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Conserved domains on  [gi|1825929349|ref|XP_033048863|]
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hepatocyte growth factor isoform X3 [Trachypithecus francoisi]

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 ...
 554-776 1.22e-66

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: 220.63  E-value: 1.22e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  554 RVVNGIPTR-TNVGWMVSLRYRN-KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDvhgRGDEKRKQVLNVSQLV 631
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHD---LSSGEEGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  632 ----YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEKCS 703
Cdd:smart00020  78 ihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTseGAGSLPDTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1825929349  704 QHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 776
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 270-350 2.09e-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: 145.61  E-value: 2.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  270 ECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 348
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 1825929349  349 AD 350
Cdd:smart00130  82 EE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 364-444 8.98e-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: 135.60  E-value: 8.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  364 ECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqIPN 442
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 1825929349  443 CD 444
Cdd:smart00130  81 CE 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 191-268 7.70e-35

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


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 127.12  E-value: 7.70e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  191 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 265
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1825929349  266 CSE 268
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 448-530 2.31e-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: 125.95  E-value: 2.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 448 GQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 527
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1825929349 528 RCE 530
Cdd:cd00108    81 RCE 83
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 104-187 8.37e-28

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: 107.01  E-value: 8.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 104 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNnGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 183
Cdd:cd00129     1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                  ....
gi 1825929349 184 YENK 187
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 ...
 554-776 1.22e-66

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: 220.63  E-value: 1.22e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  554 RVVNGIPTR-TNVGWMVSLRYRN-KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDvhgRGDEKRKQVLNVSQLV 631
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHD---LSSGEEGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  632 ----YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEKCS 703
Cdd:smart00020  78 ihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTseGAGSLPDTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1825929349  704 QHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 776
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 555-779 1.25e-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: 220.61  E-value: 1.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 555 VVNGIPTR-TNVGWMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVhgRGDEKRKQVLNVSQLV- 631
Cdd:cd00190     1 IVGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKVIv 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 632 ---YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT-GLINYDGLLRVAHLYIMGNEKCSQH 705
Cdd:cd00190    79 hpnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNVPIVSNAECKRA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1825929349 706 HRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 779
Cdd:cd00190   159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
555-776 4.11e-56

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.89  E-value: 4.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 555 VVNGIPTRTNVG-WMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRdlKDYEAWLGIHDVHGRgdEKRKQVLNVSQLV- 631
Cdd:pfam00089   1 IVGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLR--EGGEQKFDVEKIIv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 632 ---YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHH 706
Cdd:pfam00089  77 hpnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 707 RGKVTlnESEICAGAekIGSGPCEGDYGGPLVCEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 776
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 ...
 270-350 2.09e-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: 145.61  E-value: 2.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  270 ECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 348
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 1825929349  349 AD 350
Cdd:smart00130  82 EE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 271-348 1.57e-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: 1.57e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1825929349 271 CMTCNGESYRGLMDHTESGKSCQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTC 348
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 268-349 1.21e-38

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 137.89  E-value: 1.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 268 EVECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIK 346
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1825929349 347 TCA 349
Cdd:cd00108    81 RCE 83
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 548-780 3.06e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 143.25  E-value: 3.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 548 AKTKQLRVVNGIP-TRTNVGWMVSLRYRN---KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKRKq 623
Cdd:COG5640    24 AADAAPAIVGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 624 vlnVSQLVYGPE------GSDLVLMKLARPAvldDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLY 695
Cdd:COG5640   103 ---VARIVVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKADVP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 696 IMGNEKCSQHHRgkvTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKW 775
Cdd:COG5640   177 VVSDATCAAYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                  ....*
gi 1825929349 776 IHKII 780
Cdd:COG5640   254 IKSTA 258
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 364-444 8.98e-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: 135.60  E-value: 8.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  364 ECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqIPN 442
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 1825929349  443 CD 444
Cdd:smart00130  81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 365-443 1.78e-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: 134.36  E-value: 1.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 365 CIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDM-TPENFKCKDLRENYCRNPDGSESPWCFTTDPNIRVGYCSqIPNC 443
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCD-IPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 362-444 4.04e-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: 133.66  E-value: 4.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 362 TTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqI 440
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCD-I 79


