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Conserved domains on  [gi|1191911036|ref|XP_020919145|]
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hepatocyte growth factor isoform X4 [Sus scrofa]

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 ...
 489-713 8.63e-64

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: 211.77  E-value: 8.63e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  489 RVVNGIPTR-TNVGWMVSLKYRN-KHICGGSLIKESWILTARQCFpsRNKDLKDYEAWLGIHDvhgRGDEKRKQVLNVTQ 566
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV--RGSDPSNIRVRLGSHD---LSSGEEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  567 LV----YGPE--GSDLVLLKLARPAVLDDFVSTIDLPNYGCTIPEKTTCSVYGWGYT---GLINSDgLLRVAHLYIMGNE 637
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsegAGSLPD-TLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191911036  638 KCSQYHQGKVTLNESEICAGAENIVSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 713
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 205-283 3.02e-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: 3.02e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  205 ECLTCNGESYRGPMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGKP-RPWCYTLDPDTPWEYCAIKMC 283
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 297-379 2.36e-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: 134.04  E-value: 2.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 297 TTECIQGQGEGYRGTINTIWNGIPCQRWDSQYPHQHDITPENFKCKDLRENYCRNPDGA-ESPWCFTTDPNIRVGYCSqI 375
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCD-I 79


                  ....
gi 1191911036 376 PKCD 379
Cdd:cd00108    80 PRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-203 7.31e-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: 7.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  126 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1191911036  201 CSE 203
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 383-465 9.98e-34

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


:

Pssm-ID: 238056  Cd Length: 83  Bit Score: 124.03  E-value: 9.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 383 GQDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 462
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1191911036 463 RCE 465
Cdd:cd00108    81 RCE 83
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 40-122 1.51e-24

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: 97.77  E-value: 1.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  40 HEFKKSAKTTLIneDPLLKIKTKKMNTADQCANRCIRNkGLPFTCKAFVFDKARKRCLWFPFNSMsSGVKKEFGHEFDLY 119
Cdd:cd00129     2 DEFCKSAGTTLI--KIALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDLY 77


                  ...
gi 1191911036 120 ENK 122
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 ...
 489-713 8.63e-64

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: 211.77  E-value: 8.63e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  489 RVVNGIPTR-TNVGWMVSLKYRN-KHICGGSLIKESWILTARQCFpsRNKDLKDYEAWLGIHDvhgRGDEKRKQVLNVTQ 566
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV--RGSDPSNIRVRLGSHD---LSSGEEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  567 LV----YGPE--GSDLVLLKLARPAVLDDFVSTIDLPNYGCTIPEKTTCSVYGWGYT---GLINSDgLLRVAHLYIMGNE 637
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsegAGSLPD-TLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191911036  638 KCSQYHQGKVTLNESEICAGAENIVSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 713
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 490-716 2.71e-63

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: 210.60  E-value: 2.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 490 VVNGIPTR-TNVGWMVSLKYR-NKHICGGSLIKESWILTARQCFpsRNKDLKDYEAWLGIHDVhgRGDEKRKQVLNVTQL 567
Cdd:cd00190     1 IVGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCV--YSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 568 V----YGPE--GSDLVLLKLARPAVLDDFVSTIDLPNYGCTIPEKTTCSVYGWGYT--GLINSDgLLRVAHLYIMGNEKC 639
Cdd:cd00190    77 IvhpnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTseGGPLPD-VLQEVNVPIVSNAEC 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191911036 640 SQYHQGKVTLNESEICAGAENIVSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 716
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
490-713 2.94e-55

