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Conserved domains on  [gi|2462596863|ref|XP_054205836|]
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hepatocyte growth factor activator isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 291-526 3.59e-92

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: 281.47  E-value: 3.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 291 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 368
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 369 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 448
Cdd:cd00190    80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596863 449 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 526
Cdd:cd00190   154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 169-250 4.64e-26

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: 101.23  E-value: 4.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 169 CFLGNGTGYRGVASTSASGLSCLAWNSDLLYQ-ELHVDSVGAAALLGLgphAYCRNPDNDERPWCYvVKDSALSWEYCRL 247
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRhSKYTPENFPAKGLGE---NYCRNPDGDERPWCY-TTDPRVRWEYCDI 76


                  ...
gi 2462596863 248 EAC 250
Cdd:pfam00051  77 PRC 79
FN2 super family cl09951
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 3-31 1.72e-09

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


The actual alignment was detected with superfamily member smart00059:

Pssm-ID: 471955  Cd Length: 49  Bit Score: 53.46  E-value: 1.72e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596863    3 HACTSEGSAHRK-WCATTHNYDRDRAWGYC 31
Cdd:smart00059  20 HDCTSEGRSDGMlWCSTTPNYDRDGKWGFC 49
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 83-123 3.63e-09

Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1.


:

Pssm-ID: 238018  Cd Length: 43  Bit Score: 52.33  E-value: 3.63e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462596863  83 EKCFDETRYEYLEGGDRWARVRQGHVEQCECLG--GRTWCEGT 123
Cdd:cd00061     1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCDPV 43
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 45-80 5.11e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 5.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462596863  45 DPCASG-PCLNGGSCSNTqdPQSYHCSCPRAFTGKDC 80
Cdd:cd00054     3 DECASGnPCQNGGTCVNT--VGSYRCSCPPGYTGRNC 37
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 128-161 6.77e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.53  E-value: 6.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462596863 128 CLS-SPCLNGGTCHLIVatGTTVCACPPGFAGRLC 161
Cdd:cd00054     5 CASgNPCQNGGTCVNTV--GSYRCSCPPGYTGRNC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 291-526 3.59e-92

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: 281.47  E-value: 3.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 291 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 368
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 369 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 448
Cdd:cd00190    80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596863 449 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 526
Cdd:cd00190   154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 290-524 7.00e-88

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: 270.32  E-value: 7.00e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863  290 RIIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFsHSPPRDSVSVVLGQHFFNRTTDvTQTFGIEKYIP 367
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrhFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863  368 YTLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVAD 447
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSN 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596863  448 HKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACeKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 524
Cdd:smart00020 154 ATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
291-524 1.41e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 291 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHsppRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 368
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 369 TLYSVFNPsDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENvsGYSSSLREALVPLVADH 448
Cdd:pfam00089  78 PNYNPDTL-DNDIALLKLESP----VTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596863 449 KCSSpeVYGADISPNMLCAGYfdCKSDACQGDSGGPLACEKNgvaYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 524
Cdd:pfam00089 151 TCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 289-529 1.72e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 197.95  E-value: 1.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 289 PRIIGGSSSLPGSHPWLAAIYIGDS----FCAGSLVHTCWVVSAAHCFSHSPPrDSVSVVLGQHffNRTTDVTQTFGIEK 364
Cdd:COG5640    29 PAIVGGTPATVGEYPWMVALQSSNGpsgqFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGST--DLSTSGGTVVKVAR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 365 YIPYTLYSVFNPsDHDLVLIRLkkkgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPL 444
Cdd:COG5640   106 IVVHPDYDPATP-GNDIALLKL-------ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 445 VADHKCSSpevYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 524
Cdd:COG5640   178 VSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254


                  ....*
gi 2462596863 525 NDRIR 529
Cdd:COG5640   255 KSTAG 259
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 169-250 4.64e-26

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: 101.23  E-value: 4.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 169 CFLGNGTGYRGVASTSASGLSCLAWNSDLLYQ-ELHVDSVGAAALLGLgphAYCRNPDNDERPWCYvVKDSALSWEYCRL 247
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRhSKYTPENFPAKGLGE---NYCRNPDGDERPWCY-TTDPRVRWEYCDI 76


                  ...
gi 2462596863 248 EAC 250
Cdd:pfam00051  77 PRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 166-251 4.54e-24

