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Conserved domains on  [gi|257471003|ref|NP_032903|]
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plasminogen precursor [Mus musculus]

Protein Classification

KR and Tryp_SPc domain-containing protein( domain architecture ID 10840640)

protein containing domains PAN_AP_HGF, KR, and Tryp_SPc

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 582-807 8.29e-98

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: 303.43  E-value: 8.29e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 582 VVGGCVANPHSWPWQISLRTRfTGQHFCGGTLIAPEWVLTAAHCLEkSSRPEFYKVILGAHEEYIRGLDVQEISVAKLIL 661
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT-GGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 662 EPN------NRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFG-AGRLKEAQLPVIENKVCNRV 734
Cdd:cd00190   79 HPNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257471003 735 EYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIER 807
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 273-354 9.05e-41

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: 144.07  E-value: 9.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   273 YQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDG-ETAPWCYTTDSQLRWEYCEIPS 351
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   352 CES 354
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 375-456 4.69e-40

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


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 142.14  E-value: 4.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   375 QECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDK-GPWCYTTDPSVRWEYCNLKR 453
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   454 CSE 456
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 183-262 3.02e-37

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


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 134.05  E-value: 3.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   183 EECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDG-EPRPWCFTTDPTKRWEYCDIPR 261
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   .
gi 257471003   262 C 262
Cdd:smart00130  81 C 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 101-183 1.13e-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: 1.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   101 SECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPE 180
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   181 CEE 183
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 480-562 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: 125.58  E-value: 2.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   480 DCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPL 559
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHR-FTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   560 CAS 562
Cdd:smart00130  81 CEE 83
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 38-97 5.29e-13

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


:

Pssm-ID: 238532  Cd Length: 80  Bit Score: 64.80  E-value: 5.29e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257471003  38 KKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRD--VILFEKR 97
Cdd:cd01099   19 KTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDsnVDYYENK 80
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 582-807 8.29e-98

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: 303.43  E-value: 8.29e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 582 VVGGCVANPHSWPWQISLRTRfTGQHFCGGTLIAPEWVLTAAHCLEkSSRPEFYKVILGAHEEYIRGLDVQEISVAKLIL 661
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT-GGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 662 EPN------NRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFG-AGRLKEAQLPVIENKVCNRV 734
Cdd:cd00190   79 HPNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257471003 735 EYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIER 807
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 581-805 6.03e-97

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: 301.13  E-value: 6.03e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   581 RVVGGCVANPHSWPWQISLRTRfTGQHFCGGTLIAPEWVLTAAHCLEkSSRPEFYKVILGAHEeYIRGLDVQEISVAKLI 660
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG-GGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   661 LEPN------NRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFGAG--RLKEAQLPVIENKVCN 732
Cdd:smart00020  78 IHPNynpstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257471003   733 RVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCfEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWI 805
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
582-805 1.14e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.26  E-value: 1.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  582 VVGGCVANPHSWPWQISLrTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRpefYKVILGAHEEYIRGLDVQEISVAKLIL 661
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL-QLSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  662 EPN------NRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGeTQGTFG-AGRLKEAQLPVIENKVCNRv 734
Cdd:pfam00089  77 HPNynpdtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGpSDTLQEVTVPVVSRETCRS- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257471003  735 eYLNNRVKSTELCAGqlAGGVDSCQGDSGGPLVCfeKDKYiLQGVTSWGLGCARPNKPGVYVRVSRFVDWI 805
Cdd:pfam00089 155 -AYGGTVTDTMICAG--AGGKDACQGDSGGPLVC--SDGE-LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 581-812 1.53e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.05  E-value: 1.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 581 RVVGGCVANPHSWPWQISLRTRF-TGQHFCGGTLIAPEWVLTAAHCLEKSSrPEFYKVILGAHEeyIRGLDVQEISVAKL 659
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSNgPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTD--LSTSGGTVVKVARI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 660 ILEPN------NRDIALLKLSRPATitdKVIPACLPSPNYMVADRTICYITGWGETQGTFG--AGRLKEAQLPVIENKVC 731
Cdd:COG5640  107 VVHPDydpatpGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsqSGTLRKADVPVVSDATC 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 732 NRVEYLNNrvkSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIEREMRN 811
Cdd:COG5640  184 AAYGGFDG---GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260


