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Conserved domains on  [gi|158256780|dbj|BAF84363|]
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unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 494-716 7.13e-67

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: 220.24  E-value: 7.13e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   494 RVVNGIPTrtNIG---WMVSLRYRN-KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDekcKQVLNVSQ 569
Cdd:smart00020   1 RIVGGSEA--NIGsfpWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE---GQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   570 LV----YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEK 641
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTseGAGSLPDTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158256780   642 CSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 716
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 210-290 6.24e-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: 6.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   210 ECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 288
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 158256780   289 AD 290
Cdd:smart00130  82 EE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-208 1.48e-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: 137.52  E-value: 1.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 158256780   206 CSE 208
Cdd:smart00130  81 CEE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 304-384 1.64e-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: 134.44  E-value: 1.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   304 ECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqIPN 382
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 158256780   383 CD 384
Cdd:smart00130  81 CE 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 388-470 4.69e-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: 124.80  E-value: 4.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 388 GQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHISWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 467
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 158256780 468 RCE 470
Cdd:cd00108   81 RCE 83
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 39-122 1.30e-27

PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth factor proteins, plasma prekallikrein/coagulation factor XI and microneme antigen proteins, plant receptor-like protein kinases, and various nematode and leech anti-platelet proteins. Common structural features include two disulfide bonds that link the alpha-helix to the central region of the protein. PAN domains have significant functional versatility, fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


:

Pssm-ID: 238074  Cd Length: 80  Bit Score: 106.24  E-value: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNkGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129    1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                 ....
gi 158256780 119 YENK 122
Cdd:cd00129   77 YENK 80
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 494-716 7.13e-67

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: 220.24  E-value: 7.13e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   494 RVVNGIPTrtNIG---WMVSLRYRN-KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDekcKQVLNVSQ 569
Cdd:smart00020   1 RIVGGSEA--NIGsfpWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE---GQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   570 LV----YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEK 641
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTseGAGSLPDTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158256780   642 CSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 716
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 495-719 5.27e-66

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: 217.91  E-value: 5.27e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 495 VVNGIPTR-TNIGWMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVhgRGDEKCKQVLNVSQLV- 571
Cdd:cd00190    1 IVGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKVIv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 572 ---YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT-GLINYDGLLRVAHLYIMGNEKCSQH 645
Cdd:cd00190   79 hpnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNVPIVSNAECKRA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158256780 646 HRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 719
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
495-716 1.23e-55

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 189.58  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  495 VVNGIPTRTNIG-WMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRdlKDYEAWLGIHDVHGRgdEKCKQVLNVSQLV- 571
Cdd:pfam00089   1 IVGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLR--EGGEQKFDVEKIIv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  572 ---YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHH 646
Cdd:pfam00089  77 hpnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  647 RGKVTlnESEICAGAekIGSGPCEGDYGGPLVCEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 716
Cdd:pfam00089 157 GGTVT--DTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 210-290 6.24e-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: 6.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   210 ECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 288
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 158256780   289 AD 290
Cdd:smart00130  82 EE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 211-288 5.00e-39

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 138.59  E-value: 5.00e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158256780  211 CMTCNGESYRGLMDHTESGKICQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTC 288
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-208 1.48e-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: 137.52  E-value: 1.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 158256780   206 CSE 208
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 208-289 5.18e-38

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 135.97  E-value: 5.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 208 EVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIK 286
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 158256780 287 TCA 289
Cdd:cd00108   81 RCE 83
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 488-720 5.69e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 142.10  E-value: 5.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 488 AKTKQLRVVNGIP-TRTNIGWMVSLRYRN---KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGdekcKQ 563
Cdd:COG5640   24 AADAAPAIVGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSG----GT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 564 VLNVSQLVYGPE------GSDLVLMKLARPAvldDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLY 635
Cdd:COG5640  100 VVKVARIVVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKADVP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 636 IMGNEKCSQHHRgkvTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKW 715
Cdd:COG5640  177 VVSDATCAAYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                 ....*
gi 158256780 716 IHKII 720
Cdd:COG5640  254 IKSTA 258
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 126-207 7.03e-38

