Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940646  420 PRGDLDGSTKD-LIETCCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCCISYLKEKSC 479
Cdd:cd00017     1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDE 61

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568940646  505 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 553
Cdd:cd00017    11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 568940646    895 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQRdafGRTCI 937
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD---GRNCE 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 568940646   950 CQHTCENTPGSYRCSCAAGFLLAADGKHC 978
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 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 568940646  1001 QCYCRQGYQLAEDGHTCTDIDE 1022
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568940646   756 DINECVTDLHTCTRAEHCVNTPGSFQCykalTCEPG 791
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 32

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 568940646   1019 DIDECAQGAGILCTFRCVNVPGSYQCACPEqGYTmmaNGRSCK 1061
Cdd:smart00179    1 DIDECASGNPCQNGGTCVNTVGSYRCECPP-GYT---DGRNCE 39

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940646  420 PRGDLDGSTKD-LIETCCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCCISYLKEKSC 479
Cdd:cd00017     1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDE 61

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568940646  505 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 553
Cdd:cd00017    11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 568940646    895 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQRdafGRTCI 937
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD---GRNCE 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 568940646  895 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQrdafGRTCI 937
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940646  287 PPTAGSPGRLDSLPTRSPA-RPGFP-VQEKEAEAKAGPEENLiPDAQVTPRSVMQEGAAPLPrsglaalspsLATDSSSE 364
Cdd:PHA03247 2556 PPAAPPAAPDRSVPPPRPApRPSEPaVTSRARRPDAPPQSAR-PRAPVDDRGDPRGPAPPSP----------LPPDTHAP 2624

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568940646  365 DPVKPSDHPTLSTLPPDRAQVSPSPETPEEIPQHPQLLPRFRAEEDIDPNSVHSVPRG 422
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR 2682

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 568940646    435 CCAAGQQWAIDNDECQEIPENGAQSDiCRIAQRQCC 470
Cdd:smart00104    1 CCADGMRLAPMGETCEERAARINSGD-CRKAFLQCC 35

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 568940646    847 DINECTSLlEPCRSGFSCINTVGSYTCQrnplvCGRGYH 885
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCE-----CPPGYT 33

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568940646   756 DINECVTDLHTCTRAEHCVNTPGSFQCykalTCEPG 791
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 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        40
                  ....*....|....*....|....*....|....*....|...
gi 568940646  707 CEDQDECLMGTHDCswKQFCVNTLGSFYCVnhtvlCAEGYILN 749
Cdd:cd01475   184 CVVPDLCATLSHVC--QQVCISTPGSYLCA-----CTEGYALL 219

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940646   287 PPTAGSPGRLDSLPTRSPARPGFPVQEKEAEAKAGPEENLIPDAQVTPRSVMQEGAAPLPRSGLAALS------------ 354
Cdd:pfam03154  312 GPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPPHLSgpspfqmnsnlp 391

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568940646   355 --PSLATDSSSEDPVKPSDHPTLSTLPPDRAQVSPSPETPEEIPQHPQLLPrfRAEEDIDPNSVHSVP 420
Cdd:pfam03154  392 ppPALKPLSSLSTHHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLPP--PAASHPPTSGLHQVP 457

Calcium-binding EGF domain;

                           10        20
                   ....*....|....*....|....*...
gi 568940646   847 DINECTSLLEPCRSGFSCINTVGSYTCQ 874
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Anaphylotoxin-like domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568940646   435 CCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCC 470
Cdd:pfam01821    1 CCLDGMKRNPMGRSCEQRAARIKEGPRCRKAFLQCC 36

Calcium-binding EGF domain;

                           10        20
                   ....*....|....*....|....*...
gi 568940646   709 DQDECLMGTHDCSWKQFCVNTLGSFYCV 736
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

                            10        20        30
                    ....*....|....*....|....*....|....*
gi 568940646    511 CCGLGLRVRAEGQSCESNPNLGY--PCNHVMLSCC 543
Cdd:smart00104    1 CCADGMRLAPMGETCEERAARINsgDCRKAFLQCC 35

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 568940646 1019 DIDECAQGAGILCTFRCVNVPGSYQCACPEqGYTmmanGRSCK 1061
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPP-GYT----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 568940646  801 DVDECVTGtHNCQAGFSCQNTKGSFYCQarqrCMDGF 837
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCS----CPPGY 32

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568940646  420 PRGDLDGSTKD-LIETCCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCCISYLKEKSC 479
Cdd:cd00017     1 KNSEKAAQYKDkELRKCCLDGMRENPMGQTCEERAAYITDGKECRKAFLECCVYAEELRDE 61

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to repeats in fibulins.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568940646  505 YKQCCDCCGLGLRVRAEGQSCESNP---NLGYPCNHVMLSCCEGEEPLIVPE 553
Cdd:cd00017    11 DKELRKCCLDGMRENPMGQTCEERAayiTDGKECRKAFLECCVYAEELRDEE 62

Calcium-binding EGF-like domain;

                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 568940646    895 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQRdafGRTCI 937
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD---GRNCE 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 568940646  895 DVNECETGvHRCGEGQLCYNLPGSYRCDCKPGFQrdafGRTCI 937
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT----GRNCE 38

