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Conserved domains on  [gi|58865654|ref|NP_001012039|]
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EGF-containing fibulin-like extracellular matrix protein 1 precursor [Rattus norvegicus]

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List of domain hits

Name Accession Description Interval E-value
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
173-213 2.71e-06

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.


:

Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.55  E-value: 2.71e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 58865654 173 DIDECTSGtHNCRLDQVCINLRGSFTCHCLPGYqkRGEQCV 213
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY--TGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
214-244 6.72e-07

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542  Cd Length: 39  Bit Score: 46.47  E-value: 6.72e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 58865654    214 DIDECSVPPYCHQG--CVNTPGSFYCQCNPGFQ 244
Cdd:smart00179   1 DIDECASGNPCQNGgtCVNTVGSYRCECPPGYT 33
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
234-257 1.62e-05

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteristic 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.


:

Pssm-ID: 257201  Cd Length: 24  Bit Score: 42.06  E-value: 1.62e-05
                          10        20
                  ....*....|....*....|....
gi 58865654   234 SFYCQCNPGFQLAANNYTCVDINE 257
Cdd:pfam12662   1 SYTCSCPPGYQLSGDGRTCEDIDE 24
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
274-297 4.88e-05

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteristic 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.


:

Pssm-ID: 257201  Cd Length: 24  Bit Score: 40.90  E-value: 4.88e-05
                          10        20
                  ....*....|....*....|....
gi 58865654   274 SFICQCNQGYELSSDRLNCEDIDE 297
Cdd:pfam12662   1 SYTCSCPPGYQLSGDGRTCEDIDE 24
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
292-324 6.52e-04

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.


:

Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 40.06  E-value: 6.52e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 58865654 292 CEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGY 324
Cdd:cd01475 184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGY 216
EGF_CA smart00179
Calcium-binding EGF-like domain;
334-378 2.11e-03

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.07  E-value: 2.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 58865654    334 DINECETTNECREDEMCWNYHGGFRCYpqnpCQDPYvlTSENRCV 378
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCE----CPPGY--TDGRNCE 39
 
Name Accession Description Interval E-value
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
173-213 2.71e-06

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.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.55  E-value: 2.71e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 58865654 173 DIDECTSGtHNCRLDQVCINLRGSFTCHCLPGYqkRGEQCV 213
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY--TGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
214-244 6.72e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 46.47  E-value: 6.72e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 58865654    214 DIDECSVPPYCHQG--CVNTPGSFYCQCNPGFQ 244
Cdd:smart00179   1 DIDECASGNPCQNGgtCVNTVGSYRCECPPGYT 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
173-213 9.13e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 46.09  E-value: 9.13e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 58865654    173 DIDECTSGtHNCRLDQVCINLRGSFTCHCLPGYQkRGEQCV 213
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
173-206 9.89e-07

Calcium-binding EGF domain;


Pssm-ID: 254326  Cd Length: 42  Bit Score: 45.80  E-value: 9.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 58865654   173 DIDECTSGTHNCRLDQVCINLRGSFTCHCLPGYQ 206
Cdd:pfam07645   1 DVDECADGTHNCPANTVCVNTIGSFECVCPDGYE 34
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
212-251 1.36e-06

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.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 48.15  E-value: 1.36e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 58865654 212 CVDIDECSVPPY-CHQGCVNTPGSFYCQCNPGFQLAANNYT 251
Cdd:cd01475 184 CVVPDLCATLSHvCQQVCISTPGSYLCACTEGYALLEDNKT 224
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
234-257 1.62e-05

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteristic 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.


Pssm-ID: 257201  Cd Length: 24  Bit Score: 42.06  E-value: 1.62e-05
                          10        20
                  ....*....|....*....|....
gi 58865654   234 SFYCQCNPGFQLAANNYTCVDINE 257
Cdd:pfam12662   1 SYTCSCPPGYQLSGDGRTCEDIDE 24
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
274-297 4.88e-05

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteristic 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.


Pssm-ID: 257201  Cd Length: 24  Bit Score: 40.90  E-value: 4.88e-05
                          10        20
                  ....*....|....*....|....
gi 58865654   274 SFICQCNQGYELSSDRLNCEDIDE 297
Cdd:pfam12662   1 SYTCSCPPGYQLSGDGRTCEDIDE 24
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
224-252 1.75e-04

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.


