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Conserved domains on  [gi|1335114667|ref|XP_023608941|]
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coagulation factor XII [Myotis lucifugus]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 11249616)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions

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 ...
 376-615 4.51e-90

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: 278.39  E-value: 4.51e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 376 VVGGLVALPGAHPYIAALY--WGHSFCAGSLIAPCWVLTAAHCLQNRPaPEELTVVLGQDRHNQSCAQCQVLAVRAYHLH 453
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 454 EDFSPVTYQHDLALLRLQESqdgrcARRSPAVGPVCLPSSAARPAEPEaaLCEIAGWGHQFEGAEeYASFLQEAQVPLIP 533
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRP-----VTLSDNVRPICLPSSGYNLPAGT--TCTVSGWGRTSEGGP-LPDVLQEVNVPIVS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 534 HKDCSNPEMHGNAFYPGMLCAGYPDGGTDACQGDSGGPLVCEDEDRGlTLRGIISWGSGCGDRNKPGVYTDVANYLTWIR 613
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRG-VLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230


                  ..
gi 1335114667 614 EH 615
Cdd:cd00190   231 KT 232
KR super family cl00100
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 217-295 8.08e-23

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: 92.37  E-value: 8.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 217 CYEGLGFGYRGAAGTTISGARCQPWSSETTYQN--LTAEQALNWGLGhHAFCRNPDNDTQPWCFVwSGNRLSWEYCDLAR 294
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLG-ENYCRNPDGDERPWCYT-TDPRVRWEYCDIPR 78


                  .
gi 1335114667 295 C 295
Cdd:pfam00051  79 C 79
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 41-88 1.97e-18

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: 78.88  E-value: 1.97e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1335114667   41 TVTGEPCYFPFQYRRQLYHQCTRRGRIGFRPWCATTPNFDQDQRWAYC 88
Cdd:smart00059   2 NSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 96-131 4.01e-09

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: 52.25  E-value: 4.01e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1335114667  96 DHCSTHNPCQRGGTCVNMPDGPRCICPEHFTGKHCQ 131
Cdd:cd00054     3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 133-173 1.49e-08

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: 50.79  E-value: 1.49e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1335114667 133 EKCFEPQLLQFFHENETWHRLEPAGMAECQCQG--PQAHCKPL 173
Cdd:cd00061     1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCDPV 43
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 178-208 9.33e-06

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: 42.76  E-value: 9.33e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1335114667 178 CSNNPCLHGGRCLEAEGHRLCSCPEGYAGRF 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 ...
 376-615 4.51e-90

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: 278.39  E-value: 4.51e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 376 VVGGLVALPGAHPYIAALY--WGHSFCAGSLIAPCWVLTAAHCLQNRPaPEELTVVLGQDRHNQSCAQCQVLAVRAYHLH 453
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 454 EDFSPVTYQHDLALLRLQESqdgrcARRSPAVGPVCLPSSAARPAEPEaaLCEIAGWGHQFEGAEeYASFLQEAQVPLIP 533
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRP-----VTLSDNVRPICLPSSGYNLPAGT--TCTVSGWGRTSEGGP-LPDVLQEVNVPIVS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 534 HKDCSNPEMHGNAFYPGMLCAGYPDGGTDACQGDSGGPLVCEDEDRGlTLRGIISWGSGCGDRNKPGVYTDVANYLTWIR 613
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRG-VLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230


                  ..
gi 1335114667 614 EH 615
Cdd:cd00190   231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 375-612 6.24e-86

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: 267.62  E-value: 6.24e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667  375 RVVGGLVALPGAHPYIAALY--WGHSFCAGSLIAPCWVLTAAHCLQNRPaPEELTVVLGqdRHNQSCAQ-CQVLAVRAYH 451
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQygGGRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLG--SHDLSSGEeGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667  452 LHEDFSPVTYQHDLALLRLQESqdgrcARRSPAVGPVCLPSSAARPAEPEAalCEIAGWGHQFEGAEEYASFLQEAQVPL 531
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEP-----VTLSDNVRPICLPSSNYNVPAGTT--CTVSGWGRTSEGAGSLPDTLQEVNVPI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667  532 IPHKDCSNPEMHGNAFYPGMLCAGYPDGGTDACQGDSGGPLVCEDEDRglTLRGIISWGSGCGDRNKPGVYTDVANYLTW 611
Cdd:smart00020 151 VSNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRW--VLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228