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: 95.91  E-value: 4.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 166 DERCFLGNGTGYRGVASTSASGLSCLAWNSDLLYQelHVDSVGAAALLGLGpHAYCRNPDND-ERPWCYvVKDSALSWEY 244
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQ--HKFNPERFPEGLLE-ENYCRNPDGDpEGPWCY-TTDPNVRWEY 76


                  ....*..
gi 2462596863 245 CRLEACE 251
Cdd:cd00108    77 CDIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 167-252 1.57e-23

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: 94.38  E-value: 1.57e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863  167 ERCFLGNGTGYRGVASTSASGLSCLAWNS--DLLYQELHVDSVGAaallgLGPHAYCRNPDND-ERPWCYvVKDSALSWE 243
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSqtPHLHRFTPESFPDL-----GLEENYCRNPDGDsEGPWCY-TTDPNVRWE 74


                   ....*....
gi 2462596863  244 YCRLEACES 252
Cdd:smart00130  75 YCDIPQCEE 83
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 3-31 1.72e-09

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 53.46  E-value: 1.72e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596863    3 HACTSEGSAHRK-WCATTHNYDRDRAWGYC 31
Cdd:smart00059  20 HDCTSEGRSDGMlWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
3-31 2.94e-09

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 52.57  E-value: 2.94e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596863   3 HACTSEGSAH-RKWCATTHNYDRDRAWGYC 31
Cdd:pfam00040  13 HTCTTDGRRSgRLWCATTANYDGDGKWGYC 42
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 83-123 3.63e-09

Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1.


Pssm-ID: 238018  Cd Length: 43  Bit Score: 52.33  E-value: 3.63e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462596863  83 EKCFDETRYEYLEGGDRWARVRQGHVEQCECLG--GRTWCEGT 123
Cdd:cd00061     1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCDPV 43
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 3-31 3.84e-09

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 52.31  E-value: 3.84e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596863   3 HACTSEGSA-HRKWCATTHNYDRDRAWGYC 31
Cdd:cd00062    19 HDCTTEGSNdGKLWCSTTPNYDRDGKWGYC 48
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 45-80 5.11e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 5.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462596863  45 DPCASG-PCLNGGSCSNTqdPQSYHCSCPRAFTGKDC 80
Cdd:cd00054     3 DECASGnPCQNGGTCVNT--VGSYRCSCPPGYTGRNC 37
FN1 smart00058
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ...
 85-125 1.38e-04

Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, fibronectin. Found also in coagulation factor XII, HGF activator and tissue-type plasminogen activator. In t-PA and fibronectin, this domain type contributes to fibrin-binding.


Pssm-ID: 214494  Cd Length: 45  Bit Score: 39.64  E-value: 1.38e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462596863   85 CFDE-TRYEYLEGgDRWARVRQ-GHVEQCECLG---GRTWCEGTRH 125
Cdd:smart00058   1 CFDEeTGTTYRVG-DTWERPYEgGHVLQCTCLGggrGEWKCDPVPV 45
EGF_CA smart00179
Calcium-binding EGF-like domain;
45-80 1.89e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.07  E-value: 1.89e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462596863   45 DPCAS-GPCLNGGSCSNTQDpqSYHCSCPRAFT-GKDC 80
Cdd:smart00179   3 DECASgNPCQNGGTCVNTVG--SYRCECPPGYTdGRNC 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 47-79 2.03e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.82  E-value: 2.03e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462596863  47 CASGPCLNGGSCSNTqdPQSYHCSCPRAFTGKD 79
Cdd:pfam00008   1 CAPNPCSNGGTCVDT--PGGYTCICPEGYTGKR 31
fn1 pfam00039
Fibronectin type I domain;
85-115 2.87e-03

Fibronectin type I domain;


Pssm-ID: 459644  Cd Length: 40  Bit Score: 35.75  E-value: 2.87e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462596863  85 CFDETRYEYLEGGDRWARVRQ-GHVEQCECLG 115
Cdd:pfam00039   1 CYDPQTGRFYQVGETWERPSQrGHVLQCTCLG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 128-161 6.77e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.53  E-value: 6.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462596863 128 CLS-SPCLNGGTCHLIVatGTTVCACPPGFAGRLC 161
Cdd:cd00054     5 CASgNPCQNGGTCVNTV--GSYRCSCPPGYTGRNC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 291-526 3.59e-92

