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Conserved domains on  [gi|569005916|ref|XP_006531873|]
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EGF-containing fibulin-like extracellular matrix protein 2 isoform X4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EGF_CA smart00179
Calcium-binding EGF-like domain;
55-95 3.10e-06

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 3.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 569005916    55 DVDECTQaLHDCRPSQDCHNLPGSYQCTCPDGYRkIGPECV 95
Cdd:smart00179   1 DIDECAS-GNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA smart00179
Calcium-binding EGF-like domain;
96-129 1.09e-05

Calcium-binding EGF-like domain;


:

Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 1.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 569005916    96 DIDEC-RYRYCQH--RCVNLPGSFRCQCEPGFQLGPN 129
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
EGF_CA pfam07645
Calcium-binding EGF domain;
215-242 2.37e-05

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 40.68  E-value: 2.37e-05
                          10        20
                  ....*....|....*....|....*...
gi 569005916  215 DIDECETGAHQCSEAQTCVNFHGGYRCV 242
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 135-168 1.26e-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: 36.08  E-value: 1.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 569005916 135 DVNECDMGAPCE--QRCFNSYGTFLCRCNQGYELHR 168
Cdd:cd00054    1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTGRN 36
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 173-208 1.75e-03

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


The actual alignment was detected with superfamily member cd01475:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 224  Bit Score: 39.29  E-value: 1.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 569005916 173 CSDIDECGYSSYLCQYRCVNEPGRFSCHCPQGYQLL 208
Cdd:cd01475  184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALL 219
 
Name Accession Description Interval E-value
EGF_CA smart00179
Calcium-binding EGF-like domain;
55-95 3.10e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 3.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 569005916    55 DVDECTQaLHDCRPSQDCHNLPGSYQCTCPDGYRkIGPECV 95
Cdd:smart00179   1 DIDECAS-GNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
55-86 3.23e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 43.38  E-value: 3.23e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569005916   55 DVDECTQALHDCRPSQDCHNLPGSYQCTCPDG 86
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 55-95 4.99e-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: 43.01  E-value: 4.99e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569005916  55 DVDECTQAlHDCRPSQDCHNLPGSYQCTCPDGYRkiGPECV 95
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
96-129 1.09e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 1.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 569005916    96 DIDEC-RYRYCQH--RCVNLPGSFRCQCEPGFQLGPN 129
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
EGF_CA pfam07645
Calcium-binding EGF domain;
215-242 2.37e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 40.68  E-value: 2.37e-05
                          10        20
                  ....*....|....*....|....*...
gi 569005916  215 DIDECETGAHQCSEAQTCVNFHