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Conserved domains on  [gi|1129957214|ref|XP_019738233|]
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PREDICTED: plasminogen isoform X1 [Hippocampus comes]

Protein Classification

serine protease( domain architecture ID 10840655)

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 ...
 577-802 5.86e-93

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: 290.72  E-value: 5.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 577 IVGGCVAKAHSWPWQISLRTNSGIHFCGGTLIHPQWVLTAAHCLeRSRRPSSYMVILGSHRERSLETSAQQRALEKLVLG 656
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 657 PN------GADIALLKLQRPAVINDKVLPACLPEKDYVVPSGTECYVTGW-GETQGTGGEGVLKETGFPVIENKICNRPS 729
Cdd:cd00190    80 PNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWgRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129957214 730 YLNGRVKDHEMCAGNIDGGTDSCQGDSGGPLVCHAHNKFILQGVTSWGLGCANAMKPGVYARVSKFVDWIDRT 802
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 186-267 2.87e-37

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 134.05  E-value: 2.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  186 EDCIHCNGEDYRGKVSITESGVACQRWDSQEPHNHGYNPNTLPQKYLENNYCRNPDGDPK-PWCFTTNPNKRWEFCSIPR 264
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1129957214  265 CTS 267
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 104-184 6.14e-37

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 133.28  E-value: 6.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  104 ECVNGIGKNYRGTKSRTKSGKTCQRWNAKFPHKPNFTPDNEPKADLESNFCRNPDDDAGGPWCYTTDPDTRWEHCNVPSC 183
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQC 81


                   .
gi 1129957214  184 T 184
Cdd:smart00130  82 E 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 277-357 9.79e-36

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 129.82  E-value: 9.79e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  277 TCATGEGSAYRGTIAVTESGKTCQSWSTQSPHQHNRSPENYACKGLDNNYCRNPDN-ERKPWCYTTDPDTRWEYCSVPTC 355
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 1129957214  356 GD 357
Cdd:smart00130  82 EE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 373-450 5.95e-34

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


:

Pssm-ID: 395005  Cd Length: 79  Bit Score: 124.34  E-value: 5.95e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 373 CYEGDGSSYRGVTSETISGKKCQAWASMSPHRHGK-TPQQYPTADLRRNLCRNPDGDRAPWCYTTDPSVRWEFCNLEKC 450
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 477-560 4.83e-33

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.11  E-value: 4.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  477 RDCKVGNGANYRGSTSITIMGVTCQAWSAQSPHQHnSFTPESHPDKGLDGNSCRNPDNDVNGPWCYTTDRNKKWDYCQIP 556
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLH-RFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 1129957214  557 DCAG 560
Cdd:smart00130  80 QCEE 83
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 40-98 3.05e-09

Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen/hepatocyte growth factor proteins, and various proteins found in Bilateria, such as leech anti-platelet proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


:

Pssm-ID: 238532  Cd Length: 80  Bit Score: 54.40  E-value: 3.05e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129957214  40 KRMYSTNTVEECAAKCDAETSFTCRSFMYVEKDQECWTAGANSKTETV--LRRTSAALYEK 98
Cdd:cd01099    19 KTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVklLYDSNVDYYEN 79
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 577-802 5.86e-93