                 .
gi 257471003 812 N 812
Cdd:COG5640  261 L 261
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 273-354 9.05e-41

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: 144.07  E-value: 9.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   273 YQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDG-ETAPWCYTTDSQLRWEYCEIPS 351
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   352 CES 354
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 375-456 4.69e-40

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 142.14  E-value: 4.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   375 QECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDK-GPWCYTTDPSVRWEYCNLKR 453
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   454 CSE 456
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 273-353 1.49e-39

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 140.59  E-value: 1.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 273 YQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGE-TAPWCYTTDSQLRWEYCEIPS 351
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIPR 81


                 ..
gi 257471003 352 CE 353
Cdd:cd00108   82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 275-352 2.26e-39

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 140.14  E-value: 2.26e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003  275 CLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNR-TPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSC 352
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 377-454 3.44e-39

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 139.36  E-value: 3.44e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003  377 CYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSK-TPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRC 454
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 183-262 3.02e-37

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 134.05  E-value: 3.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   183 EECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDG-EPRPWCFTTDPTKRWEYCDIPR 261
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   .
gi 257471003   262 C 262
Cdd:smart00130  81 C 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 101-183 1.13e-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: 1.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   101 SECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPE 180
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   181 CEE 183
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 375-455 1.83e-36

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 131.73  E-value: 1.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 375 QECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDK-GPWCYTTDPSVRWEYCNLKR 453
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                 ..
gi 257471003 454 CS 455
Cdd:cd00108   82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 185-262 3.13e-36

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 130.89  E-value: 3.13e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003  185 CMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHG-YIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRC 262
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 102-182 3.24e-35

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 128.26  E-value: 3.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 102 ECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPEC 181
Cdd:cd00108    3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82


                 .
gi 257471003 182 E 182
Cdd:cd00108   83 E 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 182-262 1.32e-34

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: 126.72  E-value: 1.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 182 EEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEP-RPWCFTTDPTKRWEYCDIP 260
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                 ..
gi 257471003 261 RC 262
Cdd:cd00108   81 RC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 480-562 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: 125.58  E-value: 2.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   480 DCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPL 559
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHR-FTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   560 CAS 562
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 481-560 1.01e-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: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  481 CMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNgPWCYTTNPRKLYDYCDIPLC 560
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 478-561 1.64e-32

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 120.56  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 478 ETDCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDI 557
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHK-FNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDI 79


                 ....
gi 257471003 558 PLCA 561
Cdd:cd00108   80 PRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 103-181 1.81e-30

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 114.71  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  103 CKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPN-YSPSTHPNEGLEENYCRNPDNDEqGPWCYTTDPDKRYDYCNIPEC 181
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 38-97 5.29e-13

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


Pssm-ID: 238532  Cd Length: 80  Bit Score: 64.80  E-value: 5.29e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257471003  38 KKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRD--VILFEKR 97
Cdd:cd01099   19 KTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDsnVDYYENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 20-97 5.43e-11

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


Pssm-ID: 214680  Cd Length: 78  Bit Score: 59.13  E-value: 5.43e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003    20 DSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEgETDFVCRSFQYHSKEQQCVIMAENSKTSS-IIRMRDVILFEKR 97
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSRIVISVASLEECASKCL-NSNCSCRSFTYNNGTKGCLLWSESSLGDArLFPSGGVDLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 25-97 9.64e-10

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


Pssm-ID: 459635  Cd Length: 76  Bit Score: 55.64  E-value: 9.64e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257471003   25 YISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDfvCRSFQYHSKEQQCVIMAENSKT-SSIIRMRD-VILFEKR 97
Cdd:pfam00024   3 FERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPR--CRSFTYNPKSKKCHLKSSSSGSlPRLKRSDNkVDYYEKS 75
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 582-807 8.29e-98

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: 303.43  E-value: 8.29e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 582 VVGGCVANPHSWPWQISLRTRfTGQHFCGGTLIAPEWVLTAAHCLEkSSRPEFYKVILGAHEEYIRGLDVQEISVAKLIL 661
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYT-GGRHFCGGSLISPRWVLTAAHCVY-SSAPSNYTVRLGSHDLSSNEGGGQVIKVKKVIV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 662 EPN------NRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFG-AGRLKEAQLPVIENKVCNRV 734
Cdd:cd00190   79 HPNynpstyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGPlPDVLQEVNVPIVSNAECKRA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257471003 735 EYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIER 807
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 581-805 6.03e-97

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: 301.13  E-value: 6.03e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   581 RVVGGCVANPHSWPWQISLRTRfTGQHFCGGTLIAPEWVLTAAHCLEkSSRPEFYKVILGAHEeYIRGLDVQEISVAKLI 660
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYG-GGRHFCGGSLISPRWVLTAAHCVR-GSDPSNIRVRLGSHD-LSSGEEGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   661 LEPN------NRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGETQGTFGAG--RLKEAQLPVIENKVCN 732
Cdd:smart00020  78 IHPNynpstyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257471003   733 RVEYLNNRVKSTELCAGQLAGGVDSCQGDSGGPLVCfEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWI 805
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
582-805 1.14e-71

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 234.26  E-value: 1.14e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  582 VVGGCVANPHSWPWQISLrTRFTGQHFCGGTLIAPEWVLTAAHCLEKSSRpefYKVILGAHEEYIRGLDVQEISVAKLIL 661
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSL-QLSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  662 EPN------NRDIALLKLSRPATITDKVIPACLPSPNYMVADRTICYITGWGeTQGTFG-AGRLKEAQLPVIENKVCNRv 734
Cdd:pfam00089  77 HPNynpdtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWG-NTKTLGpSDTLQEVTVPVVSRETCRS- 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 257471003  735 eYLNNRVKSTELCAGqlAGGVDSCQGDSGGPLVCfeKDKYiLQGVTSWGLGCARPNKPGVYVRVSRFVDWI 805
Cdd:pfam00089 155 -AYGGTVTDTMICAG--AGGKDACQGDSGGPLVC--SDGE-LIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 581-812 1.53e-62

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.05  E-value: 1.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 581 RVVGGCVANPHSWPWQISLRTRF-TGQHFCGGTLIAPEWVLTAAHCLEKSSrPEFYKVILGAHEeyIRGLDVQEISVAKL 659
Cdd:COG5640   30 AIVGGTPATVGEYPWMVALQSSNgPSGQFCGGTLIAPRWVLTAAHCVDGDG-PSDLRVVIGSTD--LSTSGGTVVKVARI 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 660 ILEPN------NRDIALLKLSRPATitdKVIPACLPSPNYMVADRTICYITGWGETQGTFG--AGRLKEAQLPVIENKVC 731
Cdd:COG5640  107 VVHPDydpatpGNDIALLKLATPVP---GVAPAPLATSADAAAPGTPATVAGWGRTSEGPGsqSGTLRKADVPVVSDATC 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 732 NRVEYLNNrvkSTELCAGQLAGGVDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVDWIEREMRN 811
Cdd:COG5640  184 AAYGGFDG---GTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWIKSTAGG 260


                 .
gi 257471003 812 N 812
Cdd:COG5640  261 L 261
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 273-354 9.05e-41

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: 144.07  E-value: 9.05e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   273 YQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDG-ETAPWCYTTDSQLRWEYCEIPS 351
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   352 CES 354
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 375-456 4.69e-40

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 142.14  E-value: 4.69e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   375 QECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDK-GPWCYTTDPSVRWEYCNLKR 453
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   454 CSE 456
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 273-353 1.49e-39