                   .
gi 1335114667  612 I 612
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
376-612 8.51e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 209.61  E-value: 8.51e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 376 VVGGLVALPGAHPYIAALYWGHS--FCAGSLIAPCWVLTAAHCLQNRPApeeLTVVLGQDRHNQSCAQCQVLAVRAYHLH 453
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 454 EDFSPVTYQHDLALLRLQESqdgrcARRSPAVGPVCLPSSAARPAEPEAalCEIAGWGHQFEGaeEYASFLQEAQVPLIP 533
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESP-----VTLGDTVRPICLPDASSDLPVGTT--CTVSGWGNTKTL--GPSDTLQEVTVPVVS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335114667 534 HKDCSNPemHGNAFYPGMLCAGYpdGGTDACQGDSGGPLVCEDEdrglTLRGIISWGSGCGDRNKPGVYTDVANYLTWI 612
Cdd:pfam00089 149 RETCRSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 375-618 2.56e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.89  E-value: 2.56e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 375 RVVGGLVALPGAHPYIAALY-----WGHsFCAGSLIAPCWVLTAAHCLQNrPAPEELTVVLGQDRHNQSCAQcqVLAVRA 449
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQssngpSGQ-FCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGT--VVKVAR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 450 YHLHEDFSPVTYQHDLALLRLqesqdgrcARRSPAVGPVCLPSSAARPAEPEAALceIAGWGHQFEGAEEYASFLQEAQV 529
Cdd:COG5640   106 IVVHPDYDPATPGNDIALLKL--------ATPVPGVAPAPLATSADAAAPGTPAT--VAGWGRTSEGPGSQSGTLRKADV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 530 PLIPHKDCSNpemHGNAFYPGMLCAGYPDGGTDACQGDSGGPLVcEDEDRGLTLRGIISWGSGCGDRNKPGVYTDVANYL 609
Cdd:COG5640   176 PVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251


                  ....*....
gi 1335114667 610 TWIREHMAS 618
Cdd:COG5640   252 DWIKSTAGG 260
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 217-295 8.08e-23

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: 92.37  E-value: 8.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 217 CYEGLGFGYRGAAGTTISGARCQPWSSETTYQN--LTAEQALNWGLGhHAFCRNPDNDTQPWCFVwSGNRLSWEYCDLAR 294
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLG-ENYCRNPDGDERPWCYT-TDPRVRWEYCDIPR 78


                  .
gi 1335114667 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 ...
 214-295 1.48e-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: 88.97  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 214 EASCYEGLGFGYRGAAGTTISGARCQPWSSET-TYQNLTAEQALNWGLGhHAFCRNPDND-TQPWCFVWSGNrLSWEYCD 291
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLpHQHKFNPERFPEGLLE-ENYCRNPDGDpEGPWCYTTDPN-VRWEYCD 78


                  ....
gi 1335114667 292 LARC 295
Cdd:cd00108    79 IPRC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 217-295 4.87e-21

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: 87.45  E-value: 4.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667  217 CYEGLGFGYRGAAGTTISGARCQPWSSETTYQ-NLTAEQALNWGLGhHAFCRNPDND-TQPWCFVwSGNRLSWEYCDLAR 294
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLhRFTPESFPDLGLE-ENYCRNPDGDsEGPWCYT-TDPNVRWEYCDIPQ 80


                   .
gi 1335114667  295 C 295
Cdd:smart00130  81 C 81
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 41-88 1.97e-18

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: 78.88  E-value: 1.97e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1335114667   41 TVTGEPCYFPFQYRRQLYHQCTRRGRIGFRPWCATTPNFDQDQRWAYC 88
Cdd:smart00059   2 NSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 41-88 4.09e-18

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: 78.12  E-value: 4.09e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1335114667  41 TVTGEPCYFPFQYRRQLYHQCTRRGRIGFRPWCATTPNFDQDQRWAYC 88
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
47-88 9.52e-17

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 74.14  E-value: 9.52e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1335114667  47 CYFPFQYRRQLYHQCTRRGRIGFRPWCATTPNFDQDQRWAYC 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 4.01e-09

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: 52.25  E-value: 4.01e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1335114667  96 DHCSTHNPCQRGGTCVNMPDGPRCICPEHFTGKHCQ 131
Cdd:cd00054     3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 133-173 1.49e-08

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: 50.79  E-value: 1.49e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1335114667 133 EKCFEPQLLQFFHENETWHRLEPAGMAECQCQG--PQAHCKPL 173
Cdd:cd00061     1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCDPV 43
EGF_CA smart00179
Calcium-binding EGF-like domain;
96-131 1.03e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 1.03e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1335114667   96 DHCSTHNPCQRGGTCVNMPDGPRCICPEHFT-GKHCQ 131
Cdd:smart00179   3 DECASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
fn1 pfam00039
Fibronectin type I domain;
135-170 1.77e-06

