TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 46249421    363 CMHPLSVHLTKQICCC-SVGKAWGPHCEKCPLPGTAAFKEIC 403
Cdd:pfam00683    3 CSNPLPGNVTKSECCCtSVGRAWGSPCELCPPPGTDEFRELC 44

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 46249421   1208 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1250
Cdd:pfam00683    2 RCSNPLPG-NVTKSECCCTSvGRAWGSPCELCPPPGTDEFRELC 44

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 46249421     794 DIDECEHHHLCSHG-QCRNTEGSFQCVCNQGYRAsvlGDHCE 834
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGYTD---GRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 46249421     918 DIDECVNNTVCDSHGFCDNTAGSFRCLCYQGFqapQDGQGCV 959
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY---TDGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 46249421     589 DIDECAQvRHLCSQG-RCENTEGSFLCVCPAGFmasEEGTNCI 630
Cdd:smart00179    1 DIDECAS-GNPCQNGgTCVNTVGSYRCECPPGY---TDGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 46249421     835 DINECLEDSSVCQGGDCINTAGSYDCTCPDGFQLNDN 871
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRN 37

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 46249421    1335 DVNECSELNNrmslCKN-AKCINTEGSYKCLCLPGY 1369
Cdd:smart00179    1 DIDECASGNP----CQNgGTCVNTVGSYRCECPPGY 32

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 46249421  672 DIDECLKPSTCPEE-QCVNTPGSYQCVpCTEGFRG 705
Cdd:cd00054    1 DIDECASGNPCQNGgTCVNTVGSYRCS-CPPGYTG 34

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 46249421    363 CMHPLSVHLTKQICCC-SVGKAWGPHCEKCPLPGTAAFKEIC 403
Cdd:pfam00683    3 CSNPLPGNVTKSECCCtSVGRAWGSPCELCPPPGTDEFRELC 44

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 46249421   1208 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1250
Cdd:pfam00683    2 RCSNPLPG-NVTKSECCCTSvGRAWGSPCELCPPPGTDEFRELC 44

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        40
                 ....*....|....*....|....*....|....*....|..
gi 46249421  876 DINECAQPGLCGSHGECLNTQGSFHCVCEQGFSisadGRTCE 917
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|...
gi 46249421     753 DIDECQQGNLCMNG-QCRNTDGSFRCTCGQGYQ 784
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGYT 33

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 46249421  753 DIDECQQGNLCMN-GQCRNTDGSFRCTCGQGYQL 785
Cdd:cd00054    1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYTG 34

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 46249421     300 DINECQLQGVCPNG-ECLNTMGSYRCSCKMGF 330
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGY 32

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 46249421  918 DIDECVNNTVCDSHGFCDNTAGSFRCLCYQGFQ 950
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 46249421     835 DINECLEDSSVCQGGDCINTAGSYDCTCPDGFQLNDN 871
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRN 37

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 46249421    589 DIDECAQVRHLCSQ-GRCENTEGSFLCVCPAG 619
Cdd:pfam07645    1 DVDECATGTHNCPAnTVCVNTIGSFECRCPDG 32

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 46249421  300 DINECQLQGVCPN-GECLNTMGSYRCSCKMGF 330
Cdd:cd00054    1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGY 32

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 46249421  835 DINECLEDSSVCQGGDCINTAGSYDCTCPDGFQL 868
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG 34

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 46249421    876 DINECAQPG-LCGSHGECLNTQGSFHCVCEQG 906
Cdd:pfam07645    1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32

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        40
                 ....*....|....*....|....*....|....*....|..
gi 46249421  712 DVDECLQPKVCTN-GSCTNLEGSYMCSCHRGYSPtpdhRHCQ 752
Cdd:cd00054    1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYTG----RNCE 38

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 46249421    918 DIDECVNNT-VCDSHGFCDNTAGSFRCLCYQG 948
Cdd:pfam07645    1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                           10        20
                   ....*....|....*....|.
gi 46249421    736 CSCHRGYSPTPDHRHCQDIDE 756
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 46249421     631 DVDECLRPDMCRDG-RCINTAGAFRCEyCDSGYRMSRR 667
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCE-CPPGYTDGRN 37

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 46249421    363 CMHPLSVHLTKQICCC-SVGKAWGPHCEKCPLPGTAAFKEIC 403
Cdd:pfam00683    3 CSNPLPGNVTKSECCCtSVGRAWGSPCELCPPPGTDEFRELC 44

TB domain; This domain is also known as the 8 cysteine domain. This family includes the hybrid domains. This cysteine rich repeat is found in TGF binding protein and fibrillin.

