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Conserved domains on  [gi|116292750|ref|NP_005568|]
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apolipoprotein(a) precursor [Homo sapiens]

Protein Classification

serine protease( domain architecture ID 11079397)

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 ...
 1820-2034 3.23e-88

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: 287.25  E-value: 3.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1820 IVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLKkSSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLE 1899
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1900 P------TQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFG-TGLLKEAQLLVIENEVCN-HY 1971
Cdd:cd00190    80 PnynpstYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKrAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292750 1972 KY--------ICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIE 2034
Cdd:cd00190   160 SYggtitdnmLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1614-1695 1.84e-38

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: 138.68  E-value: 1.84e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1614 RQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDAD-TGPWCFTMDPSIRWEYCNLTR 1692
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDsEGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1693 CSD 1695
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1386-1466 2.61e-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: 132.51  E-value: 2.61e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1386 QDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTR 1464
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1465 CP 1466
Cdd:smart00130   81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 28-105 7.26e-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: 131.28  E-value: 7.26e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750    28 CYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNR-TTENYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 105
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1500-1581 9.67e-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: 130.97  E-value: 9.67e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1500 QDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPDSGK-QPWCYTTDPCVRWEYCNLTQ 1578
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1579 CSE 1581
Cdd:smart00130   81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 712-789 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   712 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 789
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 598-675 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   598 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 675
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 484-561 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   484 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 561
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 370-447 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   370 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 447
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 256-333 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   256 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 333
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 142-219 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   142 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 219
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 826-903 2.28e-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: 129.73  E-value: 2.28e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   826 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDPVAAPYCYTRDPSVRWEYCNLTQC 903
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1054-1131 2.35e-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: 129.73  E-value: 2.35e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1054 CYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSR-TPENYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQC 1131
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1272-1352 2.18e-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: 127.12  E-value: 2.18e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1272 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1350
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1351 CP 1352
Cdd:smart00130   81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1720-1799 2.40e-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: 126.65  E-value: 2.40e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1720 CMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHSTFIPGTNKWAGLEKNYCRNPDGDINgPWCYTMNPRKLFDYCDIPLC 1799
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1166-1246 2.84e-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: 126.74  E-value: 2.84e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1166 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEIS-PWCYTMDPNVRWEYCNLTQ 1244
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1245 CP 1246
Cdd:smart00130   81 CE 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 938-1019 9.56e-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: 125.20  E-value: 9.56e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    938 QECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPD-PVAAPWCYTTDPSVRWEYCNLTR 1016
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDgDSEGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1017 CSD 1019
Cdd:smart00130   81 CEE 83
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1820-2034 3.23e-88

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: 287.25  E-value: 3.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1820 IVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLKkSSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLE 1899
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1900 P------TQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFG-TGLLKEAQLLVIENEVCN-HY 1971
Cdd:cd00190    80 PnynpstYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKrAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292750 1972 KY--------ICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIE 2034
Cdd:cd00190   160 SYggtitdnmLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1820-2033 2.95e-85

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: 278.79  E-value: 2.95e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1820 IVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLkKSSRPSSYKVILGAHQeVNLESHVQEIEVSRLFLE 1899
Cdd:smart00020    2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIH 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1900 P------TQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFGTG--LLKEAQLLVIENEVCNHY 1971
Cdd:smart00020   80 PnynpstYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNATCRRA 159

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292750   1972 KY---------ICAEHLARGTDSCQGDSGGPLVCfEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWI 2033
Cdd:smart00020  160 YSgggaitdnmLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1820-2033 2.60e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 223.86  E-value: 2.60e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1820 IVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLkksSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLE 1899
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1900 P------TQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGeTQGTFGT-GLLKEAQLLVIENEVCNHYK 1972
Cdd:pfam00089   78 PnynpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPsDTLQEVTVPVVSRETCRSAY 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292750  1973 -------YICAEhlARGTDSCQGDSGGPLVCfeKDKYiLQGVTSWGLGCARPNKPGVYARVSRFVTWI 2033
Cdd:pfam00089  157 ggtvtdtMICAG--AGGKDACQGDSGGPLVC--SDGE-LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 1820-2040 1.90e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 191.40  E-value: 1.90e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1820 IVGGCVAHPHSWPWQVSLRTRFGK--HFCGGTLISPEWVLTAAHCLKKSSrPSSYKVILGAHqevNLESHV-QEIEVSRL 1896
Cdd:COG5640    31 IVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGST---DLSTSGgTVVKVARI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1897 FLEP------TQADIALLKLSRPAvitDKVMPACLPSPDYMVTARTECYITGWGETQGTFGT--GLLKEAQLLVIENEVC 1968
Cdd:COG5640   107 VVHPdydpatPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqsGTLRKADVPVVSDATC 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292750 1969 NHYK------YICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIEGMMRNN 2040
Cdd:COG5640   184 AAYGgfdggtMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1614-1695 1.84e-38

