NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|655663707|ref|XP_008253688|]
View 

coagulation factor XII isoform X2 [Oryctolagus cuniculus]

Protein Classification

KR and Tryp_SPc domain-containing protein( domain architecture ID 10812493)

protein containing domains FN2, FN1, KR, and Tryp_SPc

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 372-561 8.61e-59

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: 195.57  E-value: 8.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 372 VVGGLVALPGAHPYMAALY--WGHNFCAGSLIDSCWVLTAAHCLQDRPaPEELTVVLGQSRHNQSCEQCQTLAVRSYRLH 449
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 450 EAFSPNSYQHDLALLRLRESADgscalLSPYVQPVCLPSGAAQTPEskTALCEVAGWGHQYEGAEeYSSFLQEAQVPFIP 529
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVT-----LSDNVRPICLPSSGYNLPA--GTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVS 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 655663707 530 LERCSAPDVHGAAILPGMLCAGFLEGGTDACQ 561
Cdd:cd00190  152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQ 183
KR super family cl00100
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 217-295 9.20e-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.


The actual alignment was detected with superfamily member pfam00051:

Pssm-ID: 412161  Cd Length: 79  Bit Score: 95.07  E-value: 9.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707  217 CYKDRGLSYRGLARTTLSGASCQSWASEATYRN--MTAEQALSRGLGDhAFCRNPDNDIRPWCFVLSgDRLSWEYCDLAP 294
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLGE-NYCRNPDGDERPWCYTTD-PRVRWEYCDIPR 78


                  .
gi 655663707  295 C 295
Cdd:pfam00051  79 C 79
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 41-88 1.82e-19

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: 81.97  E-value: 1.82e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 655663707  41 TVTGEPCHFPFQYHRQLYHTCIHKGRPGPRPWCATTPNFDRDQQWAHC 88
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 96-131 1.15e-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: 45.32  E-value: 1.15e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 655663707  96 DHCSKHSPCHKGGTCVNTPRGPHCFCPGHLTGKHCQ 131
Cdd:cd00054    3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 133-171 3.15e-06

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: 44.25  E-value: 3.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 655663707 133 EKCFEPQLHRFFHENDMWYRFERAGVAKCRCKG--PDAHCK 171
Cdd:cd00061    1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCD 41
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 178-208 1.04e-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: 36.59  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 655663707  178 CPTNKCLNQGSCLVAEGHHLCHCRPPYTGPF 208
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 372-561 8.61e-59

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: 195.57  E-value: 8.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 372 VVGGLVALPGAHPYMAALY--WGHNFCAGSLIDSCWVLTAAHCLQDRPaPEELTVVLGQSRHNQSCEQCQTLAVRSYRLH 449
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 450 EAFSPNSYQHDLALLRLRESADgscalLSPYVQPVCLPSGAAQTPEskTALCEVAGWGHQYEGAEeYSSFLQEAQVPFIP 529
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVT-----LSDNVRPICLPSSGYNLPA--GTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVS 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 655663707 530 LERCSAPDVHGAAILPGMLCAGFLEGGTDACQ 561
Cdd:cd00190  152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQ 183
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 371-561 2.77e-58

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: 194.05  E-value: 2.77e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707   371 RVVGGLVALPGAHPYMAALY--WGHNFCAGSLIDSCWVLTAAHCLQDRPaPEELTVVLGQSRHNQScEQCQTLAVRSYRL 448
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQygGGRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707   449 HEAFSPNSYQHDLALLRLRESADgscalLSPYVQPVCLPSGAAQTPESKTalCEVAGWGHQYEGAEEYSSFLQEAQVPFI 528
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVT-----LSDNVRPICLPSSNYNVPAGTT--CTVSGWGRTSEGAGSLPDTLQEVNVPIV 151

                          170       180       190
                   ....*....|....*....|....*....|...
gi 655663707   529 PLERCSAPDVHGAAILPGMLCAGFLEGGTDACQ 561
Cdd:smart00020 152 SNATCRRAYSGGGAITDNMLCAGGLEGGKDACQ 184
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 370-561 3.86e-41

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 149.41  E-value: 3.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 370 SRVVGGLVALPGAHPYMAALY-----WGHnFCAGSLIDSCWVLTAAHCLQDrPAPEELTVVLGqsRHNQSCEQCQTLAVR 444
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQssngpSGQ-FCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIG--STDLSTSGGTVVKVA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 445 SYRLHEAFSPNSYQHDLALLRLRESADGscallspyVQPVCLPSGAAQTPESKTALceVAGWGHQYEGAEEYSSFLQEAQ 524
Cdd:COG5640  105 RIVVHPDYDPATPGNDIALLKLATPVPG--------VAPAPLATSADAAAPGTPAT--VAGWGRTSEGPGSQSGTLRKAD 174