Fibronectin type I domain;


Pssm-ID: 459644  Cd Length: 40  Bit Score: 45.00  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1335114667 135 CFEPQLLQFFHENETWHRLEPAG-MAECQCQG---PQAHC 170
Cdd:pfam00039   1 CYDPQTGRFYQVGETWERPSQRGhVLQCTCLGnggGEIRC 40
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 178-208 9.33e-06

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: 42.76  E-value: 9.33e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1335114667 178 CSNNPCLHGGRCLEAEGHRLCSCPEGYAGRF 208
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
FN1 smart00058
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ...
 135-175 1.32e-05

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: 42.34  E-value: 1.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1335114667  135 CFEPQLLQFFHENETWHRLEPAGMAE-CQCQGPQ---AHCKPLAS 175
Cdd:smart00058   1 CFDEETGTTYRVGDTWERPYEGGHVLqCTCLGGGrgeWKCDPVPV 45
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 102-129 4.94e-05

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: 40.44  E-value: 4.94e-05
                          10        20
                  ....*....|....*....|....*...
gi 1335114667 102 NPCQRGGTCVNMPDGPRCICPEHFTGKH 129
Cdd:pfam00008   4 NPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 179-209 3.60e-04

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: 38.39  E-value: 3.60e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1335114667 179 SNNPCLHGGRCLEAEGHRLCSCPEGYAGRFC 209
Cdd:cd00054     7 SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 376-615 4.51e-90

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: 278.39  E-value: 4.51e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 376 VVGGLVALPGAHPYIAALY--WGHSFCAGSLIAPCWVLTAAHCLQNRPaPEELTVVLGQDRHNQSCAQCQVLAVRAYHLH 453
Cdd:cd00190     1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 454 EDFSPVTYQHDLALLRLQESqdgrcARRSPAVGPVCLPSSAARPAEPEaaLCEIAGWGHQFEGAEeYASFLQEAQVPLIP 533
Cdd:cd00190    80 PNYNPSTYDNDIALLKLKRP-----VTLSDNVRPICLPSSGYNLPAGT--TCTVSGWGRTSEGGP-LPDVLQEVNVPIVS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 534 HKDCSNPEMHGNAFYPGMLCAGYPDGGTDACQGDSGGPLVCEDEDRGlTLRGIISWGSGCGDRNKPGVYTDVANYLTWIR 613
Cdd:cd00190   152 NAECKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRG-VLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQ 230


                  ..
gi 1335114667 614 EH 615
Cdd:cd00190   231 KT 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 375-612 6.24e-86

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: 267.62  E-value: 6.24e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667  375 RVVGGLVALPGAHPYIAALY--WGHSFCAGSLIAPCWVLTAAHCLQNRPaPEELTVVLGqdRHNQSCAQ-CQVLAVRAYH 451
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQygGGRHFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLG--SHDLSSGEeGQVIKVSKVI 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667  452 LHEDFSPVTYQHDLALLRLQESqdgrcARRSPAVGPVCLPSSAARPAEPEAalCEIAGWGHQFEGAEEYASFLQEAQVPL 531
Cdd:smart00020  78 IHPNYNPSTYDNDIALLKLKEP-----VTLSDNVRPICLPSSNYNVPAGTT--CTVSGWGRTSEGAGSLPDTLQEVNVPI 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667  532 IPHKDCSNPEMHGNAFYPGMLCAGYPDGGTDACQGDSGGPLVCEDEDRglTLRGIISWGSGCGDRNKPGVYTDVANYLTW 611
Cdd:smart00020 151 VSNATCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRW--VLVGIVSWGSGCARPGKPGVYTRVSSYLDW 228


                   .
gi 1335114667  612 I 612
Cdd:smart00020 229 I 229
Trypsin pfam00089
Trypsin;
376-612 8.51e-64

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 209.61  E-value: 8.51e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 376 VVGGLVALPGAHPYIAALYWGHS--FCAGSLIAPCWVLTAAHCLQNRPApeeLTVVLGQDRHNQSCAQCQVLAVRAYHLH 453
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 454 EDFSPVTYQHDLALLRLQESqdgrcARRSPAVGPVCLPSSAARPAEPEAalCEIAGWGHQFEGaeEYASFLQEAQVPLIP 533
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESP-----VTLGDTVRPICLPDASSDLPVGTT--CTVSGWGNTKTL--GPSDTLQEVTVPVVS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1335114667 534 HKDCSNPemHGNAFYPGMLCAGYpdGGTDACQGDSGGPLVCEDEdrglTLRGIISWGSGCGDRNKPGVYTDVANYLTWI 612
Cdd:pfam00089 149 RETCRSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 375-618 2.56e-63