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: 138.68  E-value: 1.84e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1614 RQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDAD-TGPWCFTMDPSIRWEYCNLTR 1692
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDsEGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1693 CSD 1695
Cdd:smart00130   81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1616-1693 1.96e-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: 132.82  E-value: 1.96e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1616 CYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQR-TPENYPNDGLTMNYCRNPDADTGPWCFTMDPSIRWEYCNLTRC 1693
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1386-1466 2.61e-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: 132.51  E-value: 2.61e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1386 QDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTR 1464
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1465 CP 1466
Cdd:smart00130   81 CE 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1614-1694 6.61e-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: 131.35  E-value: 6.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1614 RQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDAD-TGPWCFTMDPSIRWEYCNLTR 1692
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1693 CS 1694
Cdd:cd00108    82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 28-105 7.26e-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: 131.28  E-value: 7.26e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750    28 CYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNR-TTENYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 105
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1500-1581 9.67e-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: 130.97  E-value: 9.67e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1500 QDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPDSGK-QPWCYTTDPCVRWEYCNLTQ 1578
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1579 CSE 1581
Cdd:smart00130   81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 712-789 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   712 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 789
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 598-675 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   598 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 675
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 484-561 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   484 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 561
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 370-447 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   370 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 447
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 256-333 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   256 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 333
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 142-219 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   142 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 219
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 826-903 2.28e-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: 129.73  E-value: 2.28e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   826 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDPVAAPYCYTRDPSVRWEYCNLTQC 903
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1054-1131 2.35e-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: 129.73  E-value: 2.35e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1054 CYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSR-TPENYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQC 1131
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 140-221 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    140 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 218
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    219 CSD 221
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 710-791 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    710 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 788
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    789 CSD 791
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 596-677 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    596 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 674
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    675 CSD 677
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 482-563 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    482 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 560
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    561 CSD 563
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 368-449 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    368 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 446
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    447 CSD 449
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 254-335 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    254 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 332
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    333 CSD 335
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1052-1131 6.62e-35

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: 128.66  E-value: 6.62e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1052 QDCYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSRTPENYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1130
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    .
gi 116292750   1131 C 1131
Cdd:smart00130   81 C 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 26-107 9.48e-35

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: 128.28  E-value: 9.48e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750     26 QDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 104
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    105 CSD 107
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 824-905 1.68e-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: 127.51  E-value: 1.68e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    824 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPD-PVAAPYCYTRDPSVRWEYCNLTQ 902
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDgDSEGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    903 CSD 905
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1272-1352 2.18e-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: 127.12  E-value: 2.18e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1272 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1350
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1351 CP 1352
Cdd:smart00130   81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1720-1799 2.40e-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: 126.65  E-value: 2.40e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1720 CMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHSTFIPGTNKWAGLEKNYCRNPDGDINgPWCYTMNPRKLFDYCDIPLC 1799
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1166-1246 2.84e-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: 126.74  E-value: 2.84e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1166 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEIS-PWCYTMDPNVRWEYCNLTQ 1244
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1245 CP 1246
Cdd:smart00130   81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1388-1465 8.73e-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: 125.11  E-value: 8.73e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1388 CYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRI-PLYYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTRC 1465
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYtPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 938-1019 9.56e-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: 125.20  E-value: 9.56e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    938 QECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPD-PVAAPWCYTTDPSVRWEYCNLTR 1016
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDgDSEGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1017 CSD 1019
Cdd:smart00130   81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1500-1580 1.83e-33

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: 124.41  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1500 QDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPD-SGKQPWCYTTDPCVRWEYCNLTQ 1578
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDgDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1579 CS 1580
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1386-1466 1.94e-33

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: 124.41  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1386 QDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTR 1464
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1465 CP 1466
Cdd:cd00108    82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1502-1579 2.13e-33

