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Conserved domains on  [gi|575402995|ref|NP_001276390|]
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hepatocyte growth factor isoform 3 preproprotein [Mus musculus]

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 ...
 490-714 3.36e-63

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: 210.23  E-value: 3.36e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   490 RVVNGIPTQ-TTVGWMVSLKYRN-KHICGGSLIKESWVLTARQCFpaRNKDLKDYEAWLGIHDVHERGEekrKQILNISQ 567
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV--RGSDPSNIRVRLGSHDLSSGEE---GQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   568 LV----YGPE--GSDLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYTGLINADG--LLRVAHLYIMGNEK 639
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575402995   640 CSQHHQGKVTLNESELCAGAEKIGSGPCEGDYGGPLICeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 714
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 206-284 2.90e-39

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: 139.45  E-value: 2.90e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   206 ECMTCNGESYRGPMDHTESGKTCQRWDQQTPHRHKFLPERYPDKGFDDNYCRNPDGKP-RPWCYTLDPDTPWEYCAIKTC 284
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 300-380 6.79e-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: 132.90  E-value: 6.79e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   300 ECIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKHDITPENFKCKDLRENYCRNPDG-AESPWCFTTDPNIRVGYCSqIPK 378
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 575402995   379 CD 380
Cdd:smart00130  81 CE 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 127-204 8.02e-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: 124.04  E-value: 8.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   127 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 201
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 575402995   202 CSE 204
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 384-466 1.18e-33

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


:

Pssm-ID: 238056  Cd Length: 83  Bit Score: 123.64  E-value: 1.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 384 GQDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 463
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 575402995 464 RCE 466
Cdd:cd00108   81 RCE 83
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 41-123 4.88e-22

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: 90.45  E-value: 4.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  41 HEFKKSAKTTLTkeDPLLKIKTKKVNSADECANRCIRNrGFTFTCKAFVFDKSRKRCYWYPFNSMsSGVKKGFGHEFDLY 120
Cdd:cd00129    2 DEFCKSAGTTLI--KIALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDLY 77


                 ...
gi 575402995 121 ENK 123
Cdd:cd00129   78 ENK 80
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 490-714 3.36e-63

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: 210.23  E-value: 3.36e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   490 RVVNGIPTQ-TTVGWMVSLKYRN-KHICGGSLIKESWVLTARQCFpaRNKDLKDYEAWLGIHDVHERGEekrKQILNISQ 567
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV--RGSDPSNIRVRLGSHDLSSGEE---GQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   568 LV----YGPE--GSDLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYTGLINADG--LLRVAHLYIMGNEK 639
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575402995   640 CSQHHQGKVTLNESELCAGAEKIGSGPCEGDYGGPLICeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 714
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 503-717 1.02e-62

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: 209.05  E-value: 1.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 503 WMVSLKYR-NKHICGGSLIKESWVLTARQCFpaRNKDLKDYEAWLGIHDVHERgeEKRKQILNISQLV----YGPE--GS 575
Cdd:cd00190   14 WQVSLQYTgGRHFCGGSLISPRWVLTAAHCV--YSSAPSNYTVRLGSHDLSSN--EGGGQVIKVKKVIvhpnYNPStyDN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 576 DLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYT--GLINADgLLRVAHLYIMGNEKCSQHHQGKVTLNES 653
Cdd:cd00190   90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTseGGPLPD-VLQEVNVPIVSNAECKRAYSYGGTITDN 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575402995 654 ELCAGAEKIGSGPCEGDYGGPLICEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKV 717
Cdd:cd00190  169 MLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
491-714 3.02e-56

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.12  E-value: 3.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  491 VVNGIPTQTTVG-WMVSLKYR-NKHICGGSLIKESWVLTARQCFparnKDLKDYEAWLGIHDVHERgeEKRKQILNISQL 568
Cdd:pfam00089   1 IVGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCV----SGASDVKVVLGAHNIVLR--EGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  569 V----YGPE--GSDLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYTGLINADGLLRVAHLYIMGNEKCSQ 642
Cdd:pfam00089  75 IvhpnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575402995  643 HHQGKVTlnESELCAGAekIGSGPCEGDYGGPLICEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 714
Cdd:pfam00089 155 AYGGTVT--DTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 206-284 2.90e-39

