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Conserved domains on  [gi|62078741|ref|NP_001014028|]
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coagulation factor XII precursor [Rattus norvegicus]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 10812496)

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 ...
 362-600 2.42e-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: 283.78  E-value: 2.42e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 362 VVGGLVALPGSHPYIAALY--WGDSFCAGSLIDPCWVLTAAHCLQKRPaPEELTVVLGQDRHNQSCERCQTLAVHSYRLH 439
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 440 EGFSSKTYQHDLALLRLrgrkNSCAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEeYATFLQEAQVPFISLDR 519
Cdd:cd00190  80 PNYNPSTYDNDIALLKL----KRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 520 CSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTErqlTLRGVISWGSGCGDRNKPGVYTDVANYLDWIQE 599
Cdd:cd00190 155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRG---VLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231


                .
gi 62078741 600 H 600
Cdd:cd00190 232 T 232
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 216-294 1.50e-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: 97.38  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741   216 CYEDRGLSYRGQAKTTLSGAPCQRWASEATYRN--MTETQALSWGLGhHAFCRNPDNDTRPWCYVwSGDRLSWDYCDLEQ 293
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLG-ENYCRNPDGDERPWCYT-TDPRVRWEYCDIPR 78


                  .
gi 62078741   294 C 294
Cdd:pfam00051  79 C 79
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 40-87 1.30e-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: 82.35  E-value: 1.30e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 62078741  40 TVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYC 87
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 95-130 1.95e-08

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: 50.33  E-value: 1.95e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 62078741  95 DHCSKHSPCHKGGTCVNTPNGPHCLCPEHLTGKHCQ 130
Cdd:cd00054   3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 132-170 4.35e-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: 49.25  E-value: 4.35e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 62078741 132 EKCFESQLLKFFHENEIWFRTGPGGVARCQCKG--PQAVCK 170
Cdd:cd00061   1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCD 41
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 177-207 3.85e-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: 40.83  E-value: 3.85e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 62078741   177 CRVNPCLNGGTCLLVEDHRLCHCPAGYAGPF 207
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 ...
 362-600 2.42e-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: 283.78  E-value: 2.42e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 362 VVGGLVALPGSHPYIAALY--WGDSFCAGSLIDPCWVLTAAHCLQKRPaPEELTVVLGQDRHNQSCERCQTLAVHSYRLH 439
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 440 EGFSSKTYQHDLALLRLrgrkNSCAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEeYATFLQEAQVPFISLDR 519
Cdd:cd00190  80 PNYNPSTYDNDIALLKL----KRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 520 CSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTErqlTLRGVISWGSGCGDRNKPGVYTDVANYLDWIQE 599
Cdd:cd00190 155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRG---VLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231


                .
gi 62078741 600 H 600
Cdd:cd00190 232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 361-597 4.10e-91

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: 280.72  E-value: 4.10e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741    361 RVVGGLVALPGSHPYIAALYWGDS--FCAGSLIDPCWVLTAAHCLQKRPaPEELTVVLGQDRHNQScERCQTLAVHSYRL 438
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrhFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741    439 HEGFSSKTYQHDLALLRLRGRknscAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEEYATFLQEAQVPFISLD 518
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62078741    519 RCSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTerqlTLRGVISWGSGCGDRNKPGVYTDVANYLDWI 597
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRW----VLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
362-597 3.25e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.38  E-value: 3.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741   362 VVGGLVALPGSHPYIAALYWGDS--FCAGSLIDPCWVLTAAHCLqkrPAPEELTVVLGQDRHNQSCERCQTLAVHSYRLH 439
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741   440 EGFSSKTYQHDLALLRLRGRknscAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGaeEYATFLQEAQVPFISLDR 519
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESP----VTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62078741   520 CSSSnvHGDAILPGMLCAGFleGGADACQGDSGGPLVCDEGvterqlTLRGVISWGSGCGDRNKPGVYTDVANYLDWI 597
Cdd:pfam00089 152 CRSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG------ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 361-602 3.70e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.43  E-value: 3.70e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 361 RVVGGLVALPGSHPYIAALYWGDS----FCAGSLIDPCWVLTAAHCLQKrPAPEELTVVLGQDRHNQSceRCQTLAVHSY 436
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGpsgqFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTS--GGTVVKVARI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 437 RLHEGFSSKTYQHDLALLRLRGRknscailSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEEYATFLQEAQVPFIS 516
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATP-------VPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVS 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 517 LDRCsssNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTERQLtlrGVISWGSGCGDRNKPGVYTDVANYLDW 596
Cdd:COG5640 180 DATC---AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLV---GVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                ....*.
gi 62078741 597 IQEHTA 602
Cdd:COG5640 254 IKSTAG 259
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 216-294 1.50e-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: 97.38  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741   216 CYEDRGLSYRGQAKTTLSGAPCQRWASEATYRN--MTETQALSWGLGhHAFCRNPDNDTRPWCYVwSGDRLSWDYCDLEQ 293
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLG-ENYCRNPDGDERPWCYT-TDPRVRWEYCDIPR 78