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: 123.96  E-value: 2.13e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1502 CYHGDGRSYRGISSTTVTGRTCQSWSSMIPH-WHQRTPENYPNAGLTENYCRNPDSGKQPWCYTTDPCVRWEYCNLTQC 1579
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHrHSKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 940-1017 3.27e-33

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: 123.57  E-value: 3.27e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   940 CYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSR-TPAYYPNAGLIKNYCRNPDPVAAPWCYTTDPSVRWEYCNLTRC 1017
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1052-1131 4.89e-33

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: 123.26  E-value: 4.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1052 QDCYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSRTPENYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1130
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                  .
gi 116292750 1131 C 1131
Cdd:cd00108    82 C 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1272-1352 5.49e-33

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: 123.26  E-value: 5.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1272 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1350
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1351 CP 1352
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1166-1246 6.23e-33

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: 122.87  E-value: 6.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1166 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEI-SPWCYTMDPNVRWEYCNLTQ 1244
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1245 CP 1246
Cdd:cd00108    82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1718-1801 8.85e-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: 122.50  E-value: 8.85e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1718 QDCMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHStFIPGTNKWAGLEKNYCRNPDGDINGPWCYTMNPRKLFDYCDIP 1797
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHR-FTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                    ....
gi 116292750   1798 LCAS 1801
Cdd:smart00130   80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1274-1351 1.30e-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: 122.03  E-value: 1.30e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1274 CYHGDGQSYRGSFSTTVTGRTCQSWSSMTPH-WHQRTTEYYPNGGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQC 1351
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHrHSKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 140-220 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  140 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 218
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  219 CS 220
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 254-334 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  254 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 332
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  333 CS 334
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 368-448 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  368 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 446
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  447 CS 448
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 482-562 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  482 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 560
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  561 CS 562
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 596-676 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  596 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 674
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  675 CS 676
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 710-790 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  710 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 788
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  789 CS 790
Cdd:cd00108    82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1168-1245 7.92e-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: 119.72  E-value: 7.92e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1168 CYHGDGQSYRGSFSTTVTGRTCQSWSSMTPH-WHQRTTEYYPNGGLTRNYCRNPDAEISPWCYTMDPNVRWEYCNLTQC 1245
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHrHSKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1717-1800 9.83e-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: 119.41  E-value: 9.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1717 EQDCMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHsTFIPGTNKWAGLEKNYCRNPDGDINGPWCYTMNPRKLFDYCDI 1796
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQH-KFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDI 79


                  ....
gi 116292750 1797 PLCA 1800
Cdd:cd00108    80 PRCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 26-106 1.55e-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: 119.02  E-value: 1.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   26 QDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 104
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  105 CS 106
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 824-904 2.12e-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: 118.63  E-value: 2.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  824 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPD-PVAAPYCYTRDPSVRWEYCNLTQ 902
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDgDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  903 CS 904
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 938-1018 8.50e-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: 116.71  E-value: 8.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  938 QECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPD-PVAAPWCYTTDPSVRWEYCNLTR 1016
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDgDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1017 CS 1018
Cdd:cd00108    82 CE 83
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 1820-2034 3.23e-88

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: 287.25  E-value: 3.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1820 IVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLKkSSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLE 1899
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1900 P------TQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFG-TGLLKEAQLLVIENEVCN-HY 1971
Cdd:cd00190    80 PnynpstYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKrAY 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292750 1972 KY--------ICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIE 2034
Cdd:cd00190   160 SYggtitdnmLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 1820-2033 2.95e-85

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: 278.79  E-value: 2.95e-85
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1820 IVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLkKSSRPSSYKVILGAHQeVNLESHVQEIEVSRLFLE 1899
Cdd:smart00020    2 IVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVIIH 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1900 P------TQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGETQGTFGTG--LLKEAQLLVIENEVCNHY 1971
Cdd:smart00020   80 PnynpstYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNATCRRA 159

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292750   1972 KY---------ICAEHLARGTDSCQGDSGGPLVCfEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWI 2033
Cdd:smart00020  160 YSgggaitdnmLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
1820-2033 2.60e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 223.86  E-value: 2.60e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1820 IVGGCVAHPHSWPWQVSLRTRFGKHFCGGTLISPEWVLTAAHCLkksSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLE 1899
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1900 P------TQADIALLKLSRPAVITDKVMPACLPSPDYMVTARTECYITGWGeTQGTFGT-GLLKEAQLLVIENEVCNHYK 1972
Cdd:pfam00089   78 PnynpdtLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGPsDTLQEVTVPVVSRETCRSAY 156