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940646  287 PPTAGSPGRLDSLPTRSPA-RPGFP-VQEKEAEAKAGPEENLiPDAQVTPRSVMQEGAAPLPrsglaalspsLATDSSSE 364
Cdd:PHA03247 2556 PPAAPPAAPDRSVPPPRPApRPSEPaVTSRARRPDAPPQSAR-PRAPVDDRGDPRGPAPPSP----------LPPDTHAP 2624

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568940646  365 DPVKPSDHPTLSTLPPDRAQVSPSPETPEEIPQHPQLLPRFRAEEDIDPNSVHSVPRG 422
Cdd:PHA03247 2625 DPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQR 2682

Anaphylatoxin homologous domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

                            10        20        30
                    ....*....|....*....|....*....|....*.
gi 568940646    435 CCAAGQQWAIDNDECQEIPENGAQSDiCRIAQRQCC 470
Cdd:smart00104    1 CCADGMRLAPMGETCEERAARINSGD-CRKAFLQCC 35

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 568940646   989 CSQECANIYGSYQCYCRQGYQLAEDGHTC 1017
Cdd:pfam14670    8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 568940646    847 DINECTSLlEPCRSGFSCINTVGSYTCQrnplvCGRGYH 885
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCE-----CPPGYT 33

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568940646   756 DINECVTDLHTCTRAEHCVNTPGSFQCykalTCEPG 791
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFEC----RCPDG 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        40
                  ....*....|....*....|....*....|....*....|...
gi 568940646  707 CEDQDECLMGTHDCswKQFCVNTLGSFYCVnhtvlCAEGYILN 749
Cdd:cd01475   184 CVVPDLCATLSHVC--QQVCISTPGSYLCA-----CTEGYALL 219

Calcium-binding EGF domain;

                           10        20        30
                   ....*....|....*....|....*....|..
gi 568940646   895 DVNECETGVHRCGEGQLCYNLPGSYRCDCKPG 926
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940646  290 AGSPGRLDSLPTRSPARPGFPVQEKEAEAKAGPEEnliPDAQVTPRSVMQEGAAPLPRSGLAALSPSLATDSSSEDPvkp 369
Cdd:PHA03247 2731 ASPALPAAPAPPAVPAGPATPGGPARPARPPTTAG---PPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDP--- 2804

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940646  370 SDHPTL-----STLPPDRAQVSPSPETPEEIPQHPQLLPRFRAEEDIDPNSVhsVPRGDL 424
Cdd:PHA03247 2805 ADPPAAvlapaAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV--APGGDV 2862

Calcium-binding EGF domain;

                           10        20
                   ....*....|....*....|....*...
gi 568940646   847 DINECTSLLEPCRSGFSCINTVGSYTCQ 874
Cdd:pfam07645    1 DVDECATGTHNCPANTVCVNTIGSFECR 28

Anaphylotoxin-like domain; C3a, C4a and C5a anaphylatoxins are protein fragments generated enzymatically in serum during activation of complement molecules C3, C4, and C5. They induce smooth muscle contraction. These fragments are homologous to a three-fold repeat in fibulins.

                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 568940646   435 CCAAGQQWAIDNDECQEIPENGAQSDICRIAQRQCC 470
Cdd:pfam01821    1 CCLDGMKRNPMGRSCEQRAARIKEGPRCRKAFLQCC 36

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 568940646    756 DINECVTDlHTCTRAEHCVNTPGSFQCykalTCEPGY 792
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRC----ECPPGY 32

Calcium-binding EGF-like domain;

                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 568940646    801 DVDECVTGtHNCQAGFSCQNTKGSFYCQarqrCMDGF 837
Cdd:smart00179    1 DIDECASG-NPCQNGGTCVNTVGSYRCE----CPPGY 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        40
                  ....*....|....*....|....*....|....*....|.
gi 568940646  594 DQDECLMLPGELCQHLCINTVGSYRCACFPGFElqgdGRTC 634
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPPGYT----GRNC 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        40
                  ....*....|....*....|....*....|....*....|...
gi 568940646 1019 DIDECAQGAGILCTFRCVNVPGSYQCACPEqGYTmmanGRSCK 1061
Cdd:cd00054     1 DIDECASGNPCQNGGTCVNTVGSYRCSCPP-GYT----GRNCE 38

large tegument protein UL36; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940646  288 PTAGSPGRLDSLPTRSP----ARPGFPVQ-EKEAEAKAGPEENLIPDAQVTPRSVMQEGAAPLPRSGL-------AALSP 355
Cdd:PHA03247 2866 PPSRSPAAKPAAPARPPvrrlARPAVSRStESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPpppprpqPPLAP 2945

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568940646  356 SLATDSSSEdPVKPSDHPTLSTLPPDRAQV----SPSPETPEEIPQHPQllprfraeediDPNSVHSVPR 421
Cdd:PHA03247 2946 TTDPAGAGE-PSGAVPQPWLGALVPGRVAVprfrVPQPAPSREAPASST-----------PPLTGHSLSR 3003

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 568940646  801 DVDECVTGtHNCQAGFSCQNTKGSFYCQarqrCMDGF 837
Cdd:cd00054     1 DIDECASG-NPCQNGGTCVNTVGSYRCS----CPPGY 32

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 568940646  898 ECETGvHRCGEGQLCYNLPGSYRCDCKPGFQRD 930
Cdd:cd00053     1 ECAAS-NPCSNGGTCVNTPGSYRCVCPPGYTGD 32