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.42  E-value: 2.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 490 VVNGIPTRTNVG-WMVSLKYR-NKHICGGSLIKESWILTARQCFPSRnkdlKDYEAWLGIHDVHGRgdEKRKQVLNVTQL 567
Cdd:pfam00089   1 IVGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAHNIVLR--EGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 568 V----YGPE--GSDLVLLKLARPAVLDDFVSTIDLPNYGCTIPEKTTCSVYGWGYTGLINSDGLLRVAHLYIMGNEKCSQ 641
Cdd:pfam00089  75 IvhpnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191911036 642 YHQGKVTlnESEICAGAENIvsGPCEGDYGGPLVCEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 713
Cdd:pfam00089 155 AYGGTVT--DTMICAGAGGK--DACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 205-283 3.02e-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: 3.02e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  205 ECLTCNGESYRGPMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGKP-RPWCYTLDPDTPWEYCAIKMC 283
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 483-717 8.97e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 141.71  E-value: 8.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 483 AKTKQLRVVNGIP-TRTNVGWMVSLKYRN---KHICGGSLIKESWILTARQCFPSRNKDlkDYEAWLGIHDVHGRGDEKR 558
Cdd:COG5640    24 AADAAPAIVGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS--DLRVVIGSTDLSTSGGTVV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 559 KqvlnVTQLVYGPE------GSDLVLLKLARPAvldDFVSTIDLPNYGCTIPEKTTCSVYGWGYT--GLINSDGLLRVAH 630
Cdd:COG5640   102 K----VARIVVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKAD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 631 LYIMGNEKCSQYHQgkvTLNESEICAGAENIVSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYA 710
Cdd:COG5640   175 VPVVSDATCAAYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251


                  ....*..
gi 1191911036 711 KWIHKII 717
Cdd:COG5640   252 DWIKSTA 258
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 297-379 2.36e-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: 134.04  E-value: 2.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 297 TTECIQGQGEGYRGTINTIWNGIPCQRWDSQYPHQHDITPENFKCKDLRENYCRNPDGA-ESPWCFTTDPNIRVGYCSqI 375
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCD-I 79


                  ....
gi 1191911036 376 PKCD 379
Cdd:cd00108    80 PRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 299-379 3.90e-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: 133.67  E-value: 3.90e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  299 ECIQGQGEGYRGTINTIWNGIPCQRWDSQYPHQHDITPENFKCKDLRENYCRNPDG-AESPWCFTTDPNIRVGYCSqIPK 377
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 1191911036  378 CD 379
Cdd:smart00130  81 CE 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 203-284 7.03e-37

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 132.89  E-value: 7.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 203 EVECLTCNGESYRGPMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDG-KPRPWCYTLDPDTPWEYCAIK 281
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1191911036 282 MCA 284
Cdd:cd00108    81 RCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 300-378 1.16e-36

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 132.05  E-value: 1.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 300 CIQGQGEGYRGTINTIWNGIPCQRWDSQYPHQH-DITPENFKCKDLRENYCRNPDGAESPWCFTTDPNIRVGYCSqIPKC 378
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCD-IPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 206-283 1.23e-36

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 132.05  E-value: 1.23e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191911036 206 CLTCNGESYRGPMDHTESGKICQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGKPRPWCYTLDPDTPWEYCAIKMC 283
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-203 7.31e-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: 7.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  126 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1191911036  201 CSE 203
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 383-465 9.98e-34

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 124.03  E-value: 9.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 383 GQDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 462
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1191911036 463 RCE 465
Cdd:cd00108    81 RCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 126-202 2.00e-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: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 126 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHSY-----RGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFnperfPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 1191911036 201 CS 202
Cdd:cd00108    82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 384-466 3.46e-33

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.50  E-value: 3.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  384 QDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIF-WEPDAsKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 462
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPeSFPDL-GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 1191911036  463 RCEG 466
Cdd:smart00130  80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 386-464 4.18e-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: 116.25  E-value: 4.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 386 CYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASK-LNKNYCRNPDDDAHgPWCYTGNPLIPWDYCPISRC 464
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKgLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 128-201 8.19e-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: 115.48  E-value: 8.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 128 CIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS------YRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 201
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkytpenFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 40-122 1.51e-24

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: 97.77  E-value: 1.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  40 HEFKKSAKTTLIneDPLLKIKTKKMNTADQCANRCIRNkGLPFTCKAFVFDKARKRCLWFPFNSMsSGVKKEFGHEFDLY 119
Cdd:cd00129     2 DEFCKSAGTTLI--KIALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDLY 77