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 209.89  E-value: 2.56e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 375 RVVGGLVALPGAHPYIAALY-----WGHsFCAGSLIAPCWVLTAAHCLQNrPAPEELTVVLGQDRHNQSCAQcqVLAVRA 449
Cdd:COG5640    30 AIVGGTPATVGEYPWMVALQssngpSGQ-FCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTSGGT--VVKVAR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 450 YHLHEDFSPVTYQHDLALLRLqesqdgrcARRSPAVGPVCLPSSAARPAEPEAALceIAGWGHQFEGAEEYASFLQEAQV 529
Cdd:COG5640   106 IVVHPDYDPATPGNDIALLKL--------ATPVPGVAPAPLATSADAAAPGTPAT--VAGWGRTSEGPGSQSGTLRKADV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 530 PLIPHKDCSNpemHGNAFYPGMLCAGYPDGGTDACQGDSGGPLVcEDEDRGLTLRGIISWGSGCGDRNKPGVYTDVANYL 609
Cdd:COG5640   176 PVVSDATCAA---YGGFDGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGGGPCAAGYPGVYTRVSAYR 251


                  ....*....
gi 1335114667 610 TWIREHMAS 618
Cdd:COG5640   252 DWIKSTAGG 260
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 217-295 8.08e-23

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: 92.37  E-value: 8.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 217 CYEGLGFGYRGAAGTTISGARCQPWSSETTYQN--LTAEQALNWGLGhHAFCRNPDNDTQPWCFVwSGNRLSWEYCDLAR 294
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLG-ENYCRNPDGDERPWCYT-TDPRVRWEYCDIPR 78


                  .
gi 1335114667 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 ...
 214-295 1.48e-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: 88.97  E-value: 1.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 214 EASCYEGLGFGYRGAAGTTISGARCQPWSSET-TYQNLTAEQALNWGLGhHAFCRNPDND-TQPWCFVWSGNrLSWEYCD 291
Cdd:cd00108     1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLpHQHKFNPERFPEGLLE-ENYCRNPDGDpEGPWCYTTDPN-VRWEYCD 78


                  ....
gi 1335114667 292 LARC 295
Cdd:cd00108    79 IPRC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 217-295 4.87e-21

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: 87.45  E-value: 4.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667  217 CYEGLGFGYRGAAGTTISGARCQPWSSETTYQ-NLTAEQALNWGLGhHAFCRNPDND-TQPWCFVwSGNRLSWEYCDLAR 294
Cdd:smart00130   3 CYAGNGESYRGTVSVTKSGKPCQRWDSQTPHLhRFTPESFPDLGLE-ENYCRNPDGDsEGPWCYT-TDPNVRWEYCDIPQ 80


                   .
gi 1335114667  295 C 295
Cdd:smart00130  81 C 81
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 41-88 1.97e-18

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: 78.88  E-value: 1.97e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1335114667   41 TVTGEPCYFPFQYRRQLYHQCTRRGRIGFRPWCATTPNFDQDQRWAYC 88
Cdd:smart00059   2 NSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 41-88 4.09e-18

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: 78.12  E-value: 4.09e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1335114667  41 TVTGEPCYFPFQYRRQLYHQCTRRGRIGFRPWCATTPNFDQDQRWAYC 88
Cdd:cd00062     1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
fn2 pfam00040
Fibronectin type II domain;
47-88 9.52e-17

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 74.14  E-value: 9.52e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1335114667  47 CYFPFQYRRQLYHQCTRRGRIGFRPWCATTPNFDQDQRWAYC 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 4.01e-09

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: 52.25  E-value: 4.01e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1335114667  96 DHCSTHNPCQRGGTCVNMPDGPRCICPEHFTGKHCQ 131
Cdd:cd00054     3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 133-173 1.49e-08

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: 50.79  E-value: 1.49e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1335114667 133 EKCFEPQLLQFFHENETWHRLEPAGMAECQCQG--PQAHCKPL 173
Cdd:cd00061     1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCDPV 43
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 396-473 2.36e-08

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 54.30  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1335114667 396 GHSFCAGSLIAPCWVLTAAHCLQNRP---APEELTVVLGQDRhnqscAQCQVLAVRAYHLHEDFSPVT-YQHDLALLRLQ 471
Cdd:COG3591    10 GGGVCTGTLIGPNLVLTAGHCVYDGAgggWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGdAGYDYALLRLD 84