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 655663707 525 VPFIPLERCSApdvHGAAILPGMLCAGFLEGGTDACQ 561
Cdd:COG5640  175 VPVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQ 208
Trypsin pfam00089
Trypsin;
372-561 5.52e-40

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 144.89  E-value: 5.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707  372 VVGGLVALPGAHPYMAALYWGHN--FCAGSLIDSCWVLTAAHCLQDRPApeeLTVVLGQSRHNQSCEQCQTLAVRSYRLH 449
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707  450 EAFSPNSYQHDLALLRLRESADgscalLSPYVQPVCLPSGAAQTPEskTALCEVAGWGHQYEGAEEYSsfLQEAQVPFIP 529
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVT-----LGDTVRPICLPDASSDLPV--GTTCTVSGWGNTKTLGPSDT--LQEVTVPVVS 148

                         170       180       190
                  ....*....|....*....|....*....|..
gi 655663707  530 LERCSApdVHGAAILPGMLCAGFleGGTDACQ 561
Cdd:pfam00089 149 RETCRS--AYGGTVTDTMICAGA--GGKDACQ 176
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 217-295 9.20e-24

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: 95.07  E-value: 9.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707  217 CYKDRGLSYRGLARTTLSGASCQSWASEATYRN--MTAEQALSRGLGDhAFCRNPDNDIRPWCFVLSgDRLSWEYCDLAP 294
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLGE-NYCRNPDGDERPWCYTTD-PRVRWEYCDIPR 78


                  .
gi 655663707  295 C 295
Cdd:pfam00051  79 C 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 215-295 3.14e-21

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: 87.82  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 215 ANCYKDRGLSYRGLARTTLSGASCQSWASEA-TYRNMTAEQALSrGLGDHAFCRNPDNDI-RPWCFVlSGDRLSWEYCDL 292
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLpHQHKFNPERFPE-GLLEENYCRNPDGDPeGPWCYT-TDPNVRWEYCDI 79


                 ...
gi 655663707 293 APC 295
Cdd:cd00108   80 PRC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 216-295 2.07e-20

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: 85.52  E-value: 2.07e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707   216 NCYKDRGLSYRGLARTTLSGASCQSWASEATY-RNMTAEQALSRGLGdHAFCRNPDNDI-RPWCFVLsGDRLSWEYCDLA 293
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHlHRFTPESFPDLGLE-ENYCRNPDGDSeGPWCYTT-DPNVRWEYCDIP 79


                   ..
gi 655663707   294 PC 295
Cdd:smart00130  80 QC 81
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 41-88 1.82e-19

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: 81.97  E-value: 1.82e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 655663707  41 TVTGEPCHFPFQYHRQLYHTCIHKGRPGPRPWCATTPNFDRDQQWAHC 88
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 41-88 5.79e-19

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: 80.42  E-value: 5.79e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 655663707    41 TVTGEPCHFPFQYHRQLYHTCIHKGRPGPRPWCATTPNFDRDQQWAHC 88
Cdd:smart00059   2 NSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
47-88 2.45e-17

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 75.68  E-value: 2.45e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 655663707   47 CHFPFQYHRQLYHTCIHKGRPGPRPWCATTPNFDRDQQWAHC 88
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 96-131 1.15e-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: 45.32  E-value: 1.15e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 655663707  96 DHCSKHSPCHKGGTCVNTPRGPHCFCPGHLTGKHCQ 131
Cdd:cd00054    3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 133-171 3.15e-06

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: 44.25  E-value: 3.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 655663707 133 EKCFEPQLHRFFHENDMWYRFERAGVAKCRCKG--PDAHCK 171
Cdd:cd00061    1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCD 41
fn1 pfam00039
Fibronectin type I domain;
135-170 6.29e-06

Fibronectin type I domain;


Pssm-ID: 459644  Cd Length: 40  Bit Score: 43.07  E-value: 6.29e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 655663707  135 CFEPQLHRFFHENDMWYRFERAG-VAKCRCKG---PDAHC 170
Cdd:pfam00039   1 CYDPQTGRFYQVGETWERPSQRGhVLQCTCLGnggGEIRC 40
EGF_CA smart00179
Calcium-binding EGF-like domain;
96-131 9.45e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 9.45e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 655663707    96 DHCSKHSPCHKGGTCVNTPRGPHCFCP-GHLTGKHCQ 131
Cdd:smart00179   3 DECASGNPCQNGGTCVNTVGSYRCECPpGYTDGRNCE 39
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 98-129 5.13e-04

