Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720390250 642 GHHSGDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAVSFQDC 689
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

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 1720390250  33 CVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHC 68
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 1720390250 281 CRLNNGGCDHICRNTVGSFECSCKKGYKLLINERSC 316
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 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 1720390250 201 CNYGNGGCQHTCDDTEQGPRCGCHVKFVLHTDGKTC 236
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1720390250   70 DVDECEREDNAGCVHDCVNIPGNYRCTCYDGFhlaHDGHNC 110
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY---TDGRNC 38

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720390250  357 DVDECSiNKGGCRFG--CINTPGSYQCTCPAGqgrlHWNGKDCT 398
Cdd:smart00179   1 DIDECA-SGNPCQNGgtCVNTVGSYRCECPPG----YTDGRNCE 39

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390250 750 CGGELGEFTGYIESPNYPGNYPAGVECVWNINPPPKRKILIVVPEIFLPSEDECG-DVLVMRKNSSPSSITTYETCqTYE 828
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720390250 829 RPIAFTARSRKLWINFKTSEANSARGFQIPY 859
Cdd:pfam00431  80 IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720390250 642 GHHSGDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAVSFQDC 689
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

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 1720390250  33 CVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHC 68
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 1720390250 281 CRLNNGGCDHICRNTVGSFECSCKKGYKLLINERSC 316
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 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 1720390250 201 CNYGNGGCQHTCDDTEQGPRCGCHVKFVLHTDGKTC 236
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1720390250  318 DIDECSFDRTCDH--MCVNTPGSFQCLCHRGY 347
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGY 32

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
                  ....*....|....*....|....*....|....*...
gi 1720390250 313 ERSCQDIDECS-FDRTCDHMCVNTPGSFQCLCHRGYLL 349
Cdd:cd01475   181 GKICVVPDLCAtLSHVCQQVCISTPGSYLCACTEGYAL 218

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 1720390250  29 DVDECVEGtDNCHIDAICQNTPRSYKCICKSGYTgdGKHCK 69
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38

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 1720390250 161 CMNKNHGCAHICRETPkGGIACECRPGFELTKNQRDC 197
Cdd:pfam14670   1 CSVNNGGCSHLCLNTP-GGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1720390250  112 DVDECAEGNG-GCQQSCVNMMGSYECHCRDGF 142
Cdd:smart00179   1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGY 32

Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis factor receptor homolog 3 (TNFRH3); TNFRSF26 (also known as tumor necrosis factor receptor homolog 3 (TNFRH3) or TNFRSF24) is predominantly expressed in embryos and lymphoid cell types, along with its closely related TNFRSF22 and TNFRSF23 orthologs, and is developmentally regulated. Unlike TNFRSF22/23, TNFRSF26 does not serve as a TRAIL decoy receptor; it remains an orphan receptor.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390250 625 CRPGQHRAGTKCGQ-CPPGHH------SGDGFKPCQPCPRGTYQPEA-GRTLCFPCGGGLTTKHEGAVSFQDCDTKVQCS 696
Cdd:cd15837     1 CGPGEYKSANLCCQlCPAGHYvsepcqENHGVGECAPCEPGTFTAHPnGETSCFPCSQCRDDQEVVAECSATSDRQCQCK 80

                          90       100
                  ....*....|....*....|....*
gi 1720390250 697 PGHYYN-----TSIHRCIRCAVGSY 716
Cdd:cd15837    81 QGHFYCdenclESCFRCSRCPGGRV 105

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 1720390250  70 DVDECEREDNAGCVHDCVNIPGNYRCTCYDGFHLAH 105
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYTGRN 36

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 1720390250 357 DVDECSINkGGCRFG--CINTPGSYQCTCPAG 386
Cdd:cd00054     1 DIDECASG-NPCQNGgtCVNTVGSYRCSCPPG 31

CUB domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720390250 750 CGGELGEFTGYIESPNYPGNYPAGVECVWNINPPPKRKILIVVPEIFLPSEDECG-DVLVMRKNSSPSSITTYETCqTYE 828
Cdd:pfam00431   1 CGGVLTDSSGSISSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEDHDECGyDYVEIRDGPSASSPLLGRFC-GSG 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720390250 829 RPIAFTARSRKLWINFKTSEANSARGFQIPY 859
Cdd:pfam00431  80 IPEDIVSSSNQMTIKFVSDASVQKRGFKATY 110

Tyrosine-protein kinase ephrin type A/B receptor-like; This family has repeats of a region rich in cysteines. It is found in various ephrin type A and B receptors, which have tyrosine kinase activity.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1720390250 642 GHHSGDGFKPCQPCPRGTYQPEAGRTLCFPCGGGLTTKHEGAVSFQDC 689
Cdd:pfam07699   1 GTYSNTGLEPCIPCPRGTYQPEEGQLSCLACPLGTTTDSPGATSISDC 48