                  .
gi 62078741   294 C 294
Cdd:pfam00051  79 C 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 214-294 6.11e-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.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 92.83  E-value: 6.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 214 ATCYEDRGLSYRGQAKTTLSGAPCQRWASEATYRNMTETQALSWGLGHHAFCRNPDND-TRPWCYVWsGDRLSWDYCDLE 292
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTT-DPNVRWEYCDIP 80


                ..
gi 62078741 293 QC 294
Cdd:cd00108  81 RC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 215-294 3.65e-22

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: 90.53  E-value: 3.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741    215 TCYEDRGLSYRGQAKTTLSGAPCQRWASEATY-RNMTETQALSWGLGhHAFCRNPDND-TRPWCYVwSGDRLSWDYCDLE 292
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHlHRFTPESFPDLGLE-ENYCRNPDGDsEGPWCYT-TDPNVRWEYCDIP 79


                   ..
gi 62078741    293 QC 294
Cdd:smart00130  80 QC 81
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 40-87 1.30e-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: 82.35  E-value: 1.30e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 62078741  40 TVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYC 87
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 40-87 2.94e-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: 78.50  E-value: 2.94e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 62078741     40 TVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYC 87
Cdd:smart00059   2 NSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
46-87 3.09e-17

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 75.30  E-value: 3.09e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 62078741    46 CHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYC 87
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 95-130 1.95e-08

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: 50.33  E-value: 1.95e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 62078741  95 DHCSKHSPCHKGGTCVNTPNGPHCLCPEHLTGKHCQ 130
Cdd:cd00054   3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 132-170 4.35e-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: 49.25  E-value: 4.35e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 62078741 132 EKCFESQLLKFFHENEIWFRTGPGGVARCQCKG--PQAVCK 170
Cdd:cd00061   1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCD 41
EGF_CA smart00179
Calcium-binding EGF-like domain;
95-130 2.18e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 2.18e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 62078741     95 DHCSKHSPCHKGGTCVNTPNGPHCLCPE-HLTGKHCQ 130
Cdd:smart00179   3 DECASGNPCQNGGTCVNTVGSYRCECPPgYTDGRNCE 39
fn1 pfam00039
Fibronectin type I domain;
134-164 1.95e-05

Fibronectin type I domain;


