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Conserved domains on  [gi|568979644|ref|XP_006515929|]
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fibulin-5 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
257-285 1.39e-07

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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 47.62  E-value: 1.39e-07
                          10        20
                  ....*....|....*....|....*....
gi 568979644  257 CQHECVNQPGSYFCSCPPGYVLLDDNRSC 285
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
206-244 4.06e-07

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.09  E-value: 4.06e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568979644   206 DVNECETENPCVQ--TCVNTYGSFICRCDPGYeleEDGIHC 244
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGY---TDGRNC 38
EGF_CA pfam07645
Calcium-binding EGF domain;
126-157 1.17e-06

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.92  E-value: 1.17e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568979644  126 DVDECATDSHQCNPTQICINTEGGYTCSCTDG 157
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
174-204 2.50e-06

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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.77  E-value: 2.50e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568979644  174 GYCQQLCANVPGSYSCTCNPGFTLNDDGRSC 204
Cdd:pfam14670   6 GGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
 
Name Accession Description Interval E-value
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
257-285 1.39e-07

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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 47.62  E-value: 1.39e-07
                          10        20
                  ....*....|....*....|....*....
gi 568979644  257 CQHECVNQPGSYFCSCPPGYVLLDDNRSC 285
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
206-244 4.06e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.09  E-value: 4.06e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568979644   206 DVNECETENPCVQ--TCVNTYGSFICRCDPGYeleEDGIHC 244
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGY---TDGRNC 38
EGF_CA pfam07645
Calcium-binding EGF domain;
126-157 1.17e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.92  E-value: 1.17e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568979644  126 DVDECATDSHQCNPTQICINTEGGYTCSCTDG 157
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
206-237 1.68e-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: 1.68e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568979644 206 DVNECETENPCV--QTCVNTYGSFICRCDPGYEL 237
Cdd:cd00054    1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTG 34
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
174-204 2.50e-06

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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.77  E-value: 2.50e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568979644  174 GYCQQLCANVPGSYSCTCNPGFTLNDDGRSC 204
Cdd:pfam14670   6 GGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
120-164 2.58e-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: 2.58e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568979644 120 EGNQCVDVDECATDSHQCNptQICINTEGGYTCSCTDGYWLLEGQ 164
Cdd:cd01475  180 QGKICVVPDLCATLSHVCQ--QVCISTPGSYLCACTEGYALLEDN 222
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
244-284 3.28e-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: 3.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568979644 244 CSDMDECSFSEFLCQHECVNQPGSYFCSCPPGYVLLDDNRS 284
Cdd:cd01475  184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_CA smart00179
Calcium-binding EGF-like domain;
126-158 3.46e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 3.46e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568979644   126 DVDECATDsHQCNPTQICINTEGGYTCSCTDGY 158
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 32
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
160-203 2.59e-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: 42.37  E-value: 2.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568979644 160 LLEGQCLDIDECRYG--YCQQLCANVPGSYSCTCNPGFTLNDDGRS 203
Cdd:cd01475  179 FQGKICVVPDLCATLshVCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_CA smart00179
Calcium-binding EGF-like domain;
246-286 2.78e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 2.78e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568979644   246 DMDECSfSEFLCQH--ECVNQPGSYFCSCPPGYVlldDNRSCQ 286
Cdd:smart00179   1 DIDECA-SGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
167-205 9.14e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 9.14e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 568979644   167 DIDEC-RYGYCQQ--LCANVPGSYSCTCNPGFTlndDGRSCQ 205
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
206-234 1.44e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 36.06  E-value: 1.44e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568979644  206 DVNECETE-NPCVQ--TCVNTYGSFICRCDPG 234
Cdd:pfam07645   1 DVDECATGtHNCPAntVCVNTIGSFECRCPDG 32
 
Name Accession Description Interval E-value
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
257-285 1.39e-07

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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 47.62  E-value: 1.39e-07
                          10        20
                  ....*....|....*....|....*....
gi 568979644  257 CQHECVNQPGSYFCSCPPGYVLLDDNRSC 285
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
206-244 4.06e-07

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 46.09  E-value: 4.06e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 568979644   206 DVNECETENPCVQ--TCVNTYGSFICRCDPGYeleEDGIHC 244
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGY---TDGRNC 38
EGF_CA pfam07645
Calcium-binding EGF domain;
126-157 1.17e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.92  E-value: 1.17e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568979644  126 DVDECATDSHQCNPTQICINTEGGYTCSCTDG 157
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
206-237 1.68e-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: 1.68e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 568979644 206 DVNECETENPCV--QTCVNTYGSFICRCDPGYEL 237
Cdd:cd00054    1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTG 34
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
174-204 2.50e-06