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: 37.75  E-value: 5.13e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 655663707   98 CSKHsPCHKGGTCVNTPRGPHCFCPGHLTGKH 129
Cdd:pfam00008   1 CAPN-PCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 178-208 1.04e-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: 36.59  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 655663707  178 CPTNKCLNQGSCLVAEGHHLCHCRPPYTGPF 208
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 372-561 8.61e-59

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: 195.57  E-value: 8.61e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 372 VVGGLVALPGAHPYMAALY--WGHNFCAGSLIDSCWVLTAAHCLQDRPaPEELTVVLGQSRHNQSCEQCQTLAVRSYRLH 449
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 450 EAFSPNSYQHDLALLRLRESADgscalLSPYVQPVCLPSGAAQTPEskTALCEVAGWGHQYEGAEeYSSFLQEAQVPFIP 529
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVT-----LSDNVRPICLPSSGYNLPA--GTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVS 151

                        170       180       190
                 ....*....|....*....|....*....|..
gi 655663707 530 LERCSAPDVHGAAILPGMLCAGFLEGGTDACQ 561
Cdd:cd00190  152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQ 183
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 371-561 2.77e-58

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: 194.05  E-value: 2.77e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707   371 RVVGGLVALPGAHPYMAALY--WGHNFCAGSLIDSCWVLTAAHCLQDRPaPEELTVVLGQSRHNQScEQCQTLAVRSYRL 448
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQygGGRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707   449 HEAFSPNSYQHDLALLRLRESADgscalLSPYVQPVCLPSGAAQTPESKTalCEVAGWGHQYEGAEEYSSFLQEAQVPFI 528
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEPVT-----LSDNVRPICLPSSNYNVPAGTT--CTVSGWGRTSEGAGSLPDTLQEVNVPIV 151

                          170       180       190
                   ....*....|....*....|....*....|...
gi 655663707   529 PLERCSAPDVHGAAILPGMLCAGFLEGGTDACQ 561
Cdd:smart00020 152 SNATCRRAYSGGGAITDNMLCAGGLEGGKDACQ 184
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 370-561 3.86e-41

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 149.41  E-value: 3.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 370 SRVVGGLVALPGAHPYMAALY-----WGHnFCAGSLIDSCWVLTAAHCLQDrPAPEELTVVLGqsRHNQSCEQCQTLAVR 444
Cdd:COG5640   29 PAIVGGTPATVGEYPWMVALQssngpSGQ-FCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIG--STDLSTSGGTVVKVA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 445 SYRLHEAFSPNSYQHDLALLRLRESADGscallspyVQPVCLPSGAAQTPESKTALceVAGWGHQYEGAEEYSSFLQEAQ 524
Cdd:COG5640  105 RIVVHPDYDPATPGNDIALLKLATPVPG--------VAPAPLATSADAAAPGTPAT--VAGWGRTSEGPGSQSGTLRKAD 174

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 655663707 525 VPFIPLERCSApdvHGAAILPGMLCAGFLEGGTDACQ 561
Cdd:COG5640  175 VPVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQ 208
Trypsin pfam00089
Trypsin;
372-561 5.52e-40

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 144.89  E-value: 5.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707  372 VVGGLVALPGAHPYMAALYWGHN--FCAGSLIDSCWVLTAAHCLQDRPApeeLTVVLGQSRHNQSCEQCQTLAVRSYRLH 449
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707  450 EAFSPNSYQHDLALLRLRESADgscalLSPYVQPVCLPSGAAQTPEskTALCEVAGWGHQYEGAEEYSsfLQEAQVPFIP 529
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESPVT-----LGDTVRPICLPDASSDLPV--GTTCTVSGWGNTKTLGPSDT--LQEVTVPVVS 148

                         170       180       190
                  ....*....|....*....|....*....|..
gi 655663707  530 LERCSApdVHGAAILPGMLCAGFleGGTDACQ 561
Cdd:pfam00089 149 RETCRS--AYGGTVTDTMICAGA--GGKDACQ 176
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 217-295 9.20e-24