                  ...
gi 1191911036 120 ENK 122
Cdd:cd00129    78 ENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 37-122 6.43e-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: 6.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036   37 NTLHEFKKSAKTTLINEDPllkiKTKKMNTADQCANRCIRNKglpFTCKAFVFDKARKRCLWFPFNSMSSGVKKEFGhEF 116
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72


                   ....*.
gi 1191911036  117 DLYENK 122
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 41-121 7.63e-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: 49.86  E-value: 7.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  41 EFKKSAKTTLINEDpllkIKTKKMNTADQCANRCIRNKGlpftCKAFVFDKARKRCLWFPFNSMSSGVKKEFGHEFDLYE 120
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 1191911036 121 N 121
Cdd:pfam00024  74 K 74
 
Name Accession Description Interval E-value
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 489-713 8.63e-64

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: 211.77  E-value: 8.63e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  489 RVVNGIPTR-TNVGWMVSLKYRN-KHICGGSLIKESWILTARQCFpsRNKDLKDYEAWLGIHDvhgRGDEKRKQVLNVTQ 566
Cdd:smart00020   1 RIVGGSEANiGSFPWQVSLQYGGgRHFCGGSLISPRWVLTAAHCV--RGSDPSNIRVRLGSHD---LSSGEEGQVIKVSK 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  567 LV----YGPE--GSDLVLLKLARPAVLDDFVSTIDLPNYGCTIPEKTTCSVYGWGYT---GLINSDgLLRVAHLYIMGNE 637
Cdd:smart00020  76 VIihpnYNPStyDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTsegAGSLPD-TLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1191911036  638 KCSQYHQGKVTLNESEICAGAENIVSGPCEGDYGGPLVCeQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 713
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 490-716 2.71e-63

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: 210.60  E-value: 2.71e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 490 VVNGIPTR-TNVGWMVSLKYR-NKHICGGSLIKESWILTARQCFpsRNKDLKDYEAWLGIHDVhgRGDEKRKQVLNVTQL 567
Cdd:cd00190     1 IVGGSEAKiGSFPWQVSLQYTgGRHFCGGSLISPRWVLTAAHCV--YSSAPSNYTVRLGSHDL--SSNEGGGQVIKVKKV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 568 V----YGPE--GSDLVLLKLARPAVLDDFVSTIDLPNYGCTIPEKTTCSVYGWGYT--GLINSDgLLRVAHLYIMGNEKC 639
Cdd:cd00190    77 IvhpnYNPStyDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTseGGPLPD-VLQEVNVPIVSNAEC 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191911036 640 SQYHQGKVTLNESEICAGAENIVSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKI 716
Cdd:cd00190   156 KRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQKT 232
Trypsin pfam00089
Trypsin;
490-713 2.94e-55

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 188.42  E-value: 2.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 490 VVNGIPTRTNVG-WMVSLKYR-NKHICGGSLIKESWILTARQCFPSRnkdlKDYEAWLGIHDVHGRgdEKRKQVLNVTQL 567
Cdd:pfam00089   1 IVGGDEAQPGSFpWQVSLQLSsGKHFCGGSLISENWVLTAAHCVSGA----SDVKVVLGAHNIVLR--EGGEQKFDVEKI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 568 V----YGPE--GSDLVLLKLARPAVLDDFVSTIDLPNYGCTIPEKTTCSVYGWGYTGLINSDGLLRVAHLYIMGNEKCSQ 641
Cdd:pfam00089  75 IvhpnYNPDtlDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTLGPSDTLQEVTVPVVSRETCRS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1191911036 642 YHQGKVTlnESEICAGAENIvsGPCEGDYGGPLVCEQHkmrMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWI 713
Cdd:pfam00089 155 AYGGTVT--DTMICAGAGGK--DACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 205-283 3.02e-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: 3.02e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  205 ECLTCNGESYRGPMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDGKP-RPWCYTLDPDTPWEYCAIKMC 283
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGDSeGPWCYTTDPNVRWEYCDIPQC 81
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 483-717 8.97e-38