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: 281.47  E-value: 3.59e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 291 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHSPPRdSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 368
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQYTGGrhFCGGSLISPRWVLTAAHCVYSSAPS-NYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 369 TLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSgYSSSLREALVPLVADH 448
Cdd:cd00190    80 PNYNP-STYDNDIALLKLKRP----VTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462596863 449 KCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWIND 526
Cdd:cd00190   154 ECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRGVLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 290-524 7.00e-88

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: 270.32  E-value: 7.00e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863  290 RIIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFsHSPPRDSVSVVLGQHFFNRTTDvTQTFGIEKYIP 367
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrhFCGGSLISPRWVLTAAHCV-RGSDPSNIRVRLGSHDLSSGEE-GQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863  368 YTLYSVfNPSDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPLVAD 447
Cdd:smart00020  79 HPNYNP-STYDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSN 153

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462596863  448 HKCSSPEVYGADISPNMLCAGYFDCKSDACQGDSGGPLACeKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 524
Cdd:smart00020 154 ATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVC-NDGRWVLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
291-524 1.41e-73

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 233.10  E-value: 1.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 291 IIGGSSSLPGSHPWLAAIYIGDS--FCAGSLVHTCWVVSAAHCFSHsppRDSVSVVLGQHFFNRTTDVTQTFGIEKYIPY 368
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSG---ASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 369 TLYSVFNPsDHDLVLIRLKKKgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENvsGYSSSLREALVPLVADH 448
Cdd:pfam00089  78 PNYNPDTL-DNDIALLKLESP----VTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462596863 449 KCSSpeVYGADISPNMLCAGYfdCKSDACQGDSGGPLACEKNgvaYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 524
Cdd:pfam00089 151 TCRS--AYGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG---ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 289-529 1.72e-59

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 197.95  E-value: 1.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 289 PRIIGGSSSLPGSHPWLAAIYIGDS----FCAGSLVHTCWVVSAAHCFSHSPPrDSVSVVLGQHffNRTTDVTQTFGIEK 364
Cdd:COG5640    29 PAIVGGTPATVGEYPWMVALQSSNGpsgqFCGGTLIAPRWVLTAAHCVDGDGP-SDLRVVIGST--DLSTSGGTVVKVAR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 365 YIPYTLYSVFNPsDHDLVLIRLkkkgdrcATRSQFVQPICLPEPGSTFPAGHKCQIAGWGHLDENVSGYSSSLREALVPL 444
Cdd:COG5640   106 IVVHPDYDPATP-GNDIALLKL-------ATPVPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 445 VADHKCSSpevYGADISPNMLCAGYFDCKSDACQGDSGGPLACEKNGVAYLYGIISWGDGCGRLHKPGVYTRVANYVDWI 524
Cdd:COG5640   178 VSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYRDWI 254


                  ....*
gi 2462596863 525 NDRIR 529
Cdd:COG5640   255 KSTAG 259
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 169-250 4.64e-26

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: 101.23  E-value: 4.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 169 CFLGNGTGYRGVASTSASGLSCLAWNSDLLYQ-ELHVDSVGAAALLGLgphAYCRNPDNDERPWCYvVKDSALSWEYCRL 247
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRhSKYTPENFPAKGLGE---NYCRNPDGDERPWCY-TTDPRVRWEYCDI 76


                  ...
gi 2462596863 248 EAC 250
Cdd:pfam00051  77 PRC 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 166-251 4.54e-24

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: 95.91  E-value: 4.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863 166 DERCFLGNGTGYRGVASTSASGLSCLAWNSDLLYQelHVDSVGAAALLGLGpHAYCRNPDND-ERPWCYvVKDSALSWEY 244
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQ--HKFNPERFPEGLLE-ENYCRNPDGDpEGPWCY-TTDPNVRWEY 76


                  ....*..
gi 2462596863 245 CRLEACE 251
Cdd:cd00108    77 CDIPRCE 83
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 167-252 1.57e-23

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: 94.38  E-value: 1.57e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462596863  167 ERCFLGNGTGYRGVASTSASGLSCLAWNS--DLLYQELHVDSVGAaallgLGPHAYCRNPDND-ERPWCYvVKDSALSWE 243
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSqtPHLHRFTPESFPDL-----GLEENYCRNPDGDsEGPWCY-TTDPNVRWE 74


                   ....*....
gi 2462596863  244 YCRLEACES 252
Cdd:smart00130  75 YCDIPQCEE 83
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 3-31 1.72e-09

Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, fibronectin. Also occurs in coagulation factor XII, 2 type IV collagenases, PDC-109, and cation-independent mannose-6-phosphate and secretory phospholipase A2 receptors. In fibronectin, PDC-109, and the collagenases, this domain contributes to collagen-binding function.