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: 95.07  E-value: 9.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707  217 CYKDRGLSYRGLARTTLSGASCQSWASEATYRN--MTAEQALSRGLGDhAFCRNPDNDIRPWCFVLSgDRLSWEYCDLAP 294
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLGE-NYCRNPDGDERPWCYTTD-PRVRWEYCDIPR 78


                  .
gi 655663707  295 C 295
Cdd:pfam00051  79 C 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 215-295 3.14e-21

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: 87.82  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 215 ANCYKDRGLSYRGLARTTLSGASCQSWASEA-TYRNMTAEQALSrGLGDHAFCRNPDNDI-RPWCFVlSGDRLSWEYCDL 292
Cdd:cd00108    2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLpHQHKFNPERFPE-GLLEENYCRNPDGDPeGPWCYT-TDPNVRWEYCDI 79


                 ...
gi 655663707 293 APC 295
Cdd:cd00108   80 PRC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 216-295 2.07e-20

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: 85.52  E-value: 2.07e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707   216 NCYKDRGLSYRGLARTTLSGASCQSWASEATY-RNMTAEQALSRGLGdHAFCRNPDNDI-RPWCFVLsGDRLSWEYCDLA 293
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHlHRFTPESFPDLGLE-ENYCRNPDGDSeGPWCYTT-DPNVRWEYCDIP 79


                   ..
gi 655663707   294 PC 295
Cdd:smart00130  80 QC 81
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 41-88 1.82e-19

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: 81.97  E-value: 1.82e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 655663707  41 TVTGEPCHFPFQYHRQLYHTCIHKGRPGPRPWCATTPNFDRDQQWAHC 88
Cdd:cd00062    1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 41-88 5.79e-19

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: 80.42  E-value: 5.79e-19
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 655663707    41 TVTGEPCHFPFQYHRQLYHTCIHKGRPGPRPWCATTPNFDRDQQWAHC 88
Cdd:smart00059   2 NSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
47-88 2.45e-17

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 75.68  E-value: 2.45e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 655663707   47 CHFPFQYHRQLYHTCIHKGRPGPRPWCATTPNFDRDQQWAHC 88
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 392-473 2.74e-07

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 51.22  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655663707 392 GHNFCAGSLIDSCWVLTAAHCLQDRP---APEELTVVLGQSRhnqscEQCQTLAVRSYRLHEAFSPN-SYQHDLALLRLR 467
Cdd:COG3591   10 GGGVCTGTLIGPNLVLTAGHCVYDGAgggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASgDAGYDYALLRLD 84


                 ....*.
gi 655663707 468 ESADGS 473
Cdd:COG3591   85 EPLGDT 90
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 96-131 1.15e-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: 45.32  E-value: 1.15e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 655663707  96 DHCSKHSPCHKGGTCVNTPRGPHCFCPGHLTGKHCQ 131
Cdd:cd00054    3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 133-171 3.15e-06

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: 44.25  E-value: 3.15e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 655663707 133 EKCFEPQLHRFFHENDMWYRFERAGVAKCRCKG--PDAHCK 171
Cdd:cd00061    1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCD 41
fn1 pfam00039
Fibronectin type I domain;
135-170 6.29e-06

Fibronectin type I domain;


Pssm-ID: 459644  Cd Length: 40  Bit Score: 43.07  E-value: 6.29e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 655663707  135 CFEPQLHRFFHENDMWYRFERAG-VAKCRCKG---PDAHC 170
Cdd:pfam00039   1 CYDPQTGRFYQVGETWERPSQRGhVLQCTCLGnggGEIRC 40
EGF_CA smart00179
Calcium-binding EGF-like domain;
96-131 9.45e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 42.62  E-value: 9.45e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 655663707    96 DHCSKHSPCHKGGTCVNTPRGPHCFCP-GHLTGKHCQ 131
Cdd:smart00179   3 DECASGNPCQNGGTCVNTVGSYRCECPpGYTDGRNCE 39
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 98-131 2.08e-04

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 39.00  E-value: 2.08e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 655663707  98 CSKHSPCHKGGTCVNTPRGPHCFCPGHLTG-KHCQ 131
Cdd:cd00053    2 CAASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 98-129 5.13e-04

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: 37.75  E-value: 5.13e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 655663707   98 CSKHsPCHKGGTCVNTPRGPHCFCPGHLTGKH 129
Cdd:pfam00008   1 CAPN-PCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 178-208 1.04e-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: 36.59  E-value: 1.04e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 655663707  178 CPTNKCLNQGSCLVAEGHHLCHCRPPYTGPF 208
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH