Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805  745 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTQTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 824
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805  825 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTSDQVRLLWKDSRNVGWKDKVSYRWFLQHRPQVGYIRVRFYEGSEL 904
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 402766805  905 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 942
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 402766805 219 FNRQFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQACG 262
Cdd:cd16080    1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 402766805  692 EDSNNDGVGDICEADFDQDKVIDRIDVCPENAEIT 726
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35

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.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 402766805 379 DVDECR-NGACVLNSICINTLGSYRCGpCKPGYTGD 413
Cdd:cd00054    1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805 464 DVDIDSYPDEElpcSARNCKKDNCKYVPNSGQEDADRDGIGDAcDEDADGDgilNEQDNCVLTHNVDQRNTDKDIFGDAc 543
Cdd:NF033609 661 DSDSDSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDS- 732

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805 544 DNCRGVLNNDQKDTDGDGKGDACDDDMDGDGIKNILDNCPRVPNRDQQDRDGDGVGDAcDSCPDVSNPNQSDVDNDLVGD 623
Cdd:NF033609 733 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSD 811

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402766805 624 S-CDTNQDSDGDGHQDSTDNCPTVINSAQlDTDKDGIGDECDDDDDNDGIPDLVPPGPDNCRLVPNPAQEDSN 695
Cdd:NF033609 812 SdSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTN 883

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805  745 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTQTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 824
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805  825 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTSDQVRLLWKDSRNVGWKDKVSYRWFLQHRPQVGYIRVRFYEGSEL 904
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 402766805  905 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 942
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 402766805 219 FNRQFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQACG 262
Cdd:cd16080    1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 402766805  496 EDADRDGIGDACDEDADGDGILNEQDNCVLTHNVDQ 531
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANIDQ 36

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 402766805  615 DVDNDLVGDSCDtnQDSDGDGHQDSTDNCPTVINSAQ 651
Cdd:pfam02412   2 DSDSDGVGDACD--NDFDNDGVPDLLDNCPNNANIDQ 36

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.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 402766805 326 DVDECK-YHPCYPGVRCTNLAPGFRCDaCPVGFTGP 360
Cdd:cd00054    1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 402766805   326 DVDECK-YHPCYPGVRCTNLAPGFRCDaCPVGFT 358
Cdd:smart00179   1 DIDECAsGNPCQNGGTCVNTVGSYRCE-CPPGYT 33

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805 464 DVDIDSYPDEElpcSARNCKKDNCKYVPNSGQEDADRDGIGDAcDEDADGDgilNEQDNCVLTHNVDQRNTDKDIFGDAc 543
Cdd:NF033609 661 DSDSDSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSD---SDSDSDSDSDSDSDSDSDSDSDSDS- 732

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805 544 DNCRGVLNNDQKDTDGDGKGDACDDDMDGDGIKNILDNCPRVPNRDQQDRDGDGVGDAcDSCPDVSNPNQSDVDNDLVGD 623
Cdd:NF033609 733 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSDSD 811

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 402766805 624 S-CDTNQDSDGDGHQDSTDNCPTVINSAQlDTDKDGIGDECDDDDDNDGIPDLVPPGPDNCRLVPNPAQEDSN 695
Cdd:NF033609 812 SdSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTN 883

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805 462 GKDVDIDSYPDEELPCSARNCKKDNCKYVPNSGQEDADRDGIGDAcDEDADGDGIlNEQDNCVLTHNVDQRNTDKDIFGD 541
Cdd:NF033609 566 GSDSGSDSSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDS-DSASDSDSA-SDSDSASDSDSASDSDSASDSDSD 643

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805 542 AcDNCRGVLNNDQKDTDGDGKGDACDDDMDGDGIKNILDNCPRVPNRDQQDRDGDGVGDAcDSCPDVSNPNQSDVDNDLV 621
Cdd:NF033609 644 S-DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSDSDSDSDSDSDSDSDSD 721

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 402766805 622 GDS-CDTNQDSDGDGHQDSTDNCPTVINSAQlDTD 655
Cdd:NF033609 722 SDSdSDSDSDSDSDSDSDSDSDSDSDSDSDS-DSD 755

Thrombospondin C-terminal region; This region is found at the C-terminus of thrombospondin and related proteins.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805  745 QIDPNWVVLNQGMEIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTQTDDDYAGFIFGYQDSSSFYVVMWKQTEQTYWQAT 824
Cdd:pfam05735   1 QIDPIWVIRNQGREIQQTDNSDPGLAIGFDRFGSVDFSGTFFVNTDDDDDYIGFVFGYQSNSKFYVVMWKQVNQSYWPFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 402766805  825 PFRAVAEPGIQLKAVKSKTGPGEHLRNSLWHTGDTSDQVRLLWKDSRNVGWKDKVSYRWFLQHRPQVGYIRVRFYEGSEL 904
Cdd:pfam05735  81 PFRATGLKGIQLKVVKSTTGPGENLRNALWHTGDTTNQVRLLWHDPTWRGWKDRTAYRWHLQHRPSIGLIRVRVYEGITL 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 402766805  905 VADSGVTIDTTMRGGRLGVFCFSQENIIWSNLKYRCND 942
Cdd:pfam05735 161 LADSGNVYDTTIRGGRLGVFCFSQENVIWSDLKYKCLD 198

