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Conserved domains on  [gi|16758216|ref|NP_445943|]
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plasminogen precursor [Rattus norvegicus]

Protein Classification

serine protease( domain architecture ID 10840640)

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 ...
 582-807 1.23e-99

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: 308.44  E-value: 1.23e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 582 VVGGCVANPHSWPWQISLRTRfSGQHFCGGTLISPEWVLTAAHCLEkSSRPEFYKVILGAHEERILGSDVQQIAVTKLVL 661
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYT-GGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 662 EPN------DADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETK-GTPGAGRLKEAQLPVIENKVCNRA 734
Cdd:cd00190  79 HPNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758216 735 EYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWIER 807
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 374-456 3.01e-42

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: 148.31  E-value: 3.01e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    374 QECYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSKTPANFPDAGLEMNYCRNPDNDQRGPWCFTTDPSVRWEYCNLKR 453
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    454 CSE 456
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 273-354 2.63e-40

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: 142.91  E-value: 2.63e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    273 YQCLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDG-ETAPWCYTTDSQLRWEYCEIPS 351
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    352 CGS 354
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 183-262 1.54e-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: 134.83  E-value: 1.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    183 EECMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDG-EPRPWCFTTDPNKRWEYCDIPR 261
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   .
gi 16758216    262 C 262
Cdd:smart00130  81 C 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 101-183 2.63e-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: 2.63e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    101 SECKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHVPKYSPSTHPSEGLEENYCRNPDNDEQGPWCYTTDPDQRYEYCNIPE 180
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    181 CEE 183
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 480-562 6.89e-34

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: 124.42  E-value: 6.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    480 DCMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTMNPRKLYDYCNIPL 559
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHR-FTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    560 CAS 562
Cdd:smart00130  81 CEE 83
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 33-97 1.95e-12

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: 63.26  E-value: 1.95e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758216  33 LHSLTKKQLAAGSIADCLAKCEGETDFICRSFQYHSKEQQCVIMAENSKTSSIIRMRD--VILFEKR 97
Cdd:cd01099  14 LVSEVKTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDsnVDYYENK 80
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 582-807 1.23e-99

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: 308.44  E-value: 1.23e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 582 VVGGCVANPHSWPWQISLRTRfSGQHFCGGTLISPEWVLTAAHCLEkSSRPEFYKVILGAHEERILGSDVQQIAVTKLVL 661
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYT-GGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 662 EPN------DADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETK-GTPGAGRLKEAQLPVIENKVCNRA 734
Cdd:cd00190  79 HPNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758216 735 EYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWIER 807
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 581-805 2.82e-98

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: 304.60  E-value: 2.82e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    581 RVVGGCVANPHSWPWQISLRTRfSGQHFCGGTLISPEWVLTAAHCLEkSSRPEFYKVILGAHEeRILGSDVQQIAVTKLV 660
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG-GGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    661 LEPN------DADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETKGTPGAG--RLKEAQLPVIENKVCN 732
Cdd:smart00020  78 IHPNynpstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758216    733 RAEYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCfEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWI 805
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
582-805 1.70e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 238.88  E-value: 1.70e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   582 VVGGCVANPHSWPWQISLrTRFSGQHFCGGTLISPEWVLTAAHCLEKSSRpefYKVILGAHEERILGSDVQQIAVTKLVL 661
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL-QLSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   662 EPN------DADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETKGTPGAGRLKEAQLPVIENKVCNRAe 735
Cdd:pfam00089  77 HPNynpdtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSA- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   736 yLNNRVKSTELCAGhlAGGIDSCQGDSGGPLVCfeKDKYiLQGVTSWGLGCARPNKPGVYVRVSRYVNWI 805
Cdd:pfam00089 156 -YGGTVTDTMICAG--AGGKDACQGDSGGPLVC--SDGE-LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 581-810 4.63e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 215.28  E-value: 4.63e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 581 RVVGGCVANPHSWPWQISLRTRF-SGQHFCGGTLISPEWVLTAAHCLEKSSrPEFYKVILGAHeeRILGSDVQQIAVTKL 659
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNgPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGST--DLSTSGGTVVKVARI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 660 VLEPN------DADIALLKLSRPATitdNVIPACLPSPNYVVADRTLCYITGWGETKGTPG--AGRLKEAQLPVIENKVC 731
Cdd:COG5640 107 VVHPDydpatpGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsqSGTLRKADVPVVSDATC 183

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216 732 NraeYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWIEREMR 810
Cdd:COG5640 184 A---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 374-456 3.01e-42

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: 148.31  E-value: 3.01e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    374 QECYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSKTPANFPDAGLEMNYCRNPDNDQRGPWCFTTDPSVRWEYCNLKR 453
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    454 CSE 456
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 273-354 2.63e-40