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 141.71  E-value: 8.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 483 AKTKQLRVVNGIP-TRTNVGWMVSLKYRN---KHICGGSLIKESWILTARQCFPSRNKDlkDYEAWLGIHDVHGRGDEKR 558
Cdd:COG5640    24 AADAAPAIVGGTPaTVGEYPWMVALQSSNgpsGQFCGGTLIAPRWVLTAAHCVDGDGPS--DLRVVIGSTDLSTSGGTVV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 559 KqvlnVTQLVYGPE------GSDLVLLKLARPAvldDFVSTIDLPNYGCTIPEKTTCSVYGWGYT--GLINSDGLLRVAH 630
Cdd:COG5640   102 K----VARIVVHPDydpatpGNDIALLKLATPV---PGVAPAPLATSADAAAPGTPATVAGWGRTseGPGSQSGTLRKAD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 631 LYIMGNEKCSQYHQgkvTLNESEICAGAENIVSGPCEGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPGIFVRVAYYA 710
Cdd:COG5640   175 VPVVSDATCAAYGG---FDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251


                  ....*..
gi 1191911036 711 KWIHKII 717
Cdd:COG5640   252 DWIKSTA 258
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 297-379 2.36e-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: 134.04  E-value: 2.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 297 TTECIQGQGEGYRGTINTIWNGIPCQRWDSQYPHQHDITPENFKCKDLRENYCRNPDGA-ESPWCFTTDPNIRVGYCSqI 375
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTTDPNVRWEYCD-I 79


                  ....
gi 1191911036 376 PKCD 379
Cdd:cd00108    80 PRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 299-379 3.90e-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: 133.67  E-value: 3.90e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  299 ECIQGQGEGYRGTINTIWNGIPCQRWDSQYPHQHDITPENFKCKDLRENYCRNPDG-AESPWCFTTDPNIRVGYCSqIPK 377
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPESFPDLGLEENYCRNPDGdSEGPWCYTTDPNVRWEYCD-IPQ 80


                   ..
gi 1191911036  378 CD 379
Cdd:smart00130  81 CE 82
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 203-284 7.03e-37

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 132.89  E-value: 7.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 203 EVECLTCNGESYRGPMDHTESGKICQRWDHQTPHRHKFLPERYPDKGFDDNYCRNPDG-KPRPWCYTLDPDTPWEYCAIK 281
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGdPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1191911036 282 MCA 284
Cdd:cd00108    81 RCE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 300-378 1.16e-36

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 132.05  E-value: 1.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 300 CIQGQGEGYRGTINTIWNGIPCQRWDSQYPHQH-DITPENFKCKDLRENYCRNPDGAESPWCFTTDPNIRVGYCSqIPKC 378
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCD-IPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 206-283 1.23e-36

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


Pssm-ID: 395005  Cd Length: 79  Bit Score: 132.05  E-value: 1.23e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1191911036 206 CLTCNGESYRGPMDHTESGKICQRWDHQTPHRH-KFLPERYPDKGFDDNYCRNPDGKPRPWCYTLDPDTPWEYCAIKMC 283
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHsKYTPENFPAKGLGENYCRNPDGDERPWCYTTDPRVRWEYCDIPRC 79
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 126-203 7.31e-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: 7.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  126 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS-----YRGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRftpesFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIPQ 80


                   ...
gi 1191911036  201 CSE 203
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 383-465 9.98e-34

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


Pssm-ID: 238056  Cd Length: 83  Bit Score: 124.03  E-value: 9.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 383 GQDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 462
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIP 80


                  ...
gi 1191911036 463 RCE 465
Cdd:cd00108    81 RCE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 126-202 2.00e-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: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 126 RNCIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHSY-----RGKDLQENYCRNPRGEEGGPWCFTSNPEVRYEVCDIPQ 200
Cdd:cd00108     2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFnperfPEGLLEENYCRNPDGDPEGPWCYTTDPNVRWEYCDIPR 81


                  ..
gi 1191911036 201 CS 202
Cdd:cd00108    82 CE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 384-466 3.46e-33