                  ..
gi 1335114667 472 ES 473
Cdd:COG3591    85 EP 86
EGF_CA smart00179
Calcium-binding EGF-like domain;
96-131 1.03e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 45.32  E-value: 1.03e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1335114667   96 DHCSTHNPCQRGGTCVNMPDGPRCICPEHFT-GKHCQ 131
Cdd:smart00179   3 DECASGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
fn1 pfam00039
Fibronectin type I domain;
135-170 1.77e-06

Fibronectin type I domain;


Pssm-ID: 459644  Cd Length: 40  Bit Score: 45.00  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1335114667 135 CFEPQLLQFFHENETWHRLEPAG-MAECQCQG---PQAHC 170
Cdd:pfam00039   1 CYDPQTGRFYQVGETWERPSQRGhVLQCTCLGnggGEIRC 40
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 98-131 3.32e-06

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: 44.00  E-value: 3.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1335114667  98 CSTHNPCQRGGTCVNMPDGPRCICPEHFTG-KHCQ 131
Cdd:cd00053     2 CAASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 178-208 9.33e-06

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: 42.76  E-value: 9.33e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1335114667 178 CSNNPCLHGGRCLEAEGHRLCSCPEGYAGRF 208
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
FN1 smart00058
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ...
 135-175 1.32e-05

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: 42.34  E-value: 1.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1335114667  135 CFEPQLLQFFHENETWHRLEPAGMAE-CQCQGPQ---AHCKPLAS 175
Cdd:smart00058   1 CFDEETGTTYRVGDTWERPYEGGHVLqCTCLGGGrgeWKCDPVPV 45
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 102-129 4.94e-05

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: 40.44  E-value: 4.94e-05
                          10        20
                  ....*....|....*....|....*...
gi 1335114667 102 NPCQRGGTCVNMPDGPRCICPEHFTGKH 129
Cdd:pfam00008   4 NPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 179-209 3.60e-04

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: 38.39  E-value: 3.60e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1335114667 179 SNNPCLHGGRCLEAEGHRLCSCPEGYAGRFC 209
Cdd:cd00054     7 SGNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
EGF smart00181
Epidermal growth factor-like domain;
98-131 2.52e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 35.96  E-value: 2.52e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1335114667   98 CSTHNPCQrGGTCVNMPDGPRCICPEHFTG-KHCQ 131
Cdd:smart00181   2 CASGGPCS-NGTCINTPGSYTCSCPPGYTGdKRCE 35
alphaLP-like cd21112
alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and ...
 556-611 2.98e-03

alpha-lytic protease (alpha-LP), a bacterial serine protease of the chymotrypsin family, and similar proteins; This family represents the catalytic domain of alpha-lytic protease (alpha-LP) and its closely-related homologs. Alpha-lytic protease (EC 3.4.21.12; also called alpha-lytic endopeptidase), originally isolated from the myxobacterium Lysobacter enzymogenes, belongs to the MEROPS peptidase family S1, subfamily S1E (streptogrisin A subfamily). It is synthesized as a pro-enzyme, thus having two domains; the N-terminal pro-domain acts as a foldase, required transiently for the correct folding of the protease domain, and also acts as a potent inhibitor of the mature enzyme, while the C-terminal domain catalyzes the cleavage of peptide bonds. Members of the alpha-lytic protease subfamily include Nocardiopsis alba protease (NAPase), a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis, streptogrisins (SPG-A, SPG-B, SPG-C, and SPG-D), and Thermobifida fusca protease A (TFPA). These serine proteases have characteristic kinetic stability, exhibited by their extremely slow unfolding kinetics. The active site, characteristic of serine proteases, contains the catalytic triad consisting of serine acting as a nucleophile, aspartate as an electrophile, and histidine as a base, all required for activity. This model represents the C-terminal catalytic domain of alpha-lytic proteases.


Pssm-ID: 411050  Cd Length: 188  Bit Score: 39.21  E-value: 2.98e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1335114667 556 YPDGG------TDAC--QGDSGGPLVcededRGLTLRGIISWGSG-CGDRNKPGVYTDVANYLTW 611
Cdd:cd21112   127 YPGGTvtgltrTNACaePGDSGGPVF-----SGTQALGITSGGSGnCGSGGGTSYFQPVNPVLSA 186
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 179-208 9.54e-03

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: 34.37  E-value: 9.54e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1335114667 179 SNNPCLHGGRCLEAEGHRLCSCPEGYAGRF 208
Cdd:cd00053     4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGDR 33
 
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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