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292750  1973 -------YICAEhlARGTDSCQGDSGGPLVCfeKDKYiLQGVTSWGLGCARPNKPGVYARVSRFVTWI 2033
Cdd:pfam00089  157 ggtvtdtMICAG--AGGKDACQGDSGGPLVC--SDGE-LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 1820-2040 1.90e-54

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 191.40  E-value: 1.90e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1820 IVGGCVAHPHSWPWQVSLRTRFGK--HFCGGTLISPEWVLTAAHCLKKSSrPSSYKVILGAHqevNLESHV-QEIEVSRL 1896
Cdd:COG5640    31 IVGGTPATVGEYPWMVALQSSNGPsgQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGST---DLSTSGgTVVKVARI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1897 FLEP------TQADIALLKLSRPAvitDKVMPACLPSPDYMVTARTECYITGWGETQGTFGT--GLLKEAQLLVIENEVC 1968
Cdd:COG5640   107 VVHPdydpatPGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSqsGTLRKADVPVVSDATC 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116292750 1969 NHYK------YICAEHLARGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYARVSRFVTWIEGMMRNN 2040
Cdd:COG5640   184 AAYGgfdggtMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGGL 261
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1614-1695 1.84e-38

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: 138.68  E-value: 1.84e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1614 RQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDAD-TGPWCFTMDPSIRWEYCNLTR 1692
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDsEGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1693 CSD 1695
Cdd:smart00130   81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1616-1693 1.96e-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: 132.82  E-value: 1.96e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1616 CYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQR-TPENYPNDGLTMNYCRNPDADTGPWCFTMDPSIRWEYCNLTRC 1693
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1386-1466 2.61e-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: 132.51  E-value: 2.61e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1386 QDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTR 1464
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1465 CP 1466
Cdd:smart00130   81 CE 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1614-1694 6.61e-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: 131.35  E-value: 6.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1614 RQCYHGNGQSYRGTFSTTVTGRTCQSWSSMTPHRHQRTPENYPNDGLTMNYCRNPDAD-TGPWCFTMDPSIRWEYCNLTR 1692
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1693 CS 1694
Cdd:cd00108    82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 28-105 7.26e-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: 131.28  E-value: 7.26e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750    28 CYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNR-TTENYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 105
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1500-1581 9.67e-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: 130.97  E-value: 9.67e-36
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1500 QDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPDSGK-QPWCYTTDPCVRWEYCNLTQ 1578
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1579 CSE 1581
Cdd:smart00130   81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 712-789 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   712 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 789
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 598-675 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   598 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 675
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 484-561 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   484 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 561
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 370-447 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   370 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 447
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 256-333 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   256 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 333
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 142-219 9.91e-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: 9.91e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   142 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDAVAAPYCYTRDPGVRWEYCNLTQC 219
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 826-903 2.28e-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: 129.73  E-value: 2.28e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   826 CYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSR-TPEYYPNAGLIMNYCRNPDPVAAPYCYTRDPSVRWEYCNLTQC 903
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1054-1131 2.35e-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: 129.73  E-value: 2.35e-35
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1054 CYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSR-TPENYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQC 1131
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 140-221 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    140 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 218
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    219 CSD 221
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 710-791 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    710 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 788
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    789 CSD 791
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 596-677 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    596 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 674
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    675 CSD 677
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 482-563 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    482 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 560
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    561 CSD 563
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 368-449 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    368 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 446
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    447 CSD 449
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 254-335 3.59e-35

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: 129.43  E-value: 3.59e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    254 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 332
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    333 CSD 335
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1052-1131 6.62e-35

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: 128.66  E-value: 6.62e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1052 QDCYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSRTPENYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1130
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    .
gi 116292750   1131 C 1131
Cdd:smart00130   81 C 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 26-107 9.48e-35