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


Pssm-ID: 214527  Cd Length: 83  Bit Score: 122.50  E-value: 3.46e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  384 QDCYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIF-WEPDAsKLNKNYCRNPDDDAHGPWCYTGNPLIPWDYCPIS 462
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLHRFTPeSFPDL-GLEENYCRNPDGDSEGPWCYTTDPNVRWEYCDIP 79


                   ....
gi 1191911036  463 RCEG 466
Cdd:smart00130  80 QCEE 83
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 386-464 4.18e-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: 116.25  E-value: 4.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 386 CYRGNGKNYMGNLSKTRSGLTCSMWDKNMEDLHRHIFWEPDASK-LNKNYCRNPDDDAHgPWCYTGNPLIPWDYCPISRC 464
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSKYTPENFPAKgLGENYCRNPDGDER-PWCYTTDPRVRWEYCDIPRC 79
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 128-201 8.19e-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: 115.48  E-value: 8.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036 128 CIIGKGGSYKGTVSITKSGIKCQPWNSMIPHEHS------YRGKDLQENYCRNPRGEEgGPWCFTSNPEVRYEVCDIPQC 201
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHSkytpenFPAKGLGENYCRNPDGDE-RPWCYTTDPRVRWEYCDIPRC 79
PAN_APPLE cd00129
PAN/APPLE-like domain; present in N-terminal (N) domains of plasminogen/ hepatocyte growth ...
 40-122 1.51e-24

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: 97.77  E-value: 1.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  40 HEFKKSAKTTLIneDPLLKIKTKKMNTADQCANRCIRNkGLPFTCKAFVFDKARKRCLWFPFNSMsSGVKKEFGHEFDLY 119
Cdd:cd00129     2 DEFCKSAGTTLI--KIALKIKTTKANTADECANRCEKN-GLPFSCKAFVFAKARKQCLWFPFNSM-SGVRKEFSHGFDLY 77


                  ...
gi 1191911036 120 ENK 122
Cdd:cd00129    78 ENK 80
PAN_AP_HGF cd01099
Subfamily of PAN/APPLE-like domains; present in N-terminal (N) domains of plasminogen ...
 39-122 3.98e-13

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


Pssm-ID: 238532  Cd Length: 80  Bit Score: 65.18  E-value: 3.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  39 LHEFKKSAktTLINEDPLLKIKTKKMNTADQCANRCIRNKglPFTCKAFVFDKARKRCLWFPFNSMSSGVKKEFGHEFDL 118
Cdd:cd01099     1 LNDFKFVL--VLNKILVSEVKTEITVASLEECLRKCLEET--EFTCRSFNYNYKSKECILSDEDRMSSGVKLLYDSNVDY 76


                  ....
gi 1191911036 119 YENK 122
Cdd:cd01099    77 YENK 80
PAN_AP smart00473
divergent subfamily of APPLE domains; Apple-like domains present in Plasminogen, C. elegans ...
 37-122 6.43e-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: 6.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036   37 NTLHEFKKSAKTTLINEDPllkiKTKKMNTADQCANRCIRNKglpFTCKAFVFDKARKRCLWFPFNSMSSGVKKEFGhEF 116
Cdd:smart00473   1 KSDDCFVRLPNTKLPGFSR----IVISVASLEECASKCLNSN---CSCRSFTYNNGTKGCLLWSESSLGDARLFPSG-GV 72


                   ....*.
gi 1191911036  117 DLYENK 122
Cdd:smart00473  73 DLYEKI 78
PAN_1 pfam00024
PAN domain; The PAN domain contains a conserved core of three disulphide bridges. In some ...
 41-121 7.63e-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: 49.86  E-value: 7.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191911036  41 EFKKSAKTTLINEDpllkIKTKKMNTADQCANRCIRNKGlpftCKAFVFDKARKRCLWFPFNSMSSGVKKEFGHEFDLYE 120
Cdd:pfam00024   2 DFERVPGSSLSGVD----VSTVTVSSAEECAQRCTNEPR----CRSFTYNPKSKKCHLKSSSSGSLPRLKRSDNKVDYYE 73


                  .
gi 1191911036 121 N 121
Cdd:pfam00024  74 K 74
 
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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