Coiled coil region of thrombospondin-4 (TSP-4); This family contains the N-terminal coiled coil region of TSP-4, which is abundantly expressed in tendon and muscle, as well as in neural and osteogenic tissues, and has also been detected in brain capillaries. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-4 regulates the composition of the deposition of extracellular matrix (ECM) in tendon and skeletal muscle. The absence of TSP-4 alters the organization, composition and physiological functions of these tissues. TSP-4 deficiency causes incorrect modification of heparan-sulfate (HS), resulting in decreased activity of lipoprotein lipase (LpL) and loss of beta-glycan; HS is involved in a wide variety of cellular functions, LpL is an endothelial enzyme responsible for the uptake and hydrolysis of lipoproteins, and beta-glycan has inhibiting effect on TGF-beta signaling in skeletal muscle. The human gene THBS4 that encodes for TSP-4 contains a single nucleotide polymorphism (SNP), which is expressed at high frequency in Caucasians and associated with a significantly increased risk of premature myocardial infarction. TSP-4 also binds stromal interaction molecule 1 (STIM1), a transmembrane protein that functions in the endoplasmic reticulum (ER), and regulates calcium channel activity. Studies show that TSP-4 may act as an organizer of adhesive and axon outgrowth-promoting molecules in the ECM to optimize retinal ganglion cell responses. TSP-4 is also involved in the post-translational modification of collagen and may assist in collagen fibril assembly.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 402766805 219 FNRQFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQACG 262
Cdd:cd16080    1 VGRQLLGQMTQLNQVLGEVKDLLRQQVKETSFLRNTIAECQACG 44

Coiled coil region of thrombospondin; This domain family contains coiled coil region of subgroup B of thrombospondins, comprising TSP-3, TSP-4, and TSP-5, that assemble as pentamers. This region is located adjacent to the N-terminal domain (NTD) of thrombospondin (TSP), that mediates co-translational oligomerization via formation of a left-handed super-helix which binds hydrophilic signaling molecules such as vitamin D3 and vitamin A. Pentameric TSPs are stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end. TSP-5 is also known as cartilage oligomeric matrix protein (COMP). TSPs comprise a conserved family of extracellular, oligomeric, multidomain, calcium-binding glycoproteins. In mammals, they have several complex tissue-specific roles, including activities in wound healing and angiogenesis, connective tissue organization, vessel wall biology, and synaptogenesis, all mechanistically derived from interactions with cell surfaces, cytokines, growth factors, or components of the extracellular matrix (ECM) that together regulate many aspects of cell phenotype. In invertebrates, TSPs may have ancient functions such as bridging activities in cell-cell and cell-ECM interactions. Most protostomes and inferred basal metazoa encode a single TSP with the general domain organization of subgroup B TSPs and with a pentamerizing coiled coil.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 402766805 222 QFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQAC 261
Cdd:cd16076    1 QLARQLTELNQMLQELREEMRQQVKETAFLRNTIMECQAC 40

Coiled coil region of thrombospondin-3 (TSP-3); This family contains the N-terminal coiled coil region of TSP-3, which is highly expressed in osteosarcomas and associated with metastasis. TSP-3, along with TSP-5 and type IX collagen, is also expressed in the growth plate and all operate in concert and participate in growth plate organization that directly modulates linear growth. It forms a pentameric left-handed coiled coil with a channel that is a unique carrier for lipophilic compounds. The pentamer is stabilized by inter-subunit disulfide bonds formed between cysteine residues adjacent to the C-terminal end of the coiled coil region. TSP-3 knockout mice have been shown to display accelerated endochondral ossification and increased trabecular bone in the femoral head.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 402766805 221 RQFLGQMTQLNQLLGEVKDLLRQQVKETSFLRNTIAECQAC 261
Cdd:cd16079    3 KALITQLTLFNQILGELREDIRDQVKEMSLIRNTIMECQVC 43

Thrombospondin type 3 repeat; The thrombospondin repeat is a short aspartate rich repeat which binds to calcium ions. The repeat was initially identified in thrombospondin proteins that contained 7 of these repeats. The repeat lacks defined secondary structure.

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 402766805  692 EDSNNDGVGDICEADFDQDKVIDRIDVCPENAEIT 726
Cdd:pfam02412   1 TDSDSDGVGDACDNDFDNDGVPDLLDNCPNNANID 35

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.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 402766805 379 DVDECR-NGACVLNSICINTLGSYRCGpCKPGYTGD 413
Cdd:cd00054    1 DIDECAsGNPCQNGGTCVNTVGSYRCS-CPPGYTGR 35

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 402766805   379 DVDEC-RNGACVLNSICINTLGSYRCGpCKPGYTGDQT 415
Cdd:smart00179   1 DIDECaSGNPCQNGGTCVNTVGSYRCE-CPPGYTDGRN 37

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|...
gi 402766805  379 DVDECRNGA--CVLNSICINTLGSYRCgPCKPG 409
Cdd:pfam07645   1 DVDECATGThnCPANTVCVNTIGSFEC-RCPDG 32

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                          10        20        30
                  ....*....|....*....|....*....|
gi 402766805  384 RNGACVLNSICINTLGSYRCgPCKPGYTGD 413
Cdd:pfam12947   4 NNGGCHPNATCTNTGGSFTC-TCNDGYTGD 32

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.

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 402766805 377 CTDVDECRNGAcvlnsICINTLGSYRCGpCKPGYTGDQT 415
Cdd:cd00053    2 CAASNPCSNGG-----TCVNTPGSYRCV-CPPGYTGDRS 34

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.

                          10        20        30
                  ....*....|....*....|....*....|.
gi 402766805  290 CDSSPCFRGVRCTDTRDGFQCGpCPDGYTGN 320
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCI-CPEGYTGK 30