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 135.58  E-value: 7.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                 ..
gi 158256780 206 CS 207
Cdd:cd00108   82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 304-384 1.64e-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: 134.44  E-value: 1.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   304 ECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqIPN 382
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 158256780   383 CD 384
Cdd:smart00130  81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 305-383 3.37e-37

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: 133.59  E-value: 3.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  305 CIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDM-TPENFKCKDLRENYCRNPDGSESPWCFTTDPNIRVGYCSqIPNC 383
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCD-IPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 302-384 7.99e-37

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: 132.50  E-value: 7.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 302 TTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqI 380
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCD-I 79


                 ....
gi 158256780 381 PNCD 384
Cdd:cd00108   80 PRCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 388-470 4.69e-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: 124.80  E-value: 4.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 388 GQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHISWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 467
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 158256780 468 RCE 470
Cdd:cd00108   81 RCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 128-206 1.06e-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: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  128 CIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSF-LPSSYRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 206
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 389-471 1.39e-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: 123.27  E-value: 1.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   389 QDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHI-SWEPDAsKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 467
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTpESFPDL-GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 158256780   468 RCEG 471
Cdd:smart00130  80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 391-469 1.71e-31

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: 117.41  E-value: 1.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  391 CYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHISWEPDASK-LNENYCRNPDDDAHgPWCYTGNPLIPWDYCPISRC 469
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKgLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 39-122 1.30e-27

PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth factor proteins, plasma prekallikrein/coagulation factor XI and microneme antigen proteins, plant receptor-like protein kinases, and various nematode and leech anti-platelet proteins. Common structural features include two disulfide bonds that link the alpha-helix to the central region of the protein. PAN domains have significant functional versatility, fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238074  Cd Length: 80  Bit Score: 106.24  E-value: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNkGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129    1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                 ....
gi 158256780 119 YENK 122
Cdd:cd00129   77 YENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 37-122 2.44e-09

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: 54.51  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780    37 NTIHEFKKSAKTTLIKIDPalkiKTKKVNTADQCANRCTRNKglpFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGhEF 116
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72


                   ....*.
gi 158256780   117 DLYENK 122
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 41-121 7.61e-09

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: 52.94  E-value: 7.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   41 EFKKSAKTTLIKIDpalkIKTKKVNTADQCANRCTRNKGlpftCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYE 120
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 158256780  121 N 121
Cdd:pfam00024  74 K 74
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 494-716 7.13e-67

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: 220.24  E-value: 7.13e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   494 RVVNGIPTrtNIG---WMVSLRYRN-KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDekcKQVLNVSQ 569
Cdd:smart00020   1 RIVGGSEA--NIGsfpWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHDLSSGEE---GQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   570 LV----YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEK 641
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTseGAGSLPDTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158256780   642 CSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 716
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 495-719 5.27e-66

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: 217.91  E-value: 5.27e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 495 VVNGIPTR-TNIGWMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVhgRGDEKCKQVLNVSQLV- 571
Cdd:cd00190    1 IVGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKVIv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 572 ---YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT-GLINYDGLLRVAHLYIMGNEKCSQH 645
Cdd:cd00190   79 hpnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNVPIVSNAECKRA 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158256780 646 HRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 719
Cdd:cd00190  159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
495-716 1.23e-55

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 189.58  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  495 VVNGIPTRTNIG-WMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRdlKDYEAWLGIHDVHGRgdEKCKQVLNVSQLV- 571
Cdd:pfam00089   1 IVGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLR--EGGEQKFDVEKIIv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  572 ---YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHH 646
Cdd:pfam00089  77 hpnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  647 RGKVTlnESEICAGAekIGSGPCEGDYGGPLVCEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 716
Cdd:pfam00089 157 GGTVT--DTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 210-290 6.24e-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: 6.24e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   210 ECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 288
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 158256780   289 AD 290
Cdd:smart00130  82 EE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 211-288 5.00e-39

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 138.59  E-value: 5.00e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158256780  211 CMTCNGESYRGLMDHTESGKICQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTC 288
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-208 1.48e-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: 137.52  E-value: 1.48e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 158256780   206 CSE 208
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 208-289 5.18e-38

