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 578803647  81 CPALNTPADGRKFGSK--YLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCR 135
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 578803647 137 ISECSSQ-PCQNGGTCVEGVNQYRCICPPGRTGNRCQ 172
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 578803647  81 CPALNTPADGRKFGSK--YLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCR 135
Cdd:cd00033    1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 578803647  270 DVDECVGLQPVCPQGTTCINTGGSFQCVspeCPEG 304
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 578803647 137 ISECSSQ-PCQNGGTCVEGVNQYRCICPPGRTGNRCQ 172
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 578803647   224 DVNECELYGqegrprLCMHA--CVNTPGSYRCTCPGGYRtlaDGKSCE 269
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 578803647  240 CMHACVNTPGSYRCTCPGGYRTLADGKSC 268
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 578803647   270 DVDECVGLQPvCPQGTTCINTGGSFQCvspECPEG 304
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 578803647 270 DVDECVGLQPvCPQGTTCINTGGSFQCvspECPEG 304
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 578803647  81 CPALNTPADGRKFGSK--YLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHCR 135
Cdd:cd00033    1 CPPPPVPENGTVTGSKgsYSYGSTVTYSCNEGYTLVGSSTITCTENGGWSPPPPTCE 57

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 578803647  270 DVDECVGLQPVCPQGTTCINTGGSFQCVspeCPEG 304
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 578803647 137 ISECSSQ-PCQNGGTCVEGVNQYRCICPPGRTGNRCQ 172
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 578803647   224 DVNECELYGqegrprLCMHA--CVNTPGSYRCTCPGGYRtlaDGKSCE 269
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 578803647  240 CMHACVNTPGSYRCTCPGGYRTLADGKSC 268
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 578803647 139 ECS-SQPCQNGGTCVEGVNQYRCICPPGRTGNR 170
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 578803647  252 RCTCPGGYRTLADGKSCEDVDE 273
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. 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 Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.

                          10        20
                  ....*....|....*....|.
gi 578803647  145 CQNGGTCVEGVNQYRCICPPG 165
Cdd:pfam12661   1 CQNGGTCVDGVNGYKCQCPPG 21

secreted complement-binding protein; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 578803647  93 FGSKYLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHC 134
Cdd:PHA02927 220 FKRSYSYNDNVDFKCKYGYKLSGSSSSTCSPGNTWQPELPKC 261