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 140.59  E-value: 1.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 273 YQCLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNRTPENFPCKNLEENYCRNPDGE-TAPWCYTTDSQLRWEYCEIPS 351
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCDIPR 81


                 ..
gi 257471003 352 CE 353
Cdd:cd00108   82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 275-352 2.26e-39

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 140.14  E-value: 2.26e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003  275 CLKGRGENYRGTVSVTVSGKTCQRWSEQTPHRHNR-TPENFPCKNLEENYCRNPDGETAPWCYTTDSQLRWEYCEIPSC 352
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 377-454 3.44e-39

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 139.36  E-value: 3.44e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003  377 CYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSK-TPENFPDAGLEMNYCRNPDGDKGPWCYTTDPSVRWEYCNLKRC 454
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 183-262 3.02e-37

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 134.05  E-value: 3.02e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   183 EECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDG-EPRPWCFTTDPTKRWEYCDIPR 261
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCDIPQ 80


                   .
gi 257471003   262 C 262
Cdd:smart00130  81 C 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 101-183 1.13e-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: 1.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   101 SECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPE 180
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   181 CEE 183
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 375-455 1.83e-36

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 131.73  E-value: 1.83e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 375 QECYQSDGQSYRGTSSTTITGKKCQSWAAMFPHRHSKTPENFPDAGLEMNYCRNPDGDK-GPWCYTTDPSVRWEYCNLKR 453
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIPR 81


                 ..
gi 257471003 454 CS 455
Cdd:cd00108   82 CE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 185-262 3.13e-36

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 130.89  E-value: 3.13e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003  185 CMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHG-YIPAKFPSKNLKMNYCRNPDGEPRPWCFTTDPTKRWEYCDIPRC 262
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 102-182 3.24e-35

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 128.26  E-value: 3.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 102 ECKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPNYSPSTHPNEGLEENYCRNPDNDEQGPWCYTTDPDKRYDYCNIPEC 181
Cdd:cd00108    3 DCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPRC 82


                 .
gi 257471003 182 E 182
Cdd:cd00108   83 E 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 182-262 1.32e-34

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: 126.72  E-value: 1.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 182 EEECMYCSGEKYEGKISKTMSGLDCQAWDSQSPHAHGYIPAKFPSKNLKMNYCRNPDGEP-RPWCFTTDPTKRWEYCDIP 260
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                 ..
gi 257471003 261 RC 262
Cdd:cd00108   81 RC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 480-562 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: 125.58  E-value: 2.84e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003   480 DCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDIPL 559
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHR-FTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 257471003   560 CAS 562
Cdd:smart00130  81 CEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 481-560 1.01e-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: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  481 CMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSIFTPQTNPRAGLEKNYCRNPDGDVNgPWCYTTNPRKLYDYCDIPLC 560
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKGLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 478-561 1.64e-32

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 120.56  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 478 ETDCMYGNGKDYRGKTAVTAAGTPCQGWAAQEPHRHSiFTPQTNPRAGLEKNYCRNPDGDVNGPWCYTTNPRKLYDYCDI 557
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHK-FNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDI 79


                 ....
gi 257471003 558 PLCA 561
Cdd:cd00108   80 PRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 103-181 1.81e-30

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 114.71  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  103 CKTGIGNGYRGTMSRTKSGVACQKWGATFPHVPN-YSPSTHPNEGLEENYCRNPDNDEqGPWCYTTDPDKRYDYCNIPEC 181
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkYTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 38-97 5.29e-13

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


Pssm-ID: 238532  Cd Length: 80  Bit Score: 64.80  E-value: 5.29e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 257471003  38 KKQLAAGGVSDCLAKCEGETDFVCRSFQYHSKEQQCVIMAENSKTSSIIRMRD--VILFEKR 97
Cdd:cd01099   19 KTEITVASLEECLRKCLEETEFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDsnVDYYENK 80
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 605-811 5.14e-12

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 65.47  E-value: 5.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 605 GQHFCGGTLIAPEWVLTAAHCL---EKSSRPEFYKVILGAHEEYIRGLDVQEISVAK-LILEPN-NRDIALLKLSRPatI 679
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNGGPYGTATATRFRVPPgWVASGDaGYDYALLRLDEP--L 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003 680 TDKVIPACLPSPNYMVADRTIcYITGwgetqgtFGAGRLKEAQLpvienkvcnrveYLNNRVKSTElcAGQLAGGVDSCQ 759
Cdd:COG3591   88 GDTTGWLGLAFNDAPLAGEPV-TIIG-------YPGDRPKDLSL------------DCSGRVTGVQ--GNRLSYDCDTTG 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 257471003 760 GDSGGPLVCFEKDKYILQGVTSWGlGCARPNKpGVYVRvSRFVDWIEREMRN 811
Cdd:COG3591  146 GSSGSPVLDDSDGGGRVVGVHSAG-GADRANT-GVRLT-SAIVAALRAWASA 194
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 20-97 5.43e-11

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


Pssm-ID: 214680  Cd Length: 78  Bit Score: 59.13  E-value: 5.43e-11
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003    20 DSLDGYISTQGASLFSLTKKQLAAGGVSDCLAKCEgETDFVCRSFQYHSKEQQCVIMAENSKTSS-IIRMRDVILFEKR 97
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSRIVISVASLEECASKCL-NSNCSCRSFTYNNGTKGCLLWSESSLGDArLFPSGGVDLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 25-97 9.64e-10

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


Pssm-ID: 459635  Cd Length: 76  Bit Score: 55.64  E-value: 9.64e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 257471003   25 YISTQGASLFSLTKKQLAAGGVSDCLAKCEGETDfvCRSFQYHSKEQQCVIMAENSKT-SSIIRMRD-VILFEKR 97
Cdd:pfam00024   3 FERVPGSSLSGVDVSTVTVSSAEECAQRCTNEPR--CRSFTYNPKSKKCHLKSSSSGSlPRLKRSDNkVDYYEKS 75
Trypsin_2 pfam13365
Trypsin-like peptidase domain; This family includes trypsin-like peptidase domains.
 611-767 3.38e-05

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


Pssm-ID: 433149 [Multi-domain]  Cd Length: 142  Bit Score: 44.33  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  611 GTLIAPE-WVLTAAHCLEKSSRPEFYKVilgaheeYIRGLDVQEISVAKLILEPnNRDIALLKLSRPATItdkvIPACLP 689
Cdd:pfam13365   3 GFVVSSDgLVLTNAHVVDDAEEAAVELV-------SVVLADGREYPATVVARDP-DLDLALLRVSGDGRG----LPPLPL 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257471003  690 SPNYMVADRTICYITGwgetqgtFGAGRLKEAqlpVIENKVCNRVEYLNNRVKSTEL-CAGQLAGgvdscqGDSGGPLV 767
Cdd:pfam13365  71 GDSEPLVGGERVYAVG-------YPLGGEKLS---LSEGIVSGVDEGRDGGDDGRVIqTDAALSP------GSSGGPVF 133
DUF1986 pfam09342
Domain of unknown function (DUF1986); This domain is found in serine proteases and is ...
 593-690 1.86e-04

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: 41.76  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257471003  593 WPWQISLRtrFTGQHFCGGTLIAPEWVLTAAHCLEKSS-RPEFYKVILGAHEEY--IRG--LDVQEISVAKLILEPNnrd 667
Cdd:pfam09342   1 WPWIAKVY--LDGNMICSGVLIDASWVIVSGSCLRDTNlRHQYISVVLGGAKTLksIEGpyEQIVRVDCRHDIPESE--- 75

                          90       100
                  ....*....|....*....|...
gi 257471003  668 IALLKLSRPATITDKVIPACLPS 690
Cdd:pfam09342  76 ISLLHLASPASFSNHVLPTFVPE 98
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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