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 135.97  E-value: 5.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 208 EVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIK 286
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 158256780 287 TCA 289
Cdd:cd00108   81 RCE 83
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 488-720 5.69e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 142.10  E-value: 5.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 488 AKTKQLRVVNGIP-TRTNIGWMVSLRYRN---KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGdekcKQ 563
Cdd:COG5640   24 AADAAPAIVGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSG----GT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 564 VLNVSQLVYGPE------GSDLVLMKLARPAvldDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLY 635
Cdd:COG5640  100 VVKVARIVVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKADVP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 636 IMGNEKCSQHHRgkvTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKW 715
Cdd:COG5640  177 VVSDATCAAYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                 ....*
gi 158256780 716 IHKII 720
Cdd:COG5640  254 IKSTA 258
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 126-207 7.03e-38

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 135.58  E-value: 7.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 126 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSFLPSSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 205
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                 ..
gi 158256780 206 CS 207
Cdd:cd00108   82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 304-384 1.64e-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: 134.44  E-value: 1.64e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   304 ECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqIPN 382
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 158256780   383 CD 384
Cdd:smart00130  81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 305-383 3.37e-37

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: 133.59  E-value: 3.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  305 CIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDM-TPENFKCKDLRENYCRNPDGSESPWCFTTDPNIRVGYCSqIPNC 383
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCD-IPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 302-384 7.99e-37

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: 132.50  E-value: 7.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 302 TTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqI 380
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCD-I 79


                 ....
gi 158256780 381 PNCD 384
Cdd:cd00108   80 PRCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 388-470 4.69e-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: 124.80  E-value: 4.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780 388 GQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHISWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 467
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 158256780 468 RCE 470
Cdd:cd00108   81 RCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 128-206 1.06e-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: 1.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  128 CIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSF-LPSSYRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 206
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 389-471 1.39e-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: 123.27  E-value: 1.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   389 QDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHI-SWEPDAsKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 467
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTpESFPDL-GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 158256780   468 RCEG 471
Cdd:smart00130  80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 391-469 1.71e-31

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: 117.41  E-value: 1.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  391 CYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHISWEPDASK-LNENYCRNPDDDAHgPWCYTGNPLIPWDYCPISRC 469
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKgLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 39-122 1.30e-27

PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth factor proteins, plasma prekallikrein/coagulation factor XI and microneme antigen proteins, plant receptor-like protein kinases, and various nematode and leech anti-platelet proteins. Common structural features include two disulfide bonds that link the alpha-helix to the central region of the protein. PAN domains have significant functional versatility, fulfilling diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238074  Cd Length: 80  Bit Score: 106.24  E-value: 1.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  39 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNkGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 118
Cdd:cd00129    1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                 ....
gi 158256780 119 YENK 122
Cdd:cd00129   77 YENK 80
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 40-122 1.62e-14

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: 69.04  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780  40 HEFKKSAktTLIKIDPALKIKTKKVNTADQCANRCTRNKglPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLY 119
Cdd:cd01099    2 NDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEET--EFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDYY 77


                 ...
gi 158256780 120 ENK 122
Cdd:cd01099   78 ENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 37-122 2.44e-09

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: 54.51  E-value: 2.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780    37 NTIHEFKKSAKTTLIKIDPalkiKTKKVNTADQCANRCTRNKglpFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGhEF 116
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72


                   ....*.
gi 158256780   117 DLYENK 122
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 41-121 7.61e-09

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: 52.94  E-value: 7.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158256780   41 EFKKSAKTTLIKIDpalkIKTKKVNTADQCANRCTRNKGlpftCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYE 120
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 158256780  121 N 121
Cdd:pfam00024  74 K 74
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 59-97 4.14e-03

Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, microneme antigen proteins, and a few prokaryotic proteins. PAN/APPLE domains fulfill diverse biological functions by mediating protein-protein or protein-carbohydrate interactions.


Pssm-ID: 238533  Cd Length: 73  Bit Score: 36.64  E-value: 4.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 158256780  59 IKTKKVNTADQCANRCTRNKGlpftCKAFVFDKARKQCL 97
Cdd:cd01100   19 LSTVFASSAEQCQAACTADPG----CLAFTYNTKSKKCF 53
 
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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