Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 189491647  224 DVDECVGLQPVCPQGTTCINTGGSFQCVspeCPEG 258
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR---CPDG 32

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 189491647   178 DVNECELYGqegrprLCMHA--CVNTPGSYRCTCPGGYRtlaDGKSCE 223
Cdd:smart00179   1 DIDECASGN------PCQNGgtCVNTVGSYRCECPPGYT---DGRNCE 39

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); 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. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 189491647    81 CPALNTPADGRKFGSK--YLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHC 134
Cdd:smart00032   1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

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 189491647 137 ISECSSQ-PCQNGGTCVEGVNQYRCICPPGRTGNRCQ 172
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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 189491647  140 CSSQPCQNGGTCVEGVNQYRCICPPGRTGNR 170
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 189491647   139 ECSS-QPCQNGGTCVEGVNQYRCICPPG-RTGNRCQ 172
Cdd:smart00179   4 ECASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 39

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 189491647 178 DVNECELYGqegrprLCMH--ACVNTPGSYRCTCPGGYRtladGKSCE 223
Cdd:cd00054    1 DIDECASGN------PCQNggTCVNTVGSYRCSCPPGYT----GRNCE 38

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 189491647 224 DVDECVGLQPvCPQGTTCINTGGSFQCvspECPEG 258
Cdd:cd00054    1 DIDECASGNP-CQNGGTCVNTVGSYRC---SCPPG 31

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); 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. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 189491647    81 CPALNTPADGRKFGSK--YLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHC 134
Cdd:smart00032   1 CPPPPDIENGTVTSSSgtYSYGDTVTYSCDPGYTLIGSSTITCLENGTWSPPPPTC 56

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 189491647 137 ISECSSQ-PCQNGGTCVEGVNQYRCICPPGRTGNRCQ 172
Cdd:cd00054    2 IDECASGnPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38

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 189491647  140 CSSQPCQNGGTCVEGVNQYRCICPPGRTGNR 170
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 189491647   139 ECSS-QPCQNGGTCVEGVNQYRCICPPG-RTGNRCQ 172
Cdd:smart00179   4 ECASgNPCQNGGTCVNTVGSYRCECPPGyTDGRNCE 39

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 189491647 178 DVNECELYGqegrprLCMH--ACVNTPGSYRCTCPGGYRtladGKSCE 223
Cdd:cd00054    1 DIDECASGN------PCQNggTCVNTVGSYRCSCPPGYT----GRNCE 38

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 189491647   224 DVDECVGLQPvCPQGTTCINTGGSFQCvspECPEG 258
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRC---ECPPG 31

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 189491647  206 RCTCPGGYRTLADGKSCEDVDE 227
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

EEV Host range protein; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 189491647  82 PAL-NTPADGRKFGSKYLVDHEVHFTCNPGFRLVGPSSVVCLPNGTWTGEQPHC 134
Cdd:PHA02817  92 PALqNGFVNGIPDSKKFYYESEVSFSCKPGFVLIGTKYSVCGINSSWIPKVPIC 145