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: 142.91  E-value: 2.63e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    273 YQCLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDG-ETAPWCYTTDSQLRWEYCEIPS 351
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    352 CGS 354
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 275-352 4.48e-39

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: 138.98  E-value: 4.48e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216   275 CLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNR-TPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSC 352
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 273-352 5.56e-39

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: 139.05  E-value: 5.56e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 273 YQCLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGE-TAPWCYTTDSQLRWEYCEIPS 351
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIPR 81


                .
gi 16758216 352 C 352
Cdd:cd00108  82 C 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 374-455 2.00e-38

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: 137.51  E-value: 2.00e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 374 QECYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSKTPANFPDAGLEMNYCRNPDNDQRGPWCFTTDPSVRWEYCNLKR 453
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                ..
gi 16758216 454 CS 455
Cdd:cd00108  82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 183-262 1.54e-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: 134.83  E-value: 1.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    183 EECMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDG-EPRPWCFTTDPNKRWEYCDIPR 261
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   .
gi 16758216    262 C 262
Cdd:smart00130  81 C 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 101-183 2.63e-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: 2.63e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    101 SECKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHVPKYSPSTHPSEGLEENYCRNPDNDEQGPWCYTTDPDQRYEYCNIPE 180
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    181 CEE 183
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 376-454 3.01e-36

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: 130.89  E-value: 3.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   376 CYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSK-TPANFPDAGLEMNYCRNPDNDQRgPWCFTTDPSVRWEYCNLKRC 454
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 102-182 4.85e-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: 130.58  E-value: 4.85e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 102 ECKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHVPKYSPSTHPSEGLEENYCRNPDNDEQGPWCYTTDPDQRYEYCNIPEC 181
Cdd:cd00108   3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82


                .
gi 16758216 182 E 182
Cdd:cd00108  83 E 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 185-262 1.07e-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: 129.35  E-value: 1.07e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216   185 CMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHG-YIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPNKRWEYCDIPRC 262
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 182-262 7.48e-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: 127.11  E-value: 7.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 182 EEECMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEP-RPWCFTTDPNKRWEYCDIP 260
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                ..
gi 16758216 261 RC 262
Cdd:cd00108  81 RC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 480-562 6.89e-34

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: 124.42  E-value: 6.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    480 DCMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTMNPRKLYDYCNIPL 559
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHR-FTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    560 CAS 562
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 481-560 1.53e-32

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: 120.49  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   481 CMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRIFTPQTNPRAGLEKNYCRNPDGDVNgPWCYTMNPRKLYDYCNIPLC 560
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 478-561 1.81e-32

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: 120.56  E-value: 1.81e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 478 ETDCMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTMNPRKLYDYCNI 557
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHK-FNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDI 79


                ....
gi 16758216 558 PLCA 561
Cdd:cd00108  80 PRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 103-181 6.22e-32

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: 118.95  E-value: 6.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   103 CKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHV-PKYSPSTHPSEGLEENYCRNPDNDEqGPWCYTTDPDQRYEYCNIPEC 181
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRhSKYTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 33-97 1.95e-12

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: 63.26  E-value: 1.95e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758216  33 LHSLTKKQLAAGSIADCLAKCEGETDFICRSFQYHSKEQQCVIMAENSKTSSIIRMRD--VILFEKR 97
Cdd:cd01099  14 LVSEVKTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDsnVDYYENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 20-97 6.48e-11

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: 59.13  E-value: 6.48e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216     20 DSLDGYVSTQGASLHSLTKKQLAAGSIADCLAKCEgETDFICRSFQYHSKEQQCVIMAENSKTSS-IIRMRDVILFEKR 97
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSRIVISVASLEECASKCL-NSNCSCRSFTYNNGTKGCLLWSESSLGDArLFPSGGVDLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 25-97 4.63e-10

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: 56.41  E-value: 4.63e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758216    25 YVSTQGASLHSLTKKQLAAGSIADCLAKCEGETDfiCRSFQYHSKEQQCVIMAENSKT-SSIIRMRD-VILFEKR 97
Cdd:pfam00024   3 FERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPR--CRSFTYNPKSKKCHLKSSSSGSlPRLKRSDNkVDYYEKS 75
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 582-807 1.23e-99

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: 308.44  E-value: 1.23e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 582 VVGGCVANPHSWPWQISLRTRfSGQHFCGGTLISPEWVLTAAHCLEkSSRPEFYKVILGAHEERILGSDVQQIAVTKLVL 661
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQYT-GGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 662 EPN------DADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETK-GTPGAGRLKEAQLPVIENKVCNRA 734
Cdd:cd00190  79 HPNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSeGGPLPDVLQEVNVPIVSNAECKRA 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758216 735 EYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWIER 807
Cdd:cd00190 159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 581-805 2.82e-98