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: 290.72  E-value: 5.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 577 IVGGCVAKAHSWPWQISLRTNSGIHFCGGTLIHPQWVLTAAHCLeRSRRPSSYMVILGSHRERSLETSAQQRALEKLVLG 656
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 657 PN------GADIALLKLQRPAVINDKVLPACLPEKDYVVPSGTECYVTGW-GETQGTGGEGVLKETGFPVIENKICNRPS 729
Cdd:cd00190    80 PNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWgRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129957214 730 YLNGRVKDHEMCAGNIDGGTDSCQGDSGGPLVCHAHNKFILQGVTSWGLGCANAMKPGVYARVSKFVDWIDRT 802
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 576-799 1.13e-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: 284.57  E-value: 1.13e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  576 RIVGGCVAKAHSWPWQISLRTNSGIHFCGGTLIHPQWVLTAAHCLeRSRRPSSYMVILGSHReRSLETSAQQRALEKLVL 655
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  656 GPN------GADIALLKLQRPAVINDKVLPACLPEKDYVVPSGTECYVTGW--GETQGTGGEGVLKETGFPVIENKICNR 727
Cdd:smart00020  79 HPNynpstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWgrTSEGAGSLPDTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129957214  728 PSYLNGRVKDHEMCAGNIDGGTDSCQGDSGGPLVCHaHNKFILQGVTSWGLGCANAMKPGVYARVSKFVDWI 799
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
577-799 1.28e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 225.78  E-value: 1.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 577 IVGGCVAKAHSWPWQISLRTNSGIHFCGGTLIHPQWVLTAAHCLersRRPSSYMVILGSHRERSLETSAQQRALEKLVLG 656
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 657 PN------GADIALLKLQRPAVINDKVLPACLPEKDYVVPSGTECYVTGWGETQGTGGEGVLKETGFPVIENKICNrpSY 730
Cdd:pfam00089  78 PNynpdtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCR--SA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 731 LNGRVKDHEMCAGniDGGTDSCQGDSGGPLVCHAHnkfILQGVTSWGLGCANAMKPGVYARVSKFVDWI 799
Cdd:pfam00089 156 YGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 576-806 3.97e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 199.11  E-value: 3.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 576 RIVGGCVAKAHSWPWQISLRTNSGI--HFCGGTLIHPQWVLTAAHCLErSRRPSSYMVILGSHRERSleTSAQQRALEKL 653
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLST--SGGTVVKVARI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 654 VLGPN------GADIALLKLQRPAvinDKVLPACLPEKDYVVPSGTECYVTGW--GETQGTGGEGVLKETGFPVIENKIC 725
Cdd:COG5640   107 VVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWgrTSEGPGSQSGTLRKADVPVVSDATC 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 726 NRPSYLNGrvkDHEMCAGNIDGGTDSCQGDSGGPLVCHAHNKFILQGVTSWGLGCANAMKPGVYARVSKFVDWIDRTIKA 805
Cdd:COG5640   184 AAYGGFDG---GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260


                  .
gi 1129957214 806 N 806
Cdd:COG5640   261 L 261
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 186-267 2.87e-37

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 134.05  E-value: 2.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  186 EDCIHCNGEDYRGKVSITESGVACQRWDSQEPHNHGYNPNTLPQKYLENNYCRNPDGDPK-PWCFTTNPNKRWEFCSIPR 264
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1129957214  265 CTS 267
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 104-184 6.14e-37

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 133.28  E-value: 6.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  104 ECVNGIGKNYRGTKSRTKSGKTCQRWNAKFPHKPNFTPDNEPKADLESNFCRNPDDDAGGPWCYTTDPDTRWEHCNVPSC 183
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQC 81


                   .
gi 1129957214  184 T 184
Cdd:smart00130  82 E 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 104-183 1.86e-36

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 131.73  E-value: 1.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 104 ECVNGIGKNYRGTKSRTKSGKTCQRWNAKFPHKPNFTPDNEPKADLESNFCRNPDDDAGGPWCYTTDPDTRWEHCNVPSC 183
Cdd:cd00108     3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 277-357 9.79e-36

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 129.82  E-value: 9.79e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  277 TCATGEGSAYRGTIAVTESGKTCQSWSTQSPHQHNRSPENYACKGLDNNYCRNPDN-ERKPWCYTTDPDTRWEYCSVPTC 355
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 1129957214  356 GD 357
Cdd:smart00130  82 EE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 186-265 9.97e-36

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 129.81  E-value: 9.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 186 EDCIHCNGEDYRGKVSITESGVACQRWDSQEPHNHGYNPNTLPQKYLENNYCRNPDGDPK-PWCFTTNPNKRWEFCSIPR 264
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEgPWCYTTDPNVRWEYCDIPR 81


                  .
gi 1129957214 265 C 265
Cdd:cd00108    82 C 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 188-265 1.43e-35

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 128.96  E-value: 1.43e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 188 CIHCNGEDYRGKVSITESGVACQRWDSQEPHNHG-YNPNTLPQKYLENNYCRNPDGDPKPWCFTTNPNKRWEFCSIPRC 265
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 275-355 5.27e-35

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 127.49  E-value: 5.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 275 ETTCATGEGSAYRGTIAVTESGKTCQSWSTQSPHQHNRSPENYACKGLDNNYCRNPDNE-RKPWCYTTDPDTRWEYCSVP 353
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIP 80


                  ..
gi 1129957214 354 TC 355
Cdd:cd00108    81 RC 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 278-355 1.78e-34

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 125.88  E-value: 1.78e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 278 CATGEGSAYRGTIAVTESGKTCQSWSTQSPHQHNR-SPENYACKGLDNNYCRNPDNERKPWCYTTDPDTRWEYCSVPTC 355
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 373-450 5.95e-34

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 124.34  E-value: 5.95e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 373 CYEGDGSSYRGVTSETISGKKCQAWASMSPHRHGK-TPQQYPTADLRRNLCRNPDGDRAPWCYTTDPSVRWEFCNLEKC 450
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 372-452 4.78e-33

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.11  E-value: 4.78e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  372 DCYEGDGSSYRGVTSETISGKKCQAWASMSPHRHGKTPQQYPTADLRRNLCRNPDGD-RAPWCYTTDPSVRWEFCNLEKC 450
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDsEGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 1129957214  451 SS 452
Cdd:smart00130  82 EE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 477-560 4.83e-33

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.11  E-value: 4.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  477 RDCKVGNGANYRGSTSITIMGVTCQAWSAQSPHQHnSFTPESHPDKGLDGNSCRNPDNDVNGPWCYTTDRNKKWDYCQIP 556
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLH-RFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 1129957214  557 DCAG 560
Cdd:smart00130  80 QCEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 477-559 1.46e-31

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 117.86  E-value: 1.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 477 RDCKVGNGANYRGSTSITIMGVTCQAWSAQSPHQHNsFTPESHPDKGLDGNSCRNPDNDVNGPWCYTTDRNKKWDYCQIP 556
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHK-FNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1129957214 557 DCA 559
Cdd:cd00108    81 RCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 370-451 1.82e-30

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 114.78  E-value: 1.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 370 EDDCYEGDGSSYRGVTSETISGKKCQAWASMSPHRHGKTPQQYPTADLRRNLCRNPDGD-RAPWCYTTDPSVRWEFCNLE 448
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1129957214 449 KCS 451
Cdd:cd00108    81 RCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 105-183 2.53e-30

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 114.33  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 105 CVNGIGKNYRGTKSRTKSGKTCQRWNAKFPHKPNF-TPDNEPKADLESNFCRNPDDDAgGPWCYTTDPDTRWEHCNVPSC 183
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 479-558 2.71e-30

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 113.94  E-value: 2.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 479 CKVGNGANYRGSTSITIMGVTCQAWSAQSPHQHNSFTPESHPDKGLDGNSCRNPDNDVNgPWCYTTDRNKKWDYCQIPDC 558
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 40-98 3.05e-09

Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen/hepatocyte growth factor proteins, and various proteins found in Bilateria, such as leech anti-platelet proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238532  Cd Length: 80  Bit Score: 54.40  E-value: 3.05e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129957214  40 KRMYSTNTVEECAAKCDAETSFTCRSFMYVEKDQECWTAGANSKTETV--LRRTSAALYEK 98
Cdd:cd01099    19 KTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVklLYDSNVDYYEN 79
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 42-98 1.72e-05

divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans hypothetical ORFs and the extracellular portion of plant receptor-like protein kinases. Predicted to possess protein- and/or carbohydrate-binding functions.


Pssm-ID: 214680  Cd Length: 78  Bit Score: 43.72  E-value: 1.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1129957214   42 MYSTNTVEECAAKCdAETSFTCRSFMYVEKDQECWTAGANSKTETVLRRTSAA-LYEK 98
Cdd:smart00473  21 VISVASLEECASKC-LNSNCSCRSFTYNNGTKGCLLWSESSLGDARLFPSGGVdLYEK 77
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 26-99 3.35e-04

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 39.84  E-value: 3.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1129957214  26 SYAKTGGAWLTAINKRMYSTNTVEECAAKCDAETSftCRSFMYVEKDQECWTAGANSKTETVLRRTSAA--LYEKQ 99
Cdd:pfam00024   2 DFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPR--CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKvdYYEKS 75
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 577-802 5.86e-93