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: 128.28  E-value: 9.48e-35
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750     26 QDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDAVAA-PYCYTRDPGVRWEYCNLTQ 104
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    105 CSD 107
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 824-905 1.68e-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: 127.51  E-value: 1.68e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    824 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPD-PVAAPYCYTRDPSVRWEYCNLTQ 902
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDgDSEGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750    903 CSD 905
Cdd:smart00130   81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1272-1352 2.18e-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: 127.12  E-value: 2.18e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1272 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1350
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1351 CP 1352
Cdd:smart00130   81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1720-1799 2.40e-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: 126.65  E-value: 2.40e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1720 CMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHSTFIPGTNKWAGLEKNYCRNPDGDINgPWCYTMNPRKLFDYCDIPLC 1799
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1166-1246 2.84e-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: 126.74  E-value: 2.84e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1166 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEIS-PWCYTMDPNVRWEYCNLTQ 1244
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEgPWCYTTDPNVRWEYCDIPQ 80


                    ..
gi 116292750   1245 CP 1246
Cdd:smart00130   81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1388-1465 8.73e-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: 125.11  E-value: 8.73e-34
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1388 CYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRI-PLYYPNAGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTRC 1465
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYtPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 938-1019 9.56e-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: 125.20  E-value: 9.56e-34
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750    938 QECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPD-PVAAPWCYTTDPSVRWEYCNLTR 1016
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDgDSEGPWCYTTDPNVRWEYCDIPQ 80


                    ...
gi 116292750   1017 CSD 1019
Cdd:smart00130   81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1500-1580 1.83e-33

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: 124.41  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1500 QDCYHGDGRSYRGISSTTVTGRTCQSWSSMIPHWHQRTPENYPNAGLTENYCRNPD-SGKQPWCYTTDPCVRWEYCNLTQ 1578
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDgDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1579 CS 1580
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1386-1466 1.94e-33

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: 124.41  E-value: 1.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1386 QDCYRGDGQSYRGTLSTTITGRTCQSWSSMTPHWHRRIPLYYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTR 1464
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1465 CP 1466
Cdd:cd00108    82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1502-1579 2.13e-33

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: 123.96  E-value: 2.13e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1502 CYHGDGRSYRGISSTTVTGRTCQSWSSMIPH-WHQRTPENYPNAGLTENYCRNPDSGKQPWCYTTDPCVRWEYCNLTQC 1579
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHrHSKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 940-1017 3.27e-33

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: 123.57  E-value: 3.27e-33
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750   940 CYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSR-TPAYYPNAGLIKNYCRNPDPVAAPWCYTTDPSVRWEYCNLTRC 1017
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1052-1131 4.89e-33

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: 123.26  E-value: 4.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1052 QDCYYHYGQSYRGTYSTTVTGRTCQAWSSMTPHQHSRTPENYPNAGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1130
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                  .
gi 116292750 1131 C 1131
Cdd:cd00108    82 C 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1272-1352 5.49e-33

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: 123.26  E-value: 5.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1272 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEI-RPWCYTMDPSVRWEYCNLTQ 1350
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1351 CP 1352
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1166-1246 6.23e-33

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: 122.87  E-value: 6.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1166 QDCYHGDGQSYRGSFSTTVTGRTCQSWSSMTPHWHQRTTEYYPNGGLTRNYCRNPDAEI-SPWCYTMDPNVRWEYCNLTQ 1244
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1245 CP 1246
Cdd:cd00108    82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 1718-1801 8.85e-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: 122.50  E-value: 8.85e-33
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   1718 QDCMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHStFIPGTNKWAGLEKNYCRNPDGDINGPWCYTMNPRKLFDYCDIP 1797
Cdd:smart00130    1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHR-FTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                    ....
gi 116292750   1798 LCAS 1801
Cdd:smart00130   80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1274-1351 1.30e-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: 122.03  E-value: 1.30e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1274 CYHGDGQSYRGSFSTTVTGRTCQSWSSMTPH-WHQRTTEYYPNGGLTRNYCRNPDAEIRPWCYTMDPSVRWEYCNLTQC 1351
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHrHSKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 140-220 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  140 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 218
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  219 CS 220
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 254-334 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  254 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 332
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  333 CS 334
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 368-448 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  368 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 446
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  447 CS 448
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 482-562 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  482 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 560
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  561 CS 562
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 596-676 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  596 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 674
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  675 CS 676
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 710-790 5.76e-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: 120.18  E-value: 5.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  710 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 788
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  789 CS 790
Cdd:cd00108    82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 1168-1245 7.92e-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: 119.72  E-value: 7.92e-32
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116292750  1168 CYHGDGQSYRGSFSTTVTGRTCQSWSSMTPH-WHQRTTEYYPNGGLTRNYCRNPDAEISPWCYTMDPNVRWEYCNLTQC 1245
Cdd:pfam00051    1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHrHSKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 1717-1800 9.83e-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: 119.41  E-value: 9.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1717 EQDCMFGNGKGYRGKKATTVTGTPCQEWAAQEPHRHsTFIPGTNKWAGLEKNYCRNPDGDINGPWCYTMNPRKLFDYCDI 1796
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQH-KFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDI 79


