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 1381378387  659 NPCVS-NPCNNEGICMgDEPDAFRCSCQQGWTGRTC 693
Cdd:cd00054      3 DECASgNPCQNGGTCV-NTVGSYRCSCPPGYTGRNC 37

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381378387  297 STWG--ISPKSTETENYTHSApSTGIT-GRDVTDSfkGVFSETGSPASSSGTQSITGHpNATEQQHTSTSEEPSDSTSSi 373
Cdd:NF033849   257 HSVGtsESHSVGTSQSQSHTT-GHGSTrGWSHTQS--TSESESTGQSSSVGTSESQSH-GTTEGTSTTDSSSHSQSSSY- 331

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1381378387  374 rvtepSTDQSQMSFSSTPPFTSPAGGPTNISGTEQGLGSSSGASTEFSTGDHSSSTQSGTEGLSSQTREGNVDLGLTA 451
Cdd:NF033849   332 -----NVSSGTGVSSSHSDGTSQSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTS 404

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 1381378387  696 DIDECKQKQePCPKGSTCVNTNGSFSCECPLGFdleDGRTC 736
Cdd:cd00054      1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGY---TGRNC 37

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 1381378387  659 NPCVS-NPCNNEGICMgDEPDAFRCSCQQGWTGRTC 693
Cdd:cd00054      3 DECASgNPCQNGGTCV-NTVGSYRCSCPPGYTGRNC 37

Variant-specific surface protein (VSP); Provisional

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381378387  840 LCAAQKTQCDEERSSCTDTSGiaCCQCREGYYKHNPDDLYCLECGDGLKLENGTCVPCMFGFGGFNCGNFYKLIAVVVSP 919
Cdd:PTZ00382     1 MTPAVCTSCDSDKKPNKDGSG--CVLCSVGNCKSCVVDGVCGECNSGFSLDNGKCVSSGANRSGLSTGAIAGISVAVVAV 78

                   ...
gi 1381378387  920 AGG 922
Cdd:PTZ00382    79 VGG 81

serine-rich protein; This serine-rich protein belongs to a family with large size (over 1000 amino acids), which a highly serine-rich central region that averages over 300 aa in length. Species encoding members of this family of proteins tend to be anaerobic bacteria, including Gram-positive bacteria of the human gut microbiome and Chloroflexi from marine sediments.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1381378387  297 STWG--ISPKSTETENYTHSApSTGIT-GRDVTDSfkGVFSETGSPASSSGTQSITGHpNATEQQHTSTSEEPSDSTSSi 373
Cdd:NF033849   257 HSVGtsESHSVGTSQSQSHTT-GHGSTrGWSHTQS--TSESESTGQSSSVGTSESQSH-GTTEGTSTTDSSSHSQSSSY- 331

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1381378387  374 rvtepSTDQSQMSFSSTPPFTSPAGGPTNISGTEQGLGSSSGASTEFSTGDHSSSTQSGTEGLSSQTREGNVDLGLTA 451
Cdd:NF033849   332 -----NVSSGTGVSSSHSDGTSQSTSISHSESSSESTGTSVGHSTSSSVSSSESSSRSSSSGVSGGFSGGIAGGGVTS 404

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 1381378387  696 DIDECKQKQePCPKGSTCVNTNGSFSCECPLGFdleDGRTC 736
Cdd:cd00054      1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGY---TGRNC 37

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 1381378387  659 NPCVS-NPCNNEGICMgDEPDAFRCSCQQGWTGRTC 693
Cdd:cd00054      3 DECASgNPCQNGGTCV-NTVGSYRCSCPPGYTGRNC 37

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 1381378387  699 ECKQKQePCPKGSTCVNTNGSFSCECPLGFDLEdgRTC 736
Cdd:cd00053      1 ECAASN-PCSNGGTCVNTPGSYRCVCPPGYTGD--RSC 35

Epidermal growth factor-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 1381378387   699 ECKQKQePCPKGsTCVNTNGSFSCECPLGFdlEDGRTCS 737
Cdd:smart00181    1 ECASGG-PCSNG-TCINTPGSYTCSCPPGY--TGDKRCE 35

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 1381378387  660 PC-VSNPCNNEGICMgDEPDAFRCSCQQGWTG-RTC 693
Cdd:cd00053      1 ECaASNPCSNGGTCV-NTPGSYRCVCPPGYTGdRSC 35

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 1381378387  707 CPKGSTCVNTNGSFSCECPLGF 728
Cdd:pfam12661    1 CQNGGTCVDGVNGYKCQCPPGY 22