDWIAAMTNGLSY 283
Thrombin_light pfam09396
Thrombin light chain. Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts ...
3-49 5.17e-29

Thrombin light chain. Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.


Pssm-ID: 370463  Cd Length: 47  Bit Score: 105.06  E-value: 5.17e-29
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
1MKX_K          3 EDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGR 49
Cdd:pfam09396   1 TEEFQTFFNPRTFGQGEADCGLRPLFEKKSKKDKTEKELLESYIGGR 47
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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