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: 290.72  E-value: 5.86e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 577 IVGGCVAKAHSWPWQISLRTNSGIHFCGGTLIHPQWVLTAAHCLeRSRRPSSYMVILGSHRERSLETSAQQRALEKLVLG 656
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCV-YSSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 657 PN------GADIALLKLQRPAVINDKVLPACLPEKDYVVPSGTECYVTGW-GETQGTGGEGVLKETGFPVIENKICNRPS 729
Cdd:cd00190    80 PNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWgRTSEGGPLPDVLQEVNVPIVSNAECKRAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1129957214 730 YLNGRVKDHEMCAGNIDGGTDSCQGDSGGPLVCHAHNKFILQGVTSWGLGCANAMKPGVYARVSKFVDWIDRT 802
Cdd:cd00190   160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 576-799 1.13e-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: 284.57  E-value: 1.13e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  576 RIVGGCVAKAHSWPWQISLRTNSGIHFCGGTLIHPQWVLTAAHCLeRSRRPSSYMVILGSHReRSLETSAQQRALEKLVL 655
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  656 GPN------GADIALLKLQRPAVINDKVLPACLPEKDYVVPSGTECYVTGW--GETQGTGGEGVLKETGFPVIENKICNR 727
Cdd:smart00020  79 HPNynpstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWgrTSEGAGSLPDTLQEVNVPIVSNATCRR 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129957214  728 PSYLNGRVKDHEMCAGNIDGGTDSCQGDSGGPLVCHaHNKFILQGVTSWGLGCANAMKPGVYARVSKFVDWI 799
Cdd:smart00020 159 AYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN-DGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
577-799 1.28e-68

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 225.78  E-value: 1.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 577 IVGGCVAKAHSWPWQISLRTNSGIHFCGGTLIHPQWVLTAAHCLersRRPSSYMVILGSHRERSLETSAQQRALEKLVLG 656
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 657 PN------GADIALLKLQRPAVINDKVLPACLPEKDYVVPSGTECYVTGWGETQGTGGEGVLKETGFPVIENKICNrpSY 730
Cdd:pfam00089  78 PNynpdtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCR--SA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 731 LNGRVKDHEMCAGniDGGTDSCQGDSGGPLVCHAHnkfILQGVTSWGLGCANAMKPGVYARVSKFVDWI 799
Cdd:pfam00089 156 YGGTVTDTMICAG--AGGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 576-806 3.97e-58

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 199.11  E-value: 3.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 576 RIVGGCVAKAHSWPWQISLRTNSGI--HFCGGTLIHPQWVLTAAHCLErSRRPSSYMVILGSHRERSleTSAQQRALEKL 653
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCVD-GDGPSDLRVVIGSTDLST--SGGTVVKVARI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 654 VLGPN------GADIALLKLQRPAvinDKVLPACLPEKDYVVPSGTECYVTGW--GETQGTGGEGVLKETGFPVIENKIC 725
Cdd:COG5640   107 VVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWgrTSEGPGSQSGTLRKADVPVVSDATC 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 726 NRPSYLNGrvkDHEMCAGNIDGGTDSCQGDSGGPLVCHAHNKFILQGVTSWGLGCANAMKPGVYARVSKFVDWIDRTIKA 805
Cdd:COG5640   184 AAYGGFDG---GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260


                  .
gi 1129957214 806 N 806
Cdd:COG5640   261 L 261
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 186-267 2.87e-37

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 134.05  E-value: 2.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  186 EDCIHCNGEDYRGKVSITESGVACQRWDSQEPHNHGYNPNTLPQKYLENNYCRNPDGDPK-PWCFTTNPNKRWEFCSIPR 264
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1129957214  265 CTS 267
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 104-184 6.14e-37

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 133.28  E-value: 6.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  104 ECVNGIGKNYRGTKSRTKSGKTCQRWNAKFPHKPNFTPDNEPKADLESNFCRNPDDDAGGPWCYTTDPDTRWEHCNVPSC 183
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQC 81


                   .
gi 1129957214  184 T 184
Cdd:smart00130  82 E 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 104-183 1.86e-36