                  ....
gi 1825929349 441 PNCD 444
Cdd:cd00108    80 PRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 191-268 7.70e-35

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 127.12  E-value: 7.70e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  191 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 265
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1825929349  266 CSE 268
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 191-267 2.16e-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: 125.95  E-value: 2.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 191 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSY-----RGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 265
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFnperfPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 1825929349 266 CS 267
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 448-530 2.31e-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: 125.95  E-value: 2.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 448 GQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 527
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1825929349 528 RCE 530
Cdd:cd00108    81 RCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 449-531 7.91e-34

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 124.42  E-value: 7.91e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  449 QDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIF-WEPDAsKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 527
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPeSFPDL-GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 1825929349  528 RCEG 531
Cdd:smart00130  80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 451-529 5.95e-32

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 118.95  E-value: 5.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 451 CYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASK-LNENYCRNPDDDAHgPWCYTGNPLIPWDYCPISRC 529
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKgLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 193-266 6.43e-32

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 118.56  E-value: 6.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 193 CIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS------YRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 266
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkytpenFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 104-187 8.37e-28

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: 107.01  E-value: 8.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 104 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNnGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 183
Cdd:cd00129     1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                  ....
gi 1825929349 184 YENK 187
Cdd:cd00129    77 YENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 102-187 6.61e-10

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: 56.05  E-value: 6.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  102 NTIHEFKKSAKTTLIKIDPalkiKTKKVNTADQCANRCTRNNglpFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGhEF 181
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72


                   ....*.
gi 1825929349  182 DLYENK 187
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 106-186 2.35e-08

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: 51.40  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 106 EFKKSAKTTLIKIDpalkIKTKKVNTADQCANRCTRNNGlpftCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYE 185
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 1825929349 186 N 186
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 ...
 554-776 1.22e-66

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: 220.63  E-value: 1.22e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  554 RVVNGIPTR-TNVGWMVSLRYRN-KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDvhgRGDEKRKQVLNVSQLV 631
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCVRGSDPSNIRVRLGSHD---LSSGEEGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  632 ----YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLYIMGNEKCS 703
Cdd:smart00020  78 ihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTseGAGSLPDTLQEVNVPIVSNATCR 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1825929349  704 QHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 776
Cdd:smart00020 158 RAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 555-779 1.25e-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: 220.61  E-value: 1.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 555 VVNGIPTR-TNVGWMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVhgRGDEKRKQVLNVSQLV- 631
Cdd:cd00190     1 IVGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCVYSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKVIv 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 632 ---YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYT-GLINYDGLLRVAHLYIMGNEKCSQH 705
Cdd:cd00190    79 hpnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTsEGGPLPDVLQEVNVPIVSNAECKRA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1825929349 706 HRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 779
Cdd:cd00190   159 YSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
555-776 4.11e-56

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.89  E-value: 4.11e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 555 VVNGIPTRTNVG-WMVSLRYR-NKHICGGSLIKESWVLTARQCFPSRdlKDYEAWLGIHDVHGRgdEKRKQVLNVSQLV- 631
Cdd:pfam00089   1 IVGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA--SDVKVVLGAHNIVLR--EGGEQKFDVEKIIv 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 632 ---YGPE--GSDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHLYIMGNEKCSQHH 706
Cdd:pfam00089  77 hpnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRSAY 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 707 RGKVTlnESEICAGAekIGSGPCEGDYGGPLVCEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 776
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 ...
 270-350 2.09e-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: 145.61  E-value: 2.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  270 ECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIKTC 348
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81


                   ..
gi 1825929349  349 AD 350
Cdd:smart00130  82 EE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 271-348 1.57e-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: 1.57e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1825929349 271 CMTCNGESYRGLMDHTESGKSCQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTC 348
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 268-349 1.21e-38