Pssm-ID: 258808  Cd Length: 36  Bit Score: 39.14  E-value: 1.75e-04
                          10        20
                  ....*....|....*....|....*....
gi 58865654   224 CHQGCVNTPGSFYCQCNPGFQLAANNYTC 252
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYKLAEDGKTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
292-324 6.52e-04

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.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 40.06  E-value: 6.52e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 58865654 292 CEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGY 324
Cdd:cd01475 184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGY 216
EGF_CA smart00179
Calcium-binding EGF-like domain;
294-333 2.05e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.07  E-value: 2.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 58865654    294 DIDECrTSSYLCQY--QCVNEPGKFSCMCPQGYQvvRSRTCQ 333
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT--DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
334-378 2.11e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.07  E-value: 2.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 58865654    334 DINECETTNECREDEMCWNYHGGFRCYpqnpCQDPYvlTSENRCV 378
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCE----CPPGY--TDGRNCE 39
Plasmod_Pvs28 pfam06247
Plasmodium ookinete surface protein Pvs28; This family consists of several ookinete surface ...
233-364 8.74e-04

Plasmodium ookinete surface protein Pvs28; This family consists of several ookinete surface protein (Pvs28) from several species of Plasmodium. Pvs25 and Pvs28 are expressed on the surface of ookinetes. These proteins are potential candidates for vaccine and induce antibodies that block the infectivity of Plasmodium vivax in immunised animals.


Pssm-ID: 253638 [Multi-domain]  Cd Length: 196  Bit Score: 39.34  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865654   233 GSFYCQCNPGFQLAANNyTCVDINECDASN----------QCAQQCYNIL-GSFICQCNQGYELSSDRlnCEdIDECRts 301
Cdd:pfam06247  18 NHFECKCNEGYVLKNEN-TCEEKVKCDKLEnvnkvcgeyaTCINQANKAEeKALKCGCINGYTLSQGV--CV-PNKCN-- 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58865654   302 SYLCQY-QCVNEPG---KFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPQNP 364
Cdd:pfam06247  92 NKVCGSgKCIVDPAnpnNTTCSCNIGKVPDQNGKCTKTGETKCSLKCKENEECKLVGGYYECVCKEG 158
 
Name Accession Description Interval E-value
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
173-213 2.71e-06

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.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 44.55  E-value: 2.71e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 58865654 173 DIDECTSGtHNCRLDQVCINLRGSFTCHCLPGYqkRGEQCV 213
Cdd:cd00054   1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY--TGRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
214-244 6.72e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 46.47  E-value: 6.72e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 58865654    214 DIDECSVPPYCHQG--CVNTPGSFYCQCNPGFQ 244
Cdd:smart00179   1 DIDECASGNPCQNGgtCVNTVGSYRCECPPGYT 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
173-213 9.13e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 46.09  E-value: 9.13e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 58865654    173 DIDECTSGtHNCRLDQVCINLRGSFTCHCLPGYQkRGEQCV 213
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
173-206 9.89e-07

Calcium-binding EGF domain;


Pssm-ID: 254326  Cd Length: 42  Bit Score: 45.80  E-value: 9.89e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 58865654   173 DIDECTSGTHNCRLDQVCINLRGSFTCHCLPGYQ 206
Cdd:pfam07645   1 DVDECADGTHNCPANTVCVNTIGSFECVCPDGYE 34
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
212-251 1.36e-06

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.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 48.15  E-value: 1.36e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 58865654 212 CVDIDECSVPPY-CHQGCVNTPGSFYCQCNPGFQLAANNYT 251
Cdd:cd01475 184 CVVPDLCATLSHvCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
214-245 4.77e-06

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.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 43.78  E-value: 4.77e-06
                        10        20        30
                ....*....|....*....|....*....|....
gi 58865654 214 DIDECSVPPYCHQG--CVNTPGSFYCQCNPGFQL 245
Cdd:cd00054   1 DIDECASGNPCQNGgtCVNTVGSYRCSCPPGYTG 34
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
234-257 1.62e-05

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteristic 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.


Pssm-ID: 257201  Cd Length: 24  Bit Score: 42.06  E-value: 1.62e-05
                          10        20
                  ....*....|....*....|....
gi 58865654   234 SFYCQCNPGFQLAANNYTCVDINE 257
Cdd:pfam12662   1 SYTCSCPPGYQLSGDGRTCEDIDE 24
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
274-297 4.88e-05

Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved cysteine residues disulfide-bonded into the characteristic 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.


Pssm-ID: 257201  Cd Length: 24  Bit Score: 40.90  E-value: 4.88e-05
                          10        20
                  ....*....|....*....|....
gi 58865654   274 SFICQCNQGYELSSDRLNCEDIDE 297
Cdd:pfam12662   1 SYTCSCPPGYQLSGDGRTCEDIDE 24
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
164-205 6.22e-05

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.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 43.14  E-value: 6.22e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 58865654 164 EQSEHNVCQDIDECTSGTHNCrlDQVCINLRGSFTCHCLPGY 205
Cdd:cd01475 177 KKFQGKICVVPDLCATLSHVC--QQVCISTPGSYLCACTEGY 216
EGF_CA smart00179
Calcium-binding EGF-like domain;
254-293 1.42e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 39.54  E-value: 1.42e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 58865654    254 DINECDASNQCAQ--QCYNILGSFICQCNQGYElssDRLNCE 293
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
224-252 1.75e-04

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.


Pssm-ID: 258808  Cd Length: 36  Bit Score: 39.14  E-value: 1.75e-04
                          10        20
                  ....*....|....*....|....*....
gi 58865654   224 CHQGCVNTPGSFYCQCNPGFQLAANNYTC 252
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYKLAEDGKTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
252-291 2.79e-04

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.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 41.22  E-value: 2.79e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 58865654 252 CVDINECD-ASNQCAQQCYNILGSFICQCNQGYELSSDRLN 291
Cdd:cd01475 184 CVVPDLCAtLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
292-324 6.52e-04

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.


Pssm-ID: 238752 [Multi-domain]  Cd Length: 224  Bit Score: 40.06  E-value: 6.52e-04
                        10        20        30
                ....*....|....*....|....*....|...
gi 58865654 292 CEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGY 324
Cdd:cd01475 184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGY 216
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
254-285 6.82e-04

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.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 37.62  E-value: 6.82e-04
                        10        20        30
                ....*....|....*....|....*....|....
gi 58865654 254 DINECDASNQCA--QQCYNILGSFICQCNQGYEL 285
Cdd:cd00054   1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTG 34
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologues. This family includes ...
177-212 7.49e-04

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


Pssm-ID: 257421  Cd Length: 36  Bit Score: 37.52  E-value: 7.49e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 58865654   177 CTSGTHNCRLDQVCINLRGSFTCHCLPGYQKRGEQC 212
Cdd:pfam12947   1 CSENNGGCHPNATCTNTGGSFTCTCKSGYTGDGVTC 36
EGF_CA pfam07645
Calcium-binding EGF domain;
214-252 1.07e-03

Calcium-binding EGF domain;


Pssm-ID: 254326  Cd Length: 42  Bit Score: 36.94  E-value: 1.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 58865654   214 DIDECSVPPY-CHQG--CVNTPGSFYCQCNPGFQLAANNYTC 252
Cdd:pfam07645   1 DVDECADGTHnCPANtvCVNTIGSFECVCPDGYENNEDGTNC 42
EGF smart00181
Epidermal growth factor-like domain;
217-248 1.50e-03

Epidermal growth factor-like domain;


Pssm-ID: 214544  Cd Length: 35  Bit Score: 36.73  E-value: 1.50e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 58865654    217 ECSVPPYCHQG-CVNTPGSFYCQCNPGFQLAAN 248
Cdd:smart00181   1 ECASGGPCSNGtCINTPGSYTCSCPPGYTGDKR 33
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
217-248 1.72e-03

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.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 36.30  E-value: 1.72e-03
                        10        20        30
                ....*....|....*....|....*....|....
gi 58865654 217 ECSVPPYCHQG--CVNTPGSFYCQCNPGFQLAAN 248
Cdd:cd00053   1 ECAASNPCSNGgtCVNTPGSYRCVCPPGYTGDRS 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
294-333 2.05e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.07  E-value: 2.05e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 58865654    294 DIDECrTSSYLCQY--QCVNEPGKFSCMCPQGYQvvRSRTCQ 333
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT--DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
334-378 2.11e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.07  E-value: 2.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 58865654    334 DINECETTNECREDEMCWNYHGGFRCYpqnpCQDPYvlTSENRCV 378
Cdd:smart00179   1 DIDECASGNPCQNGGTCVNTVGSYRCE----CPPGY--TDGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
294-333 3.91e-03

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.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 35.30  E-value: 3.91e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 58865654 294 DIDECrTSSYLCQY--QCVNEPGKFSCMCPQGYqvvRSRTCQ 333
Cdd:cd00054   1 DIDEC-ASGNPCQNggTCVNTVGSYRCSCPPGY---TGRNCE 38
Plasmod_Pvs28 pfam06247
Plasmodium ookinete surface protein Pvs28; This family consists of several ookinete surface ...
233-364 8.74e-04

Plasmodium ookinete surface protein Pvs28; This family consists of several ookinete surface protein (Pvs28) from several species of Plasmodium. Pvs25 and Pvs28 are expressed on the surface of ookinetes. These proteins are potential candidates for vaccine and induce antibodies that block the infectivity of Plasmodium vivax in immunised animals.


Pssm-ID: 253638 [Multi-domain]  Cd Length: 196  Bit Score: 39.34  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58865654   233 GSFYCQCNPGFQLAANNyTCVDINECDASN----------QCAQQCYNIL-GSFICQCNQGYELSSDRlnCEdIDECRts 301
Cdd:pfam06247  18 NHFECKCNEGYVLKNEN-TCEEKVKCDKLEnvnkvcgeyaTCINQANKAEeKALKCGCINGYTLSQGV--CV-PNKCN-- 91
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58865654   302 SYLCQY-QCVNEPG---KFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPQNP 364
Cdd:pfam06247  92 NKVCGSgKCIVDPAnpnNTTCSCNIGKVPDQNGKCTKTGETKCSLKCKENEECKLVGGYYECVCKEG 158
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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