Pssm-ID: 459644  Cd Length: 40  Bit Score: 41.92  E-value: 1.95e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 62078741   134 CFESQLLKFFHENEIWFRTGPGG-VARCQCKG 164
Cdd:pfam00039   1 CYDPQTGRFYQVGETWERPSQRGhVLQCTCLG 32
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 97-128 2.12e-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: 41.60  E-value: 2.12e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 62078741    97 CSKHsPCHKGGTCVNTPNGPHCLCPEHLTGKH 128
Cdd:pfam00008   1 CAPN-PCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 177-207 3.85e-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: 40.83  E-value: 3.85e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 62078741   177 CRVNPCLNGGTCLLVEDHRLCHCPAGYAGPF 207
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
FN1 smart00058
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ...
 134-166 1.04e-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: 40.03  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 62078741    134 CFESQLLKFFHENEIWFRTGPGG-VARCQCKGPQ 166
Cdd:smart00058   1 CFDEETGTTYRVGDTWERPYEGGhVLQCTCLGGG 34
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 362-600 2.42e-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: 283.78  E-value: 2.42e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 362 VVGGLVALPGSHPYIAALY--WGDSFCAGSLIDPCWVLTAAHCLQKRPaPEELTVVLGQDRHNQSCERCQTLAVHSYRLH 439
Cdd:cd00190   1 IVGGSEAKIGSFPWQVSLQytGGRHFCGGSLISPRWVLTAAHCVYSSA-PSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 440 EGFSSKTYQHDLALLRLrgrkNSCAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEeYATFLQEAQVPFISLDR 519
Cdd:cd00190  80 PNYNPSTYDNDIALLKL----KRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGP-LPDVLQEVNVPIVSNAE 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 520 CSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTErqlTLRGVISWGSGCGDRNKPGVYTDVANYLDWIQE 599
Cdd:cd00190 155 CKRAYSYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDNGRG---VLVGIVSWGSGCARPNYPGVYTRVSSYLDWIQK 231


                .
gi 62078741 600 H 600
Cdd:cd00190 232 T 232
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 361-597 4.10e-91

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: 280.72  E-value: 4.10e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741    361 RVVGGLVALPGSHPYIAALYWGDS--FCAGSLIDPCWVLTAAHCLQKRPaPEELTVVLGQDRHNQScERCQTLAVHSYRL 438
Cdd:smart00020   1 RIVGGSEANIGSFPWQVSLQYGGGrhFCGGSLISPRWVLTAAHCVRGSD-PSNIRVRLGSHDLSSG-EEGQVIKVSKVII 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741    439 HEGFSSKTYQHDLALLRLRGRknscAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEEYATFLQEAQVPFISLD 518
Cdd:smart00020  79 HPNYNPSTYDNDIALLKLKEP----VTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEGAGSLPDTLQEVNVPIVSNA 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62078741    519 RCSSSNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTerqlTLRGVISWGSGCGDRNKPGVYTDVANYLDWI 597
Cdd:smart00020 155 TCRRAYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCNDGRW----VLVGIVSWGSGCARPGKPGVYTRVSSYLDWI 229
Trypsin pfam00089
Trypsin;
362-597 3.25e-66

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 215.38  E-value: 3.25e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741   362 VVGGLVALPGSHPYIAALYWGDS--FCAGSLIDPCWVLTAAHCLqkrPAPEELTVVLGQDRHNQSCERCQTLAVHSYRLH 439
Cdd:pfam00089   1 IVGGDEAQPGSFPWQVSLQLSSGkhFCGGSLISENWVLTAAHCV---SGASDVKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741   440 EGFSSKTYQHDLALLRLRGRknscAILSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGaeEYATFLQEAQVPFISLDR 519
Cdd:pfam00089  78 PNYNPDTLDNDIALLKLESP----VTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKTL--GPSDTLQEVTVPVVSRET 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62078741   520 CSSSnvHGDAILPGMLCAGFleGGADACQGDSGGPLVCDEGvterqlTLRGVISWGSGCGDRNKPGVYTDVANYLDWI 597
Cdd:pfam00089 152 CRSA--YGGTVTDTMICAGA--GGKDACQGDSGGPLVCSDG------ELIGIVSWGYGCASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 361-602 3.70e-64

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


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.43  E-value: 3.70e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 361 RVVGGLVALPGSHPYIAALYWGDS----FCAGSLIDPCWVLTAAHCLQKrPAPEELTVVLGQDRHNQSceRCQTLAVHSY 436
Cdd:COG5640  30 AIVGGTPATVGEYPWMVALQSSNGpsgqFCGGTLIAPRWVLTAAHCVDG-DGPSDLRVVIGSTDLSTS--GGTVVKVARI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 437 RLHEGFSSKTYQHDLALLRLRGRknscailSPHVQPVCLPSSAAPPSETVLCEVAGWGHQFEGAEEYATFLQEAQVPFIS 516
Cdd:COG5640 107 VVHPDYDPATPGNDIALLKLATP-------VPGVAPAPLATSADAAAPGTPATVAGWGRTSEGPGSQSGTLRKADVPVVS 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 517 LDRCsssNVHGDAILPGMLCAGFLEGGADACQGDSGGPLVCDEGVTERQLtlrGVISWGSGCGDRNKPGVYTDVANYLDW 596
Cdd:COG5640 180 DATC---AAYGGFDGGTMLCAGYPEGGKDACQGDSGGPLVVKDGGGWVLV---GVVSWGGGPCAAGYPGVYTRVSAYRDW 253


                ....*.
gi 62078741 597 IQEHTA 602
Cdd:COG5640 254 IKSTAG 259
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
 216-294 1.50e-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: 97.38  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741   216 CYEDRGLSYRGQAKTTLSGAPCQRWASEATYRN--MTETQALSWGLGhHAFCRNPDNDTRPWCYVwSGDRLSWDYCDLEQ 293
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAWDSQTPHRHskYTPENFPAKGLG-ENYCRNPDGDERPWCYT-TDPRVRWEYCDIPR 78


                  .
gi 62078741   294 C 294
Cdd:pfam00051  79 C 79
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
 214-294 6.11e-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.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 92.83  E-value: 6.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 214 ATCYEDRGLSYRGQAKTTLSGAPCQRWASEATYRNMTETQALSWGLGHHAFCRNPDND-TRPWCYVWsGDRLSWDYCDLE 292
Cdd:cd00108   2 RDCYWGNGESYRGTVSTTKSGKPCQRWNSQLPHQHKFNPERFPEGLLEENYCRNPDGDpEGPWCYTT-DPNVRWEYCDIP 80


                ..
gi 62078741 293 QC 294
Cdd:cd00108  81 RC 82
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
 215-294 3.65e-22

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: 90.53  E-value: 3.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741    215 TCYEDRGLSYRGQAKTTLSGAPCQRWASEATY-RNMTETQALSWGLGhHAFCRNPDND-TRPWCYVwSGDRLSWDYCDLE 292
Cdd:smart00130   2 ECYAGNGESYRGTVSVTKSGKPCQRWDSQTPHlHRFTPESFPDLGLE-ENYCRNPDGDsEGPWCYT-TDPNVRWEYCDIP 79


                   ..
gi 62078741    293 QC 294
Cdd:smart00130  80 QC 81
FN2 cd00062
Fibronectin Type II domain: FN2 is one of three types of internal repeats which combine to ...
 40-87 1.30e-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: 82.35  E-value: 1.30e-19
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 62078741  40 TVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYC 87
Cdd:cd00062   1 NSDGAPCVFPFIYRGKWYHDCTTEGSNDGKLWCSTTPNYDRDGKWGYC 48
FN2 smart00059
Fibronectin type 2 domain; One of three types of internal repeat within the plasma protein, ...
 40-87 2.94e-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: 78.50  E-value: 2.94e-18
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 62078741     40 TVDGKLCHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYC 87
Cdd:smart00059   2 NSDGEPCVFPFIYNGKKYHDCTSEGRSDGMLWCSTTPNYDRDGKWGFC 49
fn2 pfam00040
Fibronectin type II domain;
46-87 3.09e-17

Fibronectin type II domain;


Pssm-ID: 459645  Cd Length: 42  Bit Score: 75.30  E-value: 3.09e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 62078741    46 CHFPFQYHRRLYHKCIHKGQPGSRPWCATTPNFDEDQQWGYC 87
Cdd:pfam00040   1 CVFPFKYKGKWYHTCTTDGRRSGRLWCATTANYDGDGKWGYC 42
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 382-599 5.04e-11