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: 304.60  E-value: 2.82e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    581 RVVGGCVANPHSWPWQISLRTRfSGQHFCGGTLISPEWVLTAAHCLEkSSRPEFYKVILGAHEeRILGSDVQQIAVTKLV 660
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG-GGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    661 LEPN------DADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETKGTPGAG--RLKEAQLPVIENKVCN 732
Cdd:smart00020  78 IHPNynpstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16758216    733 RAEYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCfEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWI 805
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
582-805 1.70e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 238.88  E-value: 1.70e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   582 VVGGCVANPHSWPWQISLrTRFSGQHFCGGTLISPEWVLTAAHCLEKSSRpefYKVILGAHEERILGSDVQQIAVTKLVL 661
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL-QLSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   662 EPN------DADIALLKLSRPATITDNVIPACLPSPNYVVADRTLCYITGWGETKGTPGAGRLKEAQLPVIENKVCNRAe 735
Cdd:pfam00089  77 HPNynpdtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSA- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   736 yLNNRVKSTELCAGhlAGGIDSCQGDSGGPLVCfeKDKYiLQGVTSWGLGCARPNKPGVYVRVSRYVNWI 805
Cdd:pfam00089 156 -YGGTVTDTMICAG--AGGKDACQGDSGGPLVC--SDGE-LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 581-810 4.63e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 215.28  E-value: 4.63e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 581 RVVGGCVANPHSWPWQISLRTRF-SGQHFCGGTLISPEWVLTAAHCLEKSSrPEFYKVILGAHeeRILGSDVQQIAVTKL 659
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNgPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGST--DLSTSGGTVVKVARI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 660 VLEPN------DADIALLKLSRPATitdNVIPACLPSPNYVVADRTLCYITGWGETKGTPG--AGRLKEAQLPVIENKVC 731
Cdd:COG5640 107 VVHPDydpatpGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsqSGTLRKADVPVVSDATC 183

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216 732 NraeYLNNRVKSTELCAGHLAGGIDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRYVNWIEREMR 810
Cdd:COG5640 184 A---AYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAG 259
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 374-456 3.01e-42

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: 148.31  E-value: 3.01e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    374 QECYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSKTPANFPDAGLEMNYCRNPDNDQRGPWCFTTDPSVRWEYCNLKR 453
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    454 CSE 456
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 273-354 2.63e-40

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: 142.91  E-value: 2.63e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    273 YQCLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDG-ETAPWCYTTDSQLRWEYCEIPS 351
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    352 CGS 354
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 275-352 4.48e-39

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: 138.98  E-value: 4.48e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216   275 CLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNR-TPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSC 352
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 273-352 5.56e-39

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: 139.05  E-value: 5.56e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 273 YQCLKGRGENYRGTVSVTASGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGE-TAPWCYTTDSQLRWEYCEIPS 351
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIPR 81


                .
gi 16758216 352 C 352
Cdd:cd00108  82 C 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 374-455 2.00e-38

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: 137.51  E-value: 2.00e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 374 QECYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSKTPANFPDAGLEMNYCRNPDNDQRGPWCFTTDPSVRWEYCNLKR 453
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                ..
gi 16758216 454 CS 455
Cdd:cd00108  82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 183-262 1.54e-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: 134.83  E-value: 1.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    183 EECMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDG-EPRPWCFTTDPNKRWEYCDIPR 261
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   .
gi 16758216    262 C 262
Cdd:smart00130  81 C 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 101-183 2.63e-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: 2.63e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    101 SECKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHVPKYSPSTHPSEGLEENYCRNPDNDEQGPWCYTTDPDQRYEYCNIPE 180
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    181 CEE 183
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 376-454 3.01e-36

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: 130.89  E-value: 3.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   376 CYQGNGKSYRGTSSTTNTGKKCQSWVSMTPHSHSK-TPANFPDAGLEMNYCRNPDNDQRgPWCFTTDPSVRWEYCNLKRC 454
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 102-182 4.85e-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: 130.58  E-value: 4.85e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 102 ECKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHVPKYSPSTHPSEGLEENYCRNPDNDEQGPWCYTTDPDQRYEYCNIPEC 181
Cdd:cd00108   3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82


                .
gi 16758216 182 E 182
Cdd:cd00108  83 E 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 185-262 1.07e-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: 129.35  E-value: 1.07e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216   185 CMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHG-YIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPNKRWEYCDIPRC 262
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 182-262 7.48e-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: 127.11  E-value: 7.48e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 182 EEECMYCSGEKYEGKISKTMSGLDCQSWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEP-RPWCFTTDPNKRWEYCDIP 260
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                ..
gi 16758216 261 RC 262
Cdd:cd00108  81 RC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 480-562 6.89e-34