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 137.89  E-value: 1.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 268 EVECMTCNGESYRGLMDHTESGKSCQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGQP-RPWCYTLDPHTRWEYCAIK 346
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPeGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1825929349 347 TCA 349
Cdd:cd00108    81 RCE 83
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 548-780 3.06e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 143.25  E-value: 3.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 548 AKTKQLRVVNGIP-TRTNVGWMVSLRYRN---KHICGGSLIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKRKq 623
Cdd:COG5640    24 AADAAPAIVGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPSDLRVVIGSTDLSTSGGTVVK- 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 624 vlnVSQLVYGPE------GSDLVLMKLARPAvldDFVSTIDLPNYGCTIPEKTSCSVYGWGYT--GLINYDGLLRVAHLY 695
Cdd:COG5640   103 ---VARIVVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKADVP 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 696 IMGNEKCSQHHRgkvTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKW 775
Cdd:COG5640   177 VVSDATCAAYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                  ....*
gi 1825929349 776 IHKII 780
Cdd:COG5640   254 IKSTA 258
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 364-444 8.98e-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: 135.60  E-value: 8.98e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  364 ECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqIPN 442
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 1825929349  443 CD 444
Cdd:smart00130  81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 365-443 1.78e-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: 134.36  E-value: 1.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 365 CIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDM-TPENFKCKDLRENYCRNPDGSESPWCFTTDPNIRVGYCSqIPNC 443
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKyTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCD-IPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 362-444 4.04e-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: 133.66  E-value: 4.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 362 TTECIQGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDG-SESPWCFTTDPNIRVGYCSqI 440
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCD-I 79


                  ....
gi 1825929349 441 PNCD 444
Cdd:cd00108    80 PRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 191-268 7.70e-35

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 127.12  E-value: 7.70e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  191 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 265
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1825929349  266 CSE 268
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 191-267 2.16e-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: 125.95  E-value: 2.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 191 RNCIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHSY-----RGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 265
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFnperfPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 1825929349 266 CS 267
Cdd:cd00108    82 CE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 448-530 2.31e-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: 125.95  E-value: 2.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 448 GQDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 527
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1825929349 528 RCE 530
Cdd:cd00108    81 RCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 449-531 7.91e-34

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 124.42  E-value: 7.91e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  449 QDCYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIF-WEPDAsKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 527
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPeSFPDL-GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 1825929349  528 RCEG 531
Cdd:smart00130  80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 451-529 5.95e-32

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 118.95  E-value: 5.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 451 CYRGNGKNYMGNLSQTRSGLTCSMWDKNMEDLHRHIFWEPDASK-LNENYCRNPDDDAHgPWCYTGNPLIPWDYCPISRC 529
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKgLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 193-266 6.43e-32

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 118.56  E-value: 6.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 193 CIIGKGRSYKGTVSITKSGIKCQPWSSMIPHEHS------YRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 266
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkytpenFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 104-187 8.37e-28

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: 107.01  E-value: 8.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 104 IHEFKKSAKTTLIKIdpALKIKTKKVNTADQCANRCTRNnGLPFTCKAFVFDKARKQCLWFPFNSMsSGVKKEFGHEFDL 183
Cdd:cd00129     1 VDEFCKSAGTTLIKI--ALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDL 76


                  ....
gi 1825929349 184 YENK 187
Cdd:cd00129    77 YENK 80
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 105-187 1.28e-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: 69.42  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 105 HEFKKSAktTLIKIDPALKIKTKKVNTADQCANRCTRNNglPFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLY 184
Cdd:cd01099     2 NDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEET--EFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDYY 77


                  ...
gi 1825929349 185 ENK 187
Cdd:cd01099    78 ENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 102-187 6.61e-10

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: 56.05  E-value: 6.61e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349  102 NTIHEFKKSAKTTLIKIDPalkiKTKKVNTADQCANRCTRNNglpFTCKAFVFDKARKQCLWFPFNSMSSGVKKEFGhEF 181
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72


                   ....*.
gi 1825929349  182 DLYENK 187
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 106-186 2.35e-08

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: 51.40  E-value: 2.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1825929349 106 EFKKSAKTTLIKIDpalkIKTKKVNTADQCANRCTRNNGlpftCKAFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYE 185
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 1825929349 186 N 186
Cdd:pfam00024  74 K 74
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 124-162 3.59e-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: 3.59e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1825929349 124 IKTKKVNTADQCANRCTRNNGlpftCKAFVFDKARKQCL 162
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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