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: 139.45  E-value: 2.90e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   206 ECMTCNGESYRGPMDHTESGKTCQRWDQQTPHRHKFLPERYPDKGFDDNYCRNPDGKP-RPWCYTLDPDTPWEYCAIKTC 284
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 484-718 1.25e-37

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 141.33  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 484 AKTKQLRVVNGIP-TQTTVGWMVSLKYRN---KHICGGSLIKESWVLTARQCFPARNKDlkDYEAWLGIHDVHERGEEKR 559
Cdd:COG5640   24 AADAAPAIVGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS--DLRVVIGSTDLSTSGGTVV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 560 KqilnISQLVYGPE------GSDLVLLKLARPAildNFVSTIDLPSYGCTIPEKTTCSIYGWGYT--GLINADGLLRVAH 631
Cdd:COG5640  102 K----VARIVVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKAD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 632 LYIMGNEKCSQHHQgkvTLNESELCAGAEKIGSGPCEGDYGGPLICEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYA 711
Cdd:COG5640  175 VPVVSDATCAAYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251


                 ....*..
gi 575402995 712 KWIHKVI 718
Cdd:COG5640  252 DWIKSTA 258
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 204-285 4.85e-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: 133.27  E-value: 4.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 204 EVECMTCNGESYRGPMDHTESGKTCQRWDQQTPHRHKFLPERYPDKGFDDNYCRNPDG-KPRPWCYTLDPDTPWEYCAIK 282
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 575402995 283 TCA 285
Cdd:cd00108   81 RCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 300-380 6.79e-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: 132.90  E-value: 6.79e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   300 ECIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKHDITPENFKCKDLRENYCRNPDG-AESPWCFTTDPNIRVGYCSqIPK 378
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 575402995   379 CD 380
Cdd:smart00130  81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 207-284 7.64e-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: 132.43  E-value: 7.64e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575402995  207 CMTCNGESYRGPMDHTESGKTCQRWDQQTPHRH-KFLPERYPDKGFDDNYCRNPDGKPRPWCYTLDPDTPWEYCAIKTC 284
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 298-380 1.02e-36

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 132.12  E-value: 1.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 298 TTECIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKHDITPENFKCKDLRENYCRNPDGA-ESPWCFTTDPNIRVGYCSqI 376
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCD-I 79


                 ....
gi 575402995 377 PKCD 380
Cdd:cd00108   80 PRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 301-379 3.24e-36

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 130.89  E-value: 3.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  301 CIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKH-DITPENFKCKDLRENYCRNPDGAESPWCFTTDPNIRVGYCSqIPKC 379
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCD-IPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 127-204 8.02e-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: 124.04  E-value: 8.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   127 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 201
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 575402995   202 CSE 204
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 384-466 1.18e-33

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 123.64  E-value: 1.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 384 GQDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 463
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 575402995 464 RCE 466
Cdd:cd00108   81 RCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 127-203 2.44e-33

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 122.87  E-value: 2.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 127 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHSY-----RGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 201
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFnperfPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                 ..
gi 575402995 202 CS 203
Cdd:cd00108   82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 385-467 4.19e-33

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.11  E-value: 4.19e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   385 QDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIF-WEPDAsKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 463
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPeSFPDL-GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 575402995   464 RCEG 467
Cdd:smart00130  80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 387-465 5.31e-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: 115.87  E-value: 5.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  387 CYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASK-LNKNYCRNPDDDAHgPWCYTGNPLIPWDYCPISRC 465
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKgLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 129-202 1.02e-30

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 115.10  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  129 CIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS------YRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 202
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkytpenFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 41-123 4.88e-22

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: 90.45  E-value: 4.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  41 HEFKKSAKTTLTkeDPLLKIKTKKVNSADECANRCIRNrGFTFTCKAFVFDKSRKRCYWYPFNSMsSGVKKGFGHEFDLY 120
Cdd:cd00129    2 DEFCKSAGTTLI--KIALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDLY 77


                 ...
gi 575402995 121 ENK 123
Cdd:cd00129   78 ENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 38-123 4.96e-11

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


Pssm-ID: 214680  Cd Length: 78  Bit Score: 59.13  E-value: 4.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995    38 NTLHEFKKSAKTTLTKEDPllkiKTKKVNSADECANRCIRNRgftFTCKAFVFDKSRKRCYWYPFNSMSSgVKKGFGHEF 117
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGD-ARLFPSGGV 72