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 46249421   1208 VCSRPLVGkQTTYTECCCLY-GEAWGMQCALCPMKDSDDYAQLC 1250
Cdd:pfam00683    2 RCSNPLPG-NVTKSECCCTSvGRAWGSPCELCPPPGTDEFRELC 44

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        40
                 ....*....|....*....|....*....|....*....|..
gi 46249421  876 DINECAQPGLCGSHGECLNTQGSFHCVCEQGFSisadGRTCE 917
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|...
gi 46249421     753 DIDECQQGNLCMNG-QCRNTDGSFRCTCGQGYQ 784
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGYT 33

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 46249421  753 DIDECQQGNLCMN-GQCRNTDGSFRCTCGQGYQL 785
Cdd:cd00054    1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGYTG 34

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 46249421     300 DINECQLQGVCPNG-ECLNTMGSYRCSCKMGF 330
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCECPPGY 32

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 46249421  918 DIDECVNNTVCDSHGFCDNTAGSFRCLCYQGFQ 950
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 46249421     835 DINECLEDSSVCQGGDCINTAGSYDCTCPDGFQLNDN 871
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGYTDGRN 37

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 46249421    589 DIDECAQVRHLCSQ-GRCENTEGSFLCVCPAG 619
Cdd:pfam07645    1 DVDECATGTHNCPAnTVCVNTIGSFECRCPDG 32

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 46249421  300 DINECQLQGVCPN-GECLNTMGSYRCSCKMGF 330
Cdd:cd00054    1 DIDECASGNPCQNgGTCVNTVGSYRCSCPPGY 32

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 46249421  835 DINECLEDSSVCQGGDCINTAGSYDCTCPDGFQL 868
Cdd:cd00054    1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTG 34

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 46249421    876 DINECAQPG-LCGSHGECLNTQGSFHCVCEQG 906
Cdd:pfam07645    1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32

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 46249421 1335 DVNECSELNNrmslCKN-AKCINTEGSYKCLCLPGYI 1370
Cdd:cd00054    1 DIDECASGNP----CQNgGTCVNTVGSYRCSCPPGYT 33

Epidermal growth factor-like domain;

                            10        20        30
                    ....*....|....*....|....*....|.
gi 46249421     756 ECQQGNLCMNGQCRNTDGSFRCTCGQGYQLS 786
Cdd:smart00181    1 ECASGGPCSNGTCINTPGSYTCSCPPGYTGD 31

Epidermal growth factor-like domain;

                            10        20        30
                    ....*....|....*....|....*....|...
gi 46249421     303 ECQLQGVCPNGECLNTMGSYRCSCKMGFGPDPT 335
Cdd:smart00181    1 ECASGGPCSNGTCINTPGSYTCSCPPGYTGDKR 33

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 46249421    918 DIDECVNNT-VCDSHGFCDNTAGSFRCLCYQG 948
Cdd:pfam07645    1 DVDECATGThNCPANTVCVNTIGSFECRCPDG 32

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                           10        20
                   ....*....|....*....|.
gi 46249421    736 CSCHRGYSPTPDHRHCQDIDE 756
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 46249421     631 DVDECLRPDMCRDG-RCINTAGAFRCEyCDSGYRMSRR 667
Cdd:smart00179    1 DIDECASGNPCQNGgTCVNTVGSYRCE-CPPGYTDGRN 37

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteriztic pattern 'ababcc'. They are found in blood coagulation proteins such as fibrillin, Clr and Cls, thrombomodulin, and the LDL receptor. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal cysteine residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In cEGFs the C-terminal thiol resides on the C-terminal beta-sheet, resulting in long loop-lengths between the cysteine residues of disulfide 'c', typically C[10+]XC. These longer loop-lengths may have arisen by selective cysteine loss from a four-disulfide EGF template such as laminin or integrin. Tandem cEGF domains have five linking residues between terminal cysteines of adjacent domains. cEGF domains may or may not bind calcium in the linker region. cEGF domains with the consensus motif CXN4X[F,Y]XCXC are hydroxylated exclusively on the asparagine residue.

                           10        20
                   ....*....|....*....|..
gi 46249421    900 HCVCEQGFSISADGRTCEDIDE 921
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....
gi 46249421     672 DIDECLKPSTC-PEEQCVNTPGSYQCVpCTEGFR 704
Cdd:smart00179    1 DIDECASGNPCqNGGTCVNTVGSYRCE-CPPGYT 33