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 1720390250  33 CVEGTDNCHIDAICQNTPRSYKCICKSGYTGDGKHC 68
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 1720390250 281 CRLNNGGCDHICRNTVGSFECSCKKGYKLLINERSC 316
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF domain;

                          10        20        30
                  ....*....|....*....|....*....|..
gi 1720390250  29 DVDECVEGTDNCHIDAICQNTPRSYKCICKSG 60
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1720390250   29 DVDECVEGtDNCHIDAICQNTPRSYKCICKSGYTgDGKHCK 69
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39

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 1720390250 110 CLDVDECAEGNGGCQQSCVNMMGSYECHCRDGFFLSDNQHT 150
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1720390250   70 DVDECEREDNAGCVHDCVNIPGNYRCTCYDGFhlaHDGHNC 110
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCECPPGY---TDGRNC 38

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 1720390250 273 KTCKDIDECRLNNGGCDHICRNTVGSFECSCKKGYKLLINERS 315
Cdd:cd01475   182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224

Calcium-binding EGF-like domain;

                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720390250  357 DVDECSiNKGGCRFG--CINTPGSYQCTCPAGqgrlHWNGKDCT 398
Cdd:smart00179   1 DIDECA-SGNPCQNGgtCVNTVGSYRCECPPG----YTDGRNCE 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
                  ....*....|....*....|....*....|..
gi 1720390250 318 DIDECSFDRTCDHM--CVNTPGSFQCLCHRGY 347
Cdd:cd00054     1 DIDECASGNPCQNGgtCVNTVGSYRCSCPPGY 32

Calcium-binding EGF-like domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 1720390250  277 DIDECRLNNG-GCDHICRNTVGSFECSCKKGY 307
Cdd:smart00179   1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGY 32

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 1720390250 259 HCSCPVGFMLQPDRKTCKDIDE 280
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

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 1720390250 361 CSINKGGCRFGCINTPGSYQCTCPAGQgRLHWNGKDC 397
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGY-ELQDDGRTC 36

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 1720390250  94 RCTCYDGFHLAHDGHNCLDVDE 115
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22

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 1720390250 112 DVDECAEGNG-GCQQSCVNMMGSYECHCRDGF 142
Cdd:cd00054     1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGY 32

Tumor necrosis factor receptor superfamily member 14 (TNFRSF14) in teleost; also known as herpes virus entry mediator (HVEM); This subfamily of TNFRSF14 (also known as herpes virus entry mediator or HVEM, ATAR, CD270, HVEA, LIGHTR, TR2) is found in teleosts, many of which are as yet uncharacterized. It regulates T-cell immune responses by activating inflammatory as well as inhibitory signaling pathways. HVEM acts as a receptor for the canonical TNF-related ligand LIGHT (lymphotoxin-like), which exhibits inducible expression, and competes with herpes simplex virus glycoprotein D for HVEM. It also acts as a ligand for the immunoglobulin superfamily proteins BTLA (B and T lymphocyte attenuator) and CD160, a feature distinguishing HVEM from other immune regulatory molecules, thus, creating a functionally diverse set of intrinsic and bidirectional signaling pathways. HVEM is highly expressed in the gut epithelium. Genome-wide association studies have shown that HVEM is an inflammatory bowel disease (IBD) risk gene, suggesting that HVEM could have a regulatory role influencing the regulation of epithelial barrier, host defense, and the microbiota. Mouse models have revealed that HVEM is involved in colitis pathogenesis, mucosal host defense, and epithelial immunity, thus acting as a mucosal gatekeeper with multiple regulatory functions in the mucosa. HVEM plays a critical role in both tumor progression and resistance to antitumor immune responses, possibly through direct and indirect mechanisms. It is known to be expressed in several human malignancies, including esophageal squamous cell carcinoma, follicular lymphoma, and melanoma. HVEM network may therefore be an attractive target for drug intervention. In Asian seabass, the up-regulation of differentially expressed TNFRSF14 gene has been observed.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720390250 625 CRPGQHRA-GTKCGQCPPGHH-----SGDGFKPCQPCPRGTYQPEA-GRTLCFPC-----GGGLTTKHE 681
Cdd:cd13405     1 CGPAEYEInGECCPMCPPGSRvsrhcTEDTSTSCVPCPDGTYMDEPnGLEKCFPCtncdpGFGLRVKQG 69

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        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720390250  52 SYKCICKSGYTGDGKHCKDVDECEREDNaGCVHDCVNIPGNYRCTCYDGFHLAHDG 107
Cdd:cd01475   168 DFSTIEELTKKFQGKICVVPDLCATLSH-VCQQVCISTPGSYLCACTEGYALLEDN 222