                  ....
gi 116292750 1797 PLCA 1800
Cdd:cd00108    80 PRCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 26-106 1.55e-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: 119.02  E-value: 1.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750   26 QDCYHGDGQSYRGTYSTTVTGRTCQAWSSMTPHQHNRTTENYPNAGLIMNYCRNPDA-VAAPYCYTRDPGVRWEYCNLTQ 104
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  105 CS 106
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 824-904 2.12e-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: 118.63  E-value: 2.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  824 QECYHGNGQSYRGTYSTTVTGRTCQAWSSMTPHSHSRTPEYYPNAGLIMNYCRNPD-PVAAPYCYTRDPSVRWEYCNLTQ 902
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDgDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750  903 CS 904
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 938-1018 8.50e-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: 116.71  E-value: 8.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  938 QECYHGNGQSYQGTYFITVTGRTCQAWSSMTPHSHSRTPAYYPNAGLIKNYCRNPD-PVAAPWCYTTDPSVRWEYCNLTR 1016
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDgDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 116292750 1017 CS 1018
Cdd:cd00108    82 CE 83
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 1837-2034 3.68e-09

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 58.53  E-value: 3.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1837 LRTRFGKHFCGGTLISPEWVLTAAHCL---KKSSRPSSYKVILGAHQEVNLESHVQEIEVSRLFLEPTQA--DIALLKLS 1911
Cdd:COG3591     5 LETDGGGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYGTATATRFRVPPGWVASGDAgyDYALLRLD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750 1912 RPAVITDKVMPaclPSPDYMVTARTECYITGWGETQGTFGTgLLKEAQLLVIENEVCNHykyicaehlarGTDSCQGDSG 1991
Cdd:COG3591    85 EPLGDTTGWLG---LAFNDAPLAGEPVTIIGYPGDRPKDLS-LDCSGRVTGVQGNRLSY-----------DCDTTGGSSG 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 116292750 1992 GPLVCFEKDKYILQGVTSWGlGCARPNKpGVYARvSRFVTWIE 2034
Cdd:COG3591   150 SPVLDDSDGGGRVVGVHSAG-GADRANT-GVRLT-SAIVAALR 189
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 1831-1942 1.33e-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: 46.39  E-value: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1831 WPWQVSLRTRfGKHFCGGTLISPEWVLTAAHCLKKSSRPSSY-KVILGAHQEV-NLESHVQEIEVSRLFLEPTQADIALL 1908
Cdd:pfam09342    1 WPWIAKVYLD-GNMICSGVLIDASWVIVSGSCLRDTNLRHQYiSVVLGGAKTLkSIEGPYEQIVRVDCRHDIPESEISLL 79

                           90       100       110
                   ....*....|....*....|....*....|....
gi 116292750  1909 KLSRPAVITDKVMPACLPSPDYMVTARTECYITG 1942
Cdd:pfam09342   80 HLASPASFSNHVLPTFVPETRNENEKDNECLAVG 113
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 1848-1995 6.01e-03

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 39.33  E-value: 6.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116292750  1848 GTLISPE-WVLTAAHCLKKSSRPSSYKVILGAHQevnleshVQEIEVSRLFLEPtQADIALLKLSRPAviTDKVMPACLP 1926
Cdd:pfam13365    3 GFVVSSDgLVLTNAHVVDDAEEAAVELVSVVLAD-------GREYPATVVARDP-DLDLALLRVSGDG--RGLPPLPLGD 72

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116292750  1927 SPDYMVTARteCYITG--WGETQGTFGTGllkeaqllVIENEVCNHYKYICAEHLARGTDSCQGDSGGPLV 1995
Cdd:pfam13365   73 SEPLVGGER--VYAVGypLGGEKLSLSEG--------IVSGVDEGRDGGDDGRVIQTDAALSPGSSGGPVF 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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