Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767916610  24 CPALNTPADGRKFGSK--YLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCR 78
Cdd:cd00033    1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

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 767916610  80 ISECSSQ-PCQNGGTCVEGVNQYRCICPPGRTGNRCQ 115
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767916610  24 CPALNTPADGRKFGSK--YLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCR 78
Cdd:cd00033    1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767916610  213 DVDECVGLQPVCPQGTTCINTGGSFQCVspeCPEG 247
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR---CPDG 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 767916610  80 ISECSSQ-PCQNGGTCVEGVNQYRCICPPGRTGNRCQ 115
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767916610   167 DVNECELYGqegrprLCMHA--CVNTPGSYRCTCPGGYRtlaDGKSCE 212
Cdd:smart00179   1 DIDECASGN------PCQNGgtCVNTVGSYRCECPPGYT---DGRNCE 39

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20
                  ....*....|....*....|....*....
gi 767916610  183 CMHACVNTPGSYRCTCPGGYRTLADGKSC 211
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 767916610   213 DVDECVGLQPvCPQGTTCINTGGSFQCvspECPEG 247
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRC---ECPPG 31

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 767916610 213 DVDECVGLQPvCPQGTTCINTGGSFQCvspECPEG 247
Cdd:cd00054    1 DIDECASGNP-CQNGGTCVNTVGSYRC---SCPPG 31

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767916610  24 CPALNTPADGRKFGSK--YLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCR 78
Cdd:cd00033    1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767916610  213 DVDECVGLQPVCPQGTTCINTGGSFQCVspeCPEG 247
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR---CPDG 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 767916610  80 ISECSSQ-PCQNGGTCVEGVNQYRCICPPGRTGNRCQ 115
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767916610   167 DVNECELYGqegrprLCMHA--CVNTPGSYRCTCPGGYRtlaDGKSCE 212
Cdd:smart00179   1 DIDECASGN------PCQNGgtCVNTVGSYRCECPPGYT---DGRNCE 39

Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is found to be the target for a potent inhibitor of coagulation, TAK-442.

                          10        20
                  ....*....|....*....|....*....
gi 767916610  183 CMHACVNTPGSYRCTCPGGYRTLADGKSC 211
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

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 767916610  82 ECS-SQPCQNGGTCVEGVNQYRCICPPGRTGNR 113
Cdd:cd00053    1 ECAaSNPCSNGGTCVNTPGSYRCVCPPGYTGDR 33

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 767916610  195 RCTCPGGYRTLADGKSCEDVDE 216
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

EEV Host range protein; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767916610  25 PAL-NTPADGRKFGSKYLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHC 77
Cdd:PHA02817  92 PALqNGFVNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145

VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and matrix-matrix interactions thereby providing tissue integrity. Some members of the matrilin family are expressed specifically in developing cartilage rudiments. The matrilin family consists of at least four members. All the members of the matrilin family contain VWA domains, EGF-like domains and a heptad repeat coiled-coiled domain at the carboxy terminus which is responsible for the oligomerization of the matrilins. The VWA domains have been shown to be essential for matrilin network formation by interacting with matrix ligands.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 767916610 163 SVCQDVNECELygqegRPRLCMHACVNTPGSYRCTCPGGYRTLADGKS 210
Cdd:cd01475  182 KICVVPDLCAT-----LSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224