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


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 62.00  E-value: 5.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 382 GDSFCAGSLIDPCWVLTAAHCL---QKRPAPEELTVVLGQDRhnqscERCQTLAVHSYRLHEGFSSKT-YQHDLALLRLR 457
Cdd:COG3591  10 GGGVCTGTLIGPNLVLTAGHCVydgAGGGWATNIVFVPGYNG-----GPYGTATATRFRVPPGWVASGdAGYDYALLRLD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62078741 458 GRknscaiLSPHVQPVCLPSSAAPPSETVLCeVAGWGhqfeGAEEYATFLQEAqvpfisldrCSSSNVHGDailpgmlca 537
Cdd:COG3591  85 EP------LGDTTGWLGLAFNDAPLAGEPVT-IIGYP----GDRPKDLSLDCS---------GRVTGVQGN--------- 135

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62078741 538 gFLEGGADACQGDSGGPLVCDEGVTERQLtlrGVISWGSgcGDRNKPGVYTD---VANYLDWIQE 599
Cdd:COG3591 136 -RLSYDCDTTGGSSGSPVLDDSDGGGRVV---GVHSAGG--ADRANTGVRLTsaiVAALRAWASA 194
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 95-130 1.95e-08

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: 50.33  E-value: 1.95e-08
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 62078741  95 DHCSKHSPCHKGGTCVNTPNGPHCLCPEHLTGKHCQ 130
Cdd:cd00054   3 DECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FN1 cd00061
Fibronectin type 1 domain, approximately 40 residue long with two conserved disulfide bridges. ...
 132-170 4.35e-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: 49.25  E-value: 4.35e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 62078741 132 EKCFESQLLKFFHENEIWFRTGPGGVARCQCKG--PQAVCK 170
Cdd:cd00061   1 EKCFDPQTGVFYRVGETWERPSEGHVLQCTCLGnrGEARCD 41
EGF_CA smart00179
Calcium-binding EGF-like domain;
95-130 2.18e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 44.55  E-value: 2.18e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 62078741     95 DHCSKHSPCHKGGTCVNTPNGPHCLCPE-HLTGKHCQ 130
Cdd:smart00179   3 DECASGNPCQNGGTCVNTVGSYRCECPPgYTDGRNCE 39
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
 97-130 1.14e-05

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: 42.46  E-value: 1.14e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 62078741  97 CSKHSPCHKGGTCVNTPNGPHCLCPEHLTG-KHCQ 130
Cdd:cd00053   2 CAASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
fn1 pfam00039
Fibronectin type I domain;
134-164 1.95e-05

Fibronectin type I domain;


Pssm-ID: 459644  Cd Length: 40  Bit Score: 41.92  E-value: 1.95e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 62078741   134 CFESQLLKFFHENEIWFRTGPGG-VARCQCKG 164
Cdd:pfam00039   1 CYDPQTGRFYQVGETWERPSQRGhVLQCTCLG 32
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 97-128 2.12e-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: 41.60  E-value: 2.12e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 62078741    97 CSKHsPCHKGGTCVNTPNGPHCLCPEHLTGKH 128
Cdd:pfam00008   1 CAPN-PCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF pfam00008
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ...
 177-207 3.85e-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: 40.83  E-value: 3.85e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 62078741   177 CRVNPCLNGGTCLLVEDHRLCHCPAGYAGPF 207
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
FN1 smart00058
Fibronectin type 1 domain; One of three types of internal repeat within the plasma protein, ...
 134-166 1.04e-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: 40.03  E-value: 1.04e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 62078741    134 CFESQLLKFFHENEIWFRTGPGG-VARCQCKGPQ 166
Cdd:smart00058   1 CFDEETGTTYRVGDTWERPYEGGhVLQCTCLGGG 34
 
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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