Pssm-ID: 128373  Cd Length: 49  Bit Score: 53.46  E-value: 1.72e-09
                           10        20        30
                   ....*....|....*....|....*....|
gi 2462596863    3 HACTSEGSAHRK-WCATTHNYDRDRAWGYC 31
Cdd:smart00059  20 HDCTSEGRSDGMlWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
3-31 2.94e-09

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 52.57  E-value: 2.94e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596863   3 HACTSEGSAH-RKWCATTHNYDRDRAWGYC 31
Cdd:pfam00040  13 HTCTTDGRRSgRLWCATTANYDGDGKWGYC 42
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 83-123 3.63e-09

Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. FN1 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. FN1 domains also found in coagulation factor XII, HGF activator, and tissue-type plasminogen activator. In tissue plasminogen activator, FN1 domains may form functional fibrin-binding units with EGF-like domains C-terminal to FN1.


Pssm-ID: 238018  Cd Length: 43  Bit Score: 52.33  E-value: 3.63e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2462596863  83 EKCFDETRYEYLEGGDRWARVRQGHVEQCECLG--GRTWCEGT 123
Cdd:cd00061     1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCDPV 43
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 3-31 3.84e-09

Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to form larger domains within fibronectin. Fibronectin, a plasma protein that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin, usually exists as a dimer in plasma and as an insoluble multimer in extracellular matrices. Dimers of nearly identical subunits are linked by a disulfide bond close to their C-terminus. Fibronectin is composed of 3 types of modules, FN1,FN2 and FN3. The collagen binding domain contains four FN1 and two FN2 repeats.


Pssm-ID: 238019  Cd Length: 48  Bit Score: 52.31  E-value: 3.84e-09
                          10        20        30
                  ....*....|....*....|....*....|
gi 2462596863   3 HACTSEGSA-HRKWCATTHNYDRDRAWGYC 31
Cdd:cd00062    19 HDCTTEGSNdGKLWCSTTPNYDRDGKWGYC 48
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 45-80 5.11e-06

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.39  E-value: 5.11e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462596863  45 DPCASG-PCLNGGSCSNTqdPQSYHCSCPRAFTGKDC 80
Cdd:cd00054     3 DECASGnPCQNGGTCVNT--VGSYRCSCPPGYTGRNC 37
FN1 smart00058
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ...
 85-125 1.38e-04

Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, fibronectin. Found also in coagulation factor XII, HGF activator and tissue-type plasminogen activator. In t-PA and fibronectin, this domain type contributes to fibrin-binding.


Pssm-ID: 214494  Cd Length: 45  Bit Score: 39.64  E-value: 1.38e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2462596863   85 CFDE-TRYEYLEGgDRWARVRQ-GHVEQCECLG---GRTWCEGTRH 125
Cdd:smart00058   1 CFDEeTGTTYRVG-DTWERPYEgGHVLQCTCLGggrGEWKCDPVPV 45
EGF_CA smart00179
Calcium-binding EGF-like domain;
45-80 1.89e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.07  E-value: 1.89e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2462596863   45 DPCAS-GPCLNGGSCSNTQDpqSYHCSCPRAFT-GKDC 80
Cdd:smart00179   3 DECASgNPCQNGGTCVNTVG--SYRCECPPGYTdGRNC 38
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 47-79 2.03e-03

EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 394967  Cd Length: 31  Bit Score: 35.82  E-value: 2.03e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462596863  47 CASGPCLNGGSCSNTqdPQSYHCSCPRAFTGKD 79
Cdd:pfam00008   1 CAPNPCSNGGTCVDT--PGGYTCICPEGYTGKR 31
fn1 pfam00039
Fibronectin type I domain;
85-115 2.87e-03

Fibronectin type I domain;


Pssm-ID: 459644  Cd Length: 40  Bit Score: 35.75  E-value: 2.87e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462596863  85 CFDETRYEYLEGGDRWARVRQ-GHVEQCECLG 115
Cdd:pfam00039   1 CYDPQTGRFYQVGETWERPSQrGHVLQCTCLG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 128-161 6.77e-03

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 34.53  E-value: 6.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2462596863 128 CLS-SPCLNGGTCHLIVatGTTVCACPPGFAGRLC 161
Cdd:cd00054     5 CASgNPCQNGGTCVNTV--GSYRCSCPPGYTGRNC 37
 
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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