EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878401693  194 ILLDVKPWDDETDMAKMEECVRSIEVDGLLWGASKLVPVGYGIKKLQINCVVEDDKVGTDLLEEEITKFED 264
Cdd:pfam00736    1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEIDG 71

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1878401693  500 CISGLHHCHVNARCGNVMGTYFCQCHQGYSGDGHSC 535
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36

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        30
                   ....*....|....*....|....*....|....*..
gi 1878401693  664 CALRNAGCDQLCSLGSEGRVkCSCREGWELAPDQRTC 700
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYELQDDGRTC 36

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1878401693  576 CTDVDECESGNVTCEQLCTNTPGSFLCSCRAGYQL 610
Cdd:cd01475    184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYAL 218

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 1878401693   413 DVDECTFEESCRRelGNVCVNTEGSYKCVCQPGFRE 448
Cdd:smart00179    1 DIDECASGNPCQN--GGTCVNTVGSYRCECPPGYTD 34

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 1878401693  623 CKLQNGGCSHTCSNTPGGHVCHC 645
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSC 23

RPEL repeat; The RPEL repeat is named after four conserved amino acids it contains. The RPEL motif binds to actin.

                           10        20
                   ....*....|....*....|..
gi 1878401693 1125 LERKMSTRQSREELIKRGVLRE 1146
Cdd:pfam02755    2 LERKLSHRPTREELVERNILPE 23

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;

                            10        20
                    ....*....|....*....|...
gi 1878401693  1402 DSLAIKLSNRPSKRELEDKNILP 1424
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILK 23

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 1878401693   702 DIDECAMFNG-GCEQVCANQAGSFNCTCKPGF 732
Cdd:smart00179    1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGY 32

EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878401693  194 ILLDVKPWDDETDMAKMEECVRSIEVDGLLWGASKLVPVGYGIKKLQINCVVEDDKVGTDLLEEEITKFED 264
Cdd:pfam00736    1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEIDG 71

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878401693   192 SSILLDVKPWDDETDMAKMEECVRSI-EVDGLLWGAS-KLVPVGYGIKKLQINCVVEDDKVGTDLLEEEITKFED 264
Cdd:smart00888    2 VLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG 76

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1878401693  500 CISGLHHCHVNARCGNVMGTYFCQCHQGYSGDGHSC 535
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36

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        30
                   ....*....|....*....|....*....|....*..
gi 1878401693  664 CALRNAGCDQLCSLGSEGRVkCSCREGWELAPDQRTC 700
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1878401693   455 DVDECvELDGVCTNQGECENTFGSYKCVCSHGYRgNGTHCT 495
Cdd:smart00179    1 DIDEC-ASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 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 1878401693  455 DVDECvELDGVCTNQGECENTFGSYKCVCSHGYRgnGTHCT 495
Cdd:cd00054      1 DIDEC-ASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1878401693  455 DVDECVELDGVCTNQGECENTFGSYKCVCSHG 486
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 1878401693  324 DINECAQGdeGPCGYHSNCTNTPGSFVCSCIRGY 357
Cdd:cd00054      1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGY 32

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        30
                   ....*....|....*....|....*....|....*.
gi 1878401693  541 CALRGDLCQHNCANLPGGYSCLCNAGYTLANDLHNC 576
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1878401693   366 DIDECALAAVtglqaCGRRTVCKNSPGSFTCHCPAGFVlglDGYNCV 412
Cdd:smart00179    1 DIDECASGNP-----CQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1878401693   578 DVDECESGNVtCEQ--LCTNTPGSFLCSCRAGYQlhiDRQRCV 618
Cdd:smart00179    1 DIDECASGNP-CQNggTCVNTVGSYRCECPPGYT---DGRNCE 39

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;

                            10        20
                    ....*....|....*....|...
gi 1878401693  1402 DSLAIKLSNRPSKRELEDKNILP 1424
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILK 23

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 1878401693  413 DVDECTFEESCRRelGNVCVNTEGSYKCVCQPGFR 447
Cdd:cd00054      1 DIDECASGNPCQN--GGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1878401693  413 DVDECTFE-ESCRRelGNVCVNTEGSYKCVCQPG 445
Cdd:pfam07645    1 DVDECATGtHNCPA--NTVCVNTIGSFECRCPDG 32

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1878401693   496 DVNECISGlHHCHVNARCGNVMGTYFCQCHQGYSgDGHSC 535
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNC 38

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 1878401693  395 TCHCPAGFVLGLDGYNCVDVDE 416
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

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 1878401693  602 CSCRAGYQLHIDRQRCVDIDE 622
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 22

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                           10        20        30
                   ....*....|....*....|....*....|
gi 1878401693  328 CAQGDeGPCGYHSNCTNTPGSFVCSCIRGY 357
Cdd:pfam12947    1 CSDNN-GGCHPNATCTNTGGSFTCTCNDGY 29

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 1878401693  702 DIDECAMFNG-GCEQVCANQAGSFNCTCKPGFDPRT 736
Cdd:cd00054      1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTGRN 36

EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1878401693  194 ILLDVKPWDDETDMAKMEECVRSIEVDGLLWGASKLVPVGYGIKKLQINCVVEDDKVGTDLLEEEITKFED 264
Cdd:pfam00736    1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEIDG 71

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).