                   ....*.
gi 575402995   118 DLYENK 123
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 42-122 1.75e-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: 51.78  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   42 EFKKSAKTTLTKEDpllkIKTKKVNSADECANRCIRNRGftftCKAFVFDKSRKRCYWYPFNSMSSGVKKGFGHEFDLYE 121
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 575402995  122 N 122
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 ...
 490-714 3.36e-63

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: 210.23  E-value: 3.36e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   490 RVVNGIPTQ-TTVGWMVSLKYRN-KHICGGSLIKESWVLTARQCFpaRNKDLKDYEAWLGIHDVHERGEekrKQILNISQ 567
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV--RGSDPSNIRVRLGSHDLSSGEE---GQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   568 LV----YGPE--GSDLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYTGLINADG--LLRVAHLYIMGNEK 639
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLpdTLQEVNVPIVSNAT 155

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575402995   640 CSQHHQGKVTLNESELCAGAEKIGSGPCEGDYGGPLICeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 714
Cdd:smart00020 156 CRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 503-717 1.02e-62

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: 209.05  E-value: 1.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 503 WMVSLKYR-NKHICGGSLIKESWVLTARQCFpaRNKDLKDYEAWLGIHDVHERgeEKRKQILNISQLV----YGPE--GS 575
Cdd:cd00190   14 WQVSLQYTgGRHFCGGSLISPRWVLTAAHCV--YSSAPSNYTVRLGSHDLSSN--EGGGQVIKVKKVIvhpnYNPStyDN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 576 DLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYT--GLINADgLLRVAHLYIMGNEKCSQHHQGKVTLNES 653
Cdd:cd00190   90 DIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTseGGPLPD-VLQEVNVPIVSNAECKRAYSYGGTITDN 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575402995 654 ELCAGAEKIGSGPCEGDYGGPLICEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKV 717
Cdd:cd00190  169 MLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
491-714 3.02e-56

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 191.12  E-value: 3.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  491 VVNGIPTQTTVG-WMVSLKYR-NKHICGGSLIKESWVLTARQCFparnKDLKDYEAWLGIHDVHERgeEKRKQILNISQL 568
Cdd:pfam00089   1 IVGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCV----SGASDVKVVLGAHNIVLR--EGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  569 V----YGPE--GSDLVLLKLARPAILDNFVSTIDLPSYGCTIPEKTTCSIYGWGYTGLINADGLLRVAHLYIMGNEKCSQ 642
Cdd:pfam00089  75 IvhpnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575402995  643 HHQGKVTlnESELCAGAekIGSGPCEGDYGGPLICEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 714
Cdd:pfam00089 155 AYGGTVT--DTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 206-284 2.90e-39

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: 139.45  E-value: 2.90e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   206 ECMTCNGESYRGPMDHTESGKTCQRWDQQTPHRHKFLPERYPDKGFDDNYCRNPDGKP-RPWCYTLDPDTPWEYCAIKTC 284
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 484-718 1.25e-37

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 141.33  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 484 AKTKQLRVVNGIP-TQTTVGWMVSLKYRN---KHICGGSLIKESWVLTARQCFPARNKDlkDYEAWLGIHDVHERGEEKR 559
Cdd:COG5640   24 AADAAPAIVGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS--DLRVVIGSTDLSTSGGTVV 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 560 KqilnISQLVYGPE------GSDLVLLKLARPAildNFVSTIDLPSYGCTIPEKTTCSIYGWGYT--GLINADGLLRVAH 631
Cdd:COG5640  102 K----VARIVVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKAD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 632 LYIMGNEKCSQHHQgkvTLNESELCAGAEKIGSGPCEGDYGGPLICEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYA 711
Cdd:COG5640  175 VPVVSDATCAAYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251


                 ....*..
gi 575402995 712 KWIHKVI 718
Cdd:COG5640  252 DWIKSTA 258
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 204-285 4.85e-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: 133.27  E-value: 4.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 204 EVECMTCNGESYRGPMDHTESGKTCQRWDQQTPHRHKFLPERYPDKGFDDNYCRNPDG-KPRPWCYTLDPDTPWEYCAIK 282
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 575402995 283 TCA 285
Cdd:cd00108   81 RCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 300-380 6.79e-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: 132.90  E-value: 6.79e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   300 ECIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKHDITPENFKCKDLRENYCRNPDG-AESPWCFTTDPNIRVGYCSqIPK 378
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 575402995   379 CD 380
Cdd:smart00130  81 CE 82
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 207-284 7.64e-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: 132.43  E-value: 7.64e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575402995  207 CMTCNGESYRGPMDHTESGKTCQRWDQQTPHRH-KFLPERYPDKGFDDNYCRNPDGKPRPWCYTLDPDTPWEYCAIKTC 284
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 298-380 1.02e-36

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 132.12  E-value: 1.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 298 TTECIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKHDITPENFKCKDLRENYCRNPDGA-ESPWCFTTDPNIRVGYCSqI 376
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCD-I 79


                 ....
gi 575402995 377 PKCD 380
Cdd:cd00108   80 PRCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 301-379 3.24e-36

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 130.89  E-value: 3.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  301 CIQGQGEGYRGTSNTIWNGIPCQRWDSQYPHKH-DITPENFKCKDLRENYCRNPDGAESPWCFTTDPNIRVGYCSqIPKC 379
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCD-IPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 127-204 8.02e-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: 124.04  E-value: 8.02e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   127 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 201
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 575402995   202 CSE 204
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 384-466 1.18e-33

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 123.64  E-value: 1.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 384 GQDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 463
Cdd:cd00108    1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                 ...
gi 575402995 464 RCE 466
Cdd:cd00108   81 RCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 127-203 2.44e-33

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 122.87  E-value: 2.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995 127 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHSY-----RGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 201
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFnperfPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                 ..
gi 575402995 202 CS 203
Cdd:cd00108   82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 385-467 4.19e-33

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.11  E-value: 4.19e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   385 QDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIF-WEPDAsKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 463
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPeSFPDL-GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 575402995   464 RCEG 467
Cdd:smart00130  80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 387-465 5.31e-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: 115.87  E-value: 5.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  387 CYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASK-LNKNYCRNPDDDAHgPWCYTGNPLIPWDYCPISRC 465
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKgLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 129-202 1.02e-30

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 115.10  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  129 CIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS------YRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 202
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkytpenFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 41-123 4.88e-22

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: 90.45  E-value: 4.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  41 HEFKKSAKTTLTkeDPLLKIKTKKVNSADECANRCIRNrGFTFTCKAFVFDKSRKRCYWYPFNSMsSGVKKGFGHEFDLY 120
Cdd:cd00129    2 DEFCKSAGTTLI--KIALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDLY 77


                 ...
gi 575402995 121 ENK 123
Cdd:cd00129   78 ENK 80
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 40-123 1.93e-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: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995  40 LHEFKKSAktTLTKEDPLLKIKTKKVNSADECANRCIRNRGFTftCKAFVFDKSRKRCYWYPFNSMSSGVKKGFGHEFDL 119
Cdd:cd01099    1 LNDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEETEFT--CRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDY 76


                 ....
gi 575402995 120 YENK 123
Cdd:cd01099   77 YENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 38-123 4.96e-11

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


Pssm-ID: 214680  Cd Length: 78  Bit Score: 59.13  E-value: 4.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995    38 NTLHEFKKSAKTTLTKEDPllkiKTKKVNSADECANRCIRNRgftFTCKAFVFDKSRKRCYWYPFNSMSSgVKKGFGHEF 117
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGD-ARLFPSGGV 72


                   ....*.
gi 575402995   118 DLYENK 123
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 42-122 1.75e-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: 51.78  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575402995   42 EFKKSAKTTLTKEDpllkIKTKKVNSADECANRCIRNRGftftCKAFVFDKSRKRCYWYPFNSMSSGVKKGFGHEFDLYE 121
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 575402995  122 N 122
Cdd:pfam00024  74 K 74
APPLE_Factor_XI_like cd01100
Subfamily of PAN/APPLE-like domains; present in plasma prekallikrein/coagulation factor XI, ...
 60-98 2.07e-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: 37.41  E-value: 2.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 575402995  60 IKTKKVNSADECANRCIrnrgFTFTCKAFVFDKSRKRCY 98
Cdd:cd01100   19 LSTVFASSAEQCQAACT----ADPGCLAFTYNTKSKKCF 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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