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: 124.42  E-value: 6.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216    480 DCMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTMNPRKLYDYCNIPL 559
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHR-FTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 16758216    560 CAS 562
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 481-560 1.53e-32

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: 120.49  E-value: 1.53e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   481 CMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRIFTPQTNPRAGLEKNYCRNPDGDVNgPWCYTMNPRKLYDYCNIPLC 560
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 478-561 1.81e-32

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: 120.56  E-value: 1.81e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 478 ETDCMYGNGKEYRGKTAVTAAGTPCQEWAAQEPHSHRiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTMNPRKLYDYCNI 557
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHK-FNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDI 79


                ....
gi 16758216 558 PLCA 561
Cdd:cd00108  80 PRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 103-181 6.22e-32

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: 118.95  E-value: 6.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   103 CKTGIGKGYRGTMSKTKTGVTCQKWSDTSPHV-PKYSPSTHPSEGLEENYCRNPDNDEqGPWCYTTDPDQRYEYCNIPEC 181
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRhSKYTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 33-97 1.95e-12

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: 63.26  E-value: 1.95e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16758216  33 LHSLTKKQLAAGSIADCLAKCEGETDFICRSFQYHSKEQQCVIMAENSKTSSIIRMRD--VILFEKR 97
Cdd:cd01099  14 LVSEVKTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDsnVDYYENK 80
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 604-811 3.98e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 65.85  E-value: 3.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 604 SGQHFCGGTLISPEWVLTAAHCL---EKSSRPEFYKVILGAHEERILGSDVQQIAVTKLVLEPNDA--DIALLKLSRPat 678
Cdd:COG3591   9 GGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYGTATATRFRVPPGWVASGDAgyDYALLRLDEP-- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216 679 ITDNVIPACLPSPNYVVADRTLcYITGWGetkgtpgAGRLKEAQLpvienkvcnraeYLNNRVKSTElcAGHLAGGIDSC 758
Cdd:COG3591  87 LGDTTGWLGLAFNDAPLAGEPV-TIIGYP-------GDRPKDLSL------------DCSGRVTGVQ--GNRLSYDCDTT 144

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16758216 759 QGDSGGPLVCFEKDKYILQGVTSWGlGCARPNKpGVYVRvSRYVNWIEREMRN 811
Cdd:COG3591 145 GGSSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVRLT-SAIVAALRAWASA 194
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 20-97 6.48e-11

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: 59.13  E-value: 6.48e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216     20 DSLDGYVSTQGASLHSLTKKQLAAGSIADCLAKCEgETDFICRSFQYHSKEQQCVIMAENSKTSS-IIRMRDVILFEKR 97
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSRIVISVASLEECASKCL-NSNCSCRSFTYNNGTKGCLLWSESSLGDArLFPSGGVDLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 25-97 4.63e-10

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: 56.41  E-value: 4.63e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16758216    25 YVSTQGASLHSLTKKQLAAGSIADCLAKCEGETDfiCRSFQYHSKEQQCVIMAENSKT-SSIIRMRD-VILFEKR 97
Cdd:pfam00024   3 FERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPR--CRSFTYNPKSKKCHLKSSSSGSlPRLKRSDNkVDYYEKS 75
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 611-767 9.08e-06

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 46.26  E-value: 9.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   611 GTLISPE-WVLTAAHCLEKSSRPEFYKVILGAHEERILgsdvqqiaVTKLVLEPNDADIALLKLSRPATItdnvIPACLP 689
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLADGREY--------PATVVARDPDLDLALLRVSGDGRG----LPPLPL 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16758216   690 SPNYVVADRTLCYITGWgetkgtPGAGRLKEaqlpVIENKVCNRAEYLNNRVKSTEL-CAGHLAGgidscqGDSGGPLV 767
Cdd:pfam13365  71 GDSEPLVGGERVYAVGY------PLGGEKLS----LSEGIVSGVDEGRDGGDDGRVIqTDAALSP------GSSGGPVF 133
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 593-690 5.64e-05

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: 43.31  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16758216   593 WPWQISLRtrFSGQHFCGGTLISPEWVLTAAHCLEKSS-RPEFYKVILGAHEE-RILGSDVQQIAVTKLVLEPNDADIAL 670
Cdd:pfam09342   1 WPWIAKVY--LDGNMICSGVLIDASWVIVSGSCLRDTNlRHQYISVVLGGAKTlKSIEGPYEQIVRVDCRHDIPESEISL 78

                          90       100
                  ....*....|....*....|
gi 16758216   671 LKLSRPATITDNVIPACLPS 690
Cdd:pfam09342  79 LHLASPASFSNHVLPTFVPE 98
 
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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