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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 43.77  E-value: 2.50e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 568979644  174 GYCQQLCANVPGSYSCTCNPGFTLNDDGRSC 204
Cdd:pfam14670   6 GGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
120-164 2.58e-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: 2.58e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 568979644 120 EGNQCVDVDECATDSHQCNptQICINTEGGYTCSCTDGYWLLEGQ 164
Cdd:cd01475  180 QGKICVVPDLCATLSHVCQ--QVCISTPGSYLCACTEGYALLEDN 222
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
244-284 3.28e-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: 3.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568979644 244 CSDMDECSFSEFLCQHECVNQPGSYFCSCPPGYVLLDDNRS 284
Cdd:cd01475  184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
195-242 2.30e-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: 45.45  E-value: 2.30e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568979644 195 FTLNDDGRSCQDVNECETENP-CVQTCVNTYGSFICRCDPGYELEEDGI 242
Cdd:cd01475  175 LTKKFQGKICVVPDLCATLSHvCQQVCISTPGSYLCACTEGYALLEDNK 223
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
126-160 2.77e-05

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: 41.08  E-value: 2.77e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568979644 126 DVDECATDsHQCNPTQICINTEGGYTCSCTDGYWL 160
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
126-158 3.46e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 40.69  E-value: 3.46e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 568979644   126 DVDECATDsHQCNPTQICINTEGGYTCSCTDGY 158
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 32
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
188-209 4.66e-05

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.


Pssm-ID: 463661  Cd Length: 22  Bit Score: 40.08  E-value: 4.66e-05
                          10        20
                  ....*....|....*....|..
gi 568979644  188 SCTCNPGFTLNDDGRSCQDVNE 209
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
270-290 1.01e-04

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.


Pssm-ID: 463661  Cd Length: 22  Bit Score: 38.93  E-value: 1.01e-04
                          10        20
                  ....*....|....*....|.
gi 568979644  270 CSCPPGYVLLDDNRSCQDINE 290
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
130-158 1.07e-04

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.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 39.12  E-value: 1.07e-04
                          10        20
                  ....*....|....*....|....*....
gi 568979644  130 CATDSHQCNPTQICINTEGGYTCSCTDGY 158
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGY 29
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
160-203 2.59e-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: 42.37  E-value: 2.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568979644 160 LLEGQCLDIDECRYG--YCQQLCANVPGSYSCTCNPGFTLNDDGRS 203
Cdd:cd01475  179 FQGKICVVPDLCATLshVCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_CA smart00179
Calcium-binding EGF-like domain;
246-286 2.78e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 2.78e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 568979644   246 DMDECSfSEFLCQH--ECVNQPGSYFCSCPPGYVlldDNRSCQ 286
Cdd:smart00179   1 DIDECA-SGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
246-278 6.97e-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: 37.23  E-value: 6.97e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 568979644 246 DMDECSfSEFLCQH--ECVNQPGSYFCSCPPGYVL 278
Cdd:cd00054    1 DIDECA-SGNPCQNggTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
167-205 9.14e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.84  E-value: 9.14e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 568979644   167 DIDEC-RYGYCQQ--LCANVPGSYSCTCNPGFTlndDGRSCQ 205
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPPGYT---DGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
206-234 1.44e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 36.06  E-value: 1.44e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568979644  206 DVNECETE-NPCVQ--TCVNTYGSFICRCDPG 234
Cdd:pfam07645   1 DVDECATGtHNCPAntVCVNTIGSFECRCPDG 32
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
210-244 1.57e-03

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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 36.07  E-value: 1.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 568979644  210 CETEN-PCVQTCVNTYGSFICRCDPGYELEEDGIHC 244
Cdd:pfam14670   1 CSVNNgGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
167-205 7.41e-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: 34.15  E-value: 7.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 568979644 167 DIDECR-YGYCQ--QLCANVPGSYSCTCNPGFTlnddGRSCQ 205
Cdd:cd00054    1 DIDECAsGNPCQngGTCVNTVGSYRCSCPPGYT----GRNCE 38
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
177-204 8.89e-03

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.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 33.73  E-value: 8.89e-03
                          10        20
                  ....*....|....*....|....*...
gi 568979644  177 QQLCANVPGSYSCTCNPGFTLndDGRSC 204
Cdd:pfam12947  11 NATCTNTGGSFTCTCNDGYTG--DGVTC 36
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
209-238 9.48e-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: 33.99  E-value: 9.48e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 568979644 209 ECETENPCV--QTCVNTYGSFICRCDPGYELE 238
Cdd:cd00053    1 ECAASNPCSngGTCVNTPGSYRCVCPPGYTGD 32
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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