                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1878401693   192 SSILLDVKPWDDETDMAKMEECVRSI-EVDGLLWGAS-KLVPVGYGIKKLQINCVVEDDKVGTDLLEEEITKFED 264
Cdd:smart00888    2 VLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG 76

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1878401693  500 CISGLHHCHVNARCGNVMGTYFCQCHQGYSGDGHSC 535
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36

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        30
                   ....*....|....*....|....*....|....*..
gi 1878401693  664 CALRNAGCDQLCSLGSEGRVkCSCREGWELAPDQRTC 700
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 1878401693   455 DVDECvELDGVCTNQGECENTFGSYKCVCSHGYRgNGTHCT 495
Cdd:smart00179    1 DIDEC-ASGNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 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 1878401693  455 DVDECvELDGVCTNQGECENTFGSYKCVCSHGYRgnGTHCT 495
Cdd:cd00054      1 DIDEC-ASGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1878401693  455 DVDECVELDGVCTNQGECENTFGSYKCVCSHG 486
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 1878401693  324 DINECAQGdeGPCGYHSNCTNTPGSFVCSCIRGY 357
Cdd:cd00054      1 DIDECASG--NPCQNGGTCVNTVGSYRCSCPPGY 32

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        30
                   ....*....|....*....|....*....|....*.
gi 1878401693  541 CALRGDLCQHNCANLPGGYSCLCNAGYTLANDLHNC 576
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1878401693   366 DIDECALAAVtglqaCGRRTVCKNSPGSFTCHCPAGFVlglDGYNCV 412
Cdd:smart00179    1 DIDECASGNP-----CQNGGTCVNTVGSYRCECPPGYT---DGRNCE 39

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1878401693   578 DVDECESGNVtCEQ--LCTNTPGSFLCSCRAGYQlhiDRQRCV 618
Cdd:smart00179    1 DIDECASGNP-CQNggTCVNTVGSYRCECPPGYT---DGRNCE 39

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1878401693  459 CVELDGVCTNQGECENTFGSYKCVCSHGYRGNGTHC 494
Cdd:pfam12947    1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36

Repeat in Drosophila CG10860, human KIAA0680 and C. elegans F26H9.2;

                            10        20
                    ....*....|....*....|...
gi 1878401693  1402 DSLAIKLSNRPSKRELEDKNILP 1424
Cdd:smart00707    1 DVLNRKLSQRPTREELEERNILK 23

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 1878401693  413 DVDECTFEESCRRelGNVCVNTEGSYKCVCQPGFR 447
Cdd:cd00054      1 DIDECASGNPCQN--GGTCVNTVGSYRCSCPPGYT 33

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....
gi 1878401693  413 DVDECTFE-ESCRRelGNVCVNTEGSYKCVCQPG 445
Cdd:pfam07645    1 DVDECATGtHNCPA--NTVCVNTIGSFECRCPDG 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 1878401693  578 DVDECESGNVtCE--QLCTNTPGSFLCSCRAGYQLH 611
Cdd:cd00054      1 DIDECASGNP-CQngGTCVNTVGSYRCSCPPGYTGR 35

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 1878401693  684 KCSCREGWELAPDQRTCLDIDE 705
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

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 1878401693  395 TCHCPAGFVLGLDGYNCVDVDE 416
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

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 1878401693  602 CSCRAGYQLHIDRQRCVDIDE 622
Cdd:pfam12662    2 CSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|..
gi 1878401693   702 DIDECAMFNG-GCEQVCANQAGSFNCTCKPGF 732
Cdd:smart00179    1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGY 32

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1878401693  702 DIDECAMFNGGCEQ--VCANQAGSFNCTCKPG 731
Cdd:pfam07645    1 DVDECATGTHNCPAntVCVNTIGSFECRCPDG 32

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1878401693  537 DIDECALRGDLCQHN--CANLPGGYSCLCNAG 566
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 1878401693  702 DIDECAMFNG-GCEQVCANQAGSFNCTCKPGFDPRT 736
Cdd:cd00054      1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTGRN 36

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.

                           10        20        30
                   ....*....|....*....|....*....|
gi 1878401693  582 CESGNVTC--EQLCTNTPGSFLCSCRAGYQ 609
Cdd:pfam12947    1 CSDNNGGChpNATCTNTGGSFTCTCNDGYT 30