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 131.73  E-value: 1.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 104 ECVNGIGKNYRGTKSRTKSGKTCQRWNAKFPHKPNFTPDNEPKADLESNFCRNPDDDAGGPWCYTTDPDTRWEHCNVPSC 183
Cdd:cd00108     3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 277-357 9.79e-36

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 129.82  E-value: 9.79e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  277 TCATGEGSAYRGTIAVTESGKTCQSWSTQSPHQHNRSPENYACKGLDNNYCRNPDN-ERKPWCYTTDPDTRWEYCSVPTC 355
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 1129957214  356 GD 357
Cdd:smart00130  82 EE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 186-265 9.97e-36

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 129.81  E-value: 9.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 186 EDCIHCNGEDYRGKVSITESGVACQRWDSQEPHNHGYNPNTLPQKYLENNYCRNPDGDPK-PWCFTTNPNKRWEFCSIPR 264
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEgPWCYTTDPNVRWEYCDIPR 81


                  .
gi 1129957214 265 C 265
Cdd:cd00108    82 C 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 188-265 1.43e-35

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 128.96  E-value: 1.43e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 188 CIHCNGEDYRGKVSITESGVACQRWDSQEPHNHG-YNPNTLPQKYLENNYCRNPDGDPKPWCFTTNPNKRWEFCSIPRC 265
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 275-355 5.27e-35

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 127.49  E-value: 5.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 275 ETTCATGEGSAYRGTIAVTESGKTCQSWSTQSPHQHNRSPENYACKGLDNNYCRNPDNE-RKPWCYTTDPDTRWEYCSVP 353
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIP 80


                  ..
gi 1129957214 354 TC 355
Cdd:cd00108    81 RC 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 278-355 1.78e-34

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 125.88  E-value: 1.78e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 278 CATGEGSAYRGTIAVTESGKTCQSWSTQSPHQHNR-SPENYACKGLDNNYCRNPDNERKPWCYTTDPDTRWEYCSVPTC 355
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 373-450 5.95e-34

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 124.34  E-value: 5.95e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 373 CYEGDGSSYRGVTSETISGKKCQAWASMSPHRHGK-TPQQYPTADLRRNLCRNPDGDRAPWCYTTDPSVRWEFCNLEKC 450
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 372-452 4.78e-33

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.11  E-value: 4.78e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  372 DCYEGDGSSYRGVTSETISGKKCQAWASMSPHRHGKTPQQYPTADLRRNLCRNPDGD-RAPWCYTTDPSVRWEFCNLEKC 450
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDsEGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 1129957214  451 SS 452
Cdd:smart00130  82 EE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 477-560 4.83e-33

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.11  E-value: 4.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214  477 RDCKVGNGANYRGSTSITIMGVTCQAWSAQSPHQHnSFTPESHPDKGLDGNSCRNPDNDVNGPWCYTTDRNKKWDYCQIP 556
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLH-RFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 1129957214  557 DCAG 560
Cdd:smart00130  80 QCEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 477-559 1.46e-31

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 117.86  E-value: 1.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 477 RDCKVGNGANYRGSTSITIMGVTCQAWSAQSPHQHNsFTPESHPDKGLDGNSCRNPDNDVNGPWCYTTDRNKKWDYCQIP 556
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHK-FNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1129957214 557 DCA 559
Cdd:cd00108    81 RCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 370-451 1.82e-30

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 114.78  E-value: 1.82e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 370 EDDCYEGDGSSYRGVTSETISGKKCQAWASMSPHRHGKTPQQYPTADLRRNLCRNPDGD-RAPWCYTTDPSVRWEFCNLE 448
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1129957214 449 KCS 451
Cdd:cd00108    81 RCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 105-183 2.53e-30

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 114.33  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 105 CVNGIGKNYRGTKSRTKSGKTCQRWNAKFPHKPNF-TPDNEPKADLESNFCRNPDDDAgGPWCYTTDPDTRWEHCNVPSC 183
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 479-558 2.71e-30

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 113.94  E-value: 2.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 479 CKVGNGANYRGSTSITIMGVTCQAWSAQSPHQHNSFTPESHPDKGLDGNSCRNPDNDVNgPWCYTTDRNKKWDYCQIPDC 558
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 40-98 3.05e-09

Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen/hepatocyte growth factor proteins, and various proteins found in Bilateria, such as leech anti-platelet proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238532  Cd Length: 80  Bit Score: 54.40  E-value: 3.05e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1129957214  40 KRMYSTNTVEECAAKCDAETSFTCRSFMYVEKDQECWTAGANSKTETV--LRRTSAALYEK 98
Cdd:cd01099    19 KTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVklLYDSNVDYYEN 79
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 594-805 2.35e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 54.68  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 594 LRTNSGIHFCGGTLIHPQWVLTAAHCL---ERSRRPSSYMVILGSHRERSLETSAQQ-RALEKLVLGPN-GADIALLKLQ 668
Cdd:COG3591     5 LETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYGTATATRfRVPPGWVASGDaGYDYALLRLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 669 RPavINDKVLPACLPEKDyVVPSGTECYVtgwgetqgtggegvlkeTGFPvienkiCNRPSYL----NGRVKDHEmcAGN 744
Cdd:COG3591    85 EP--LGDTTGWLGLAFND-APLAGEPVTI-----------------IGYP------GDRPKDLsldcSGRVTGVQ--GNR 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1129957214 745 IDGGTDSCQGDSGGPLVCHAHNKFILQGVTSWGL-GCANAmkpGVYARvSKFVDWIDRTIKA 805
Cdd:COG3591   137 LSYDCDTTGGSSGSPVLDDSDGGGRVVGVHSAGGaDRANT---GVRLT-SAIVAALRAWASA 194
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 588-699 1.23e-06

Domain of unknown function (DUF1986); This domain is found in serine proteases and is predicted to contain disulphide bonds.


Pssm-ID: 286432  Cd Length: 116  Bit Score: 47.93  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 588 WPWQISLRTNsGIHFCGGTLIHPQWVLTAAHCLERSRRPSSYM-VILGSHRE-RSLETSAQQRALEKLVLGPNGADIALL 665
Cdd:pfam09342   1 WPWIAKVYLD-GNMICSGVLIDASWVIVSGSCLRDTNLRHQYIsVVLGGAKTlKSIEGPYEQIVRVDCRHDIPESEISLL 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1129957214 666 KLQRPAVINDKVLPACLPEKDYVVPSGTECYVTG 699
Cdd:pfam09342  80 HLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 42-98 1.72e-05

divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans hypothetical ORFs and the extracellular portion of plant receptor-like protein kinases. Predicted to possess protein- and/or carbohydrate-binding functions.


Pssm-ID: 214680  Cd Length: 78  Bit Score: 43.72  E-value: 1.72e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1129957214   42 MYSTNTVEECAAKCdAETSFTCRSFMYVEKDQECWTAGANSKTETVLRRTSAA-LYEK 98
Cdd:smart00473  21 VISVASLEECASKC-LNSNCSCRSFTYNNGTKGCLLWSESSLGDARLFPSGGVdLYEK 77
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 26-99 3.35e-04

PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some members of the family there is an additional fourth disulphide bridge the links the N and C termini of the domain. The domain is found in diverse proteins, in some they mediate protein-protein interactions, in others they mediate protein-carbohydrate interactions.


Pssm-ID: 459635  Cd Length: 76  Bit Score: 39.84  E-value: 3.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1129957214  26 SYAKTGGAWLTAINKRMYSTNTVEECAAKCDAETSftCRSFMYVEKDQECWTAGANSKTETVLRRTSAA--LYEKQ 99
Cdd:pfam00024   2 DFERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPR--CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKvdYYEKS 75
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 605-761 4.57e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 38.17  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1129957214 605 GTLIHPQ-WVLTAAHCLERSRRPSSYMVILGSHRERSLETsaqqraleKLVLGPNGADIALLKLQRPAViNDKVLPACLP 683
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLADGREYPA--------TVVARDPDLDLALLRVSGDGR-GLPPLPLGDS 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1129957214 684 EKDYVvpsGTECYVTGWGETQGTGGegvlketgfpVIENKICN-RPSYLNGRVKDHEMCAGNIDGGTdscqgdSGGPLV 761
Cdd:pfam13365  74 EPLVG---GERVYAVGYPLGGEKLS----------LSEGIVSGvDEGRDGGDDGRVIQTDAALSPGS------SGGPVF 133
 
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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