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Conserved domains on  [gi|56693245|ref|NP_001008587|]
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EGF-containing fibulin-like extracellular matrix protein 2 precursor [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EGF_CA pfam07645
Calcium-binding EGF domain;
120-159 5.05e-06

Calcium-binding EGF domain;


:

Pssm-ID: 311536  Cd Length: 42  Bit Score: 44.65  E-value: 5.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 56693245   120 DVDECERDSHDCQPSQQCFNTEGSFSCQCPDGYR--KVGTEC 159
Cdd:pfam07645   1 DVDECADGTHNCPANTVCVNTIGSFECVCPDGYEnnEDGTNC 42
EGF_CA pfam07645
Calcium-binding EGF domain;
200-238 4.11e-05

Calcium-binding EGF domain;


:

Pssm-ID: 311536  Cd Length: 42  Bit Score: 41.95  E-value: 4.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 56693245   200 DVDECGMGA---PCSQWCYNTYGTFLCRCEQGYELGPDGFAC 238
Cdd:pfam07645   1 DVDECADGThncPANTVCVNTIGSFECVCPDGYENNEDGTNC 42
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
180-203 1.22e-04

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: 315355  Cd Length: 24  Bit Score: 40.50  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|....
gi 56693245   180 SFSCQCEPGFQLAGNNRSCIDVDE 203
Cdd:pfam12662   1 SYTCSCPPGYTLAGDGRTCVDIDE 24
EGF_CA smart00179
Calcium-binding EGF-like domain;
161-190 2.33e-03

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.84  E-value: 2.33e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 56693245    161 DIDEC-RYRYCQH--RCVNVPGSFSCQCEPGFQ 190
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPPGYT 33
 
Name Accession Description Interval E-value
EGF_CA pfam07645
Calcium-binding EGF domain;
120-159 5.05e-06

Calcium-binding EGF domain;


Pssm-ID: 311536  Cd Length: 42  Bit Score: 44.65  E-value: 5.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 56693245   120 DVDECERDSHDCQPSQQCFNTEGSFSCQCPDGYR--KVGTEC 159
Cdd:pfam07645   1 DVDECADGTHNCPANTVCVNTIGSFECVCPDGYEnnEDGTNC 42
EGF_CA smart00179
Calcium-binding EGF-like domain;
120-160 8.34e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 44.16  E-value: 8.34e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 56693245    120 DVDECERDsHDCQPSQQCFNTEGSFSCQCPDGYRKvGTECI 160
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD-GRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
120-160 1.69e-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: 43.01  E-value: 1.69e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 56693245 120 DVDECErDSHDCQPSQQCFNTEGSFSCQCPDGYRkvGTECI 160
Cdd:cd00054   1 DIDECA-SGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA pfam07645
Calcium-binding EGF domain;
200-238 4.11e-05

Calcium-binding EGF domain;


Pssm-ID: 311536  Cd Length: 42  Bit Score: 41.95  E-value: 4.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 56693245   200 DVDECGMGA---PCSQWCYNTYGTFLCRCEQGYELGPDGFAC 238
Cdd:pfam07645   1 DVDECADGThncPANTVCVNTIGSFECVCPDGYENNEDGTNC 42
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
180-203 1.22e-04

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: 315355  Cd Length: 24  Bit Score: 40.50  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|....
gi 56693245   180 SFSCQCEPGFQLAGNNRSCIDVDE 203
Cdd:pfam12662   1 SYTCSCPPGYTLAGDGRTCVDIDE 24
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
195-235 2.87e-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  Cd Length: 224  Bit Score: 41.99  E-value: 2.87e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 56693245 195 NRSCIDVDECGMGAP-CSQWCYNTYGTFLCRCEQGYELGPDG 235
Cdd:cd01475 181 GKICVVPDLCATLSHvCQQVCISTPGSYLCACTEGYALLEDN 222
EGF_CA smart00179
Calcium-binding EGF-like domain;
161-190 2.33e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.84  E-value: 2.33e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 56693245    161 DIDEC-RYRYCQH--RCVNVPGSFSCQCEPGFQ 190
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPPGYT 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
200-234 3.42e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.46  E-value: 3.42e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 56693245    200 DVDECGMGAPCSQ--WCYNTYGTFLCRCEQGYELGPD 234
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
159-197 3.67e-03

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  Cd Length: 224  Bit Score: 38.52  E-value: 3.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 56693245 159 CIDIDECRY--RYCQHRCVNVPGSFSCQCEPGFQLAGNNRS 197
Cdd:cd01475 184 CVVPDLCATlsHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
 
Name Accession Description Interval E-value
EGF_CA pfam07645
Calcium-binding EGF domain;
120-159 5.05e-06

Calcium-binding EGF domain;


Pssm-ID: 311536  Cd Length: 42  Bit Score: 44.65  E-value: 5.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 56693245   120 DVDECERDSHDCQPSQQCFNTEGSFSCQCPDGYR--KVGTEC 159
Cdd:pfam07645   1 DVDECADGTHNCPANTVCVNTIGSFECVCPDGYEnnEDGTNC 42
EGF_CA smart00179
Calcium-binding EGF-like domain;
120-160 8.34e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 44.16  E-value: 8.34e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 56693245    120 DVDECERDsHDCQPSQQCFNTEGSFSCQCPDGYRKvGTECI 160
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGYTD-GRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
120-160 1.69e-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: 43.01  E-value: 1.69e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 56693245 120 DVDECErDSHDCQPSQQCFNTEGSFSCQCPDGYRkvGTECI 160
Cdd:cd00054   1 DIDECA-SGNPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA pfam07645
Calcium-binding EGF domain;
200-238 4.11e-05

Calcium-binding EGF domain;


Pssm-ID: 311536  Cd Length: 42  Bit Score: 41.95  E-value: 4.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 56693245   200 DVDECGMGA---PCSQWCYNTYGTFLCRCEQGYELGPDGFAC 238
Cdd:pfam07645   1 DVDECADGThncPANTVCVNTIGSFECVCPDGYENNEDGTNC 42
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
180-203 1.22e-04

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: 315355  Cd Length: 24  Bit Score: 40.50  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|....
gi 56693245   180 SFSCQCEPGFQLAGNNRSCIDVDE 203
Cdd:pfam12662   1 SYTCSCPPGYTLAGDGRTCVDIDE 24
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
124-159 2.36e-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: 315598  Cd Length: 36  Bit Score: 39.81  E-value: 2.36e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 56693245   124 CERDSHDCQPSQQCFNTEGSFSCQCPDGYRKVGTEC 159
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTDGSFTCTCNDGYTGDGVTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
195-235 2.87e-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  Cd Length: 224  Bit Score: 41.99  E-value: 2.87e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 56693245 195 NRSCIDVDECGMGAP-CSQWCYNTYGTFLCRCEQGYELGPDG 235
Cdd:cd01475 181 GKICVVPDLCATLSHvCQQVCISTPGSYLCACTEGYALLEDN 222
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
170-198 6.93e-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: 317114  Cd Length: 36  Bit Score: 38.37  E-value: 6.93e-04
                          10        20
                  ....*....|....*....|....*....
gi 56693245   170 CQHRCVNVPGSFSCQCEPGFQLAGNNRSC 198
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYKLAEDGKTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
114-152 8.52e-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  Cd Length: 224  Bit Score: 40.45  E-value: 8.52e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 56693245 114 QQDSCVDVDECERDSHDCQpsQQCFNTEGSFSCQCPDGY 152
Cdd:cd01475 180 QGKICVVPDLCATLSHVCQ--QVCISTPGSYLCACTEGY 216
EGF_CA smart00179
Calcium-binding EGF-like domain;
161-190 2.33e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.84  E-value: 2.33e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 56693245    161 DIDEC-RYRYCQH--RCVNVPGSFSCQCEPGFQ 190
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPPGYT 33
EGF_CA smart00179
Calcium-binding EGF-like domain;
200-234 3.42e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.46  E-value: 3.42e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 56693245    200 DVDECGMGAPCSQ--WCYNTYGTFLCRCEQGYELGPD 234
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
159-197 3.67e-03

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  Cd Length: 224  Bit Score: 38.52  E-value: 3.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 56693245 159 CIDIDECRY--RYCQHRCVNVPGSFSCQCEPGFQLAGNNRS 197
Cdd:cd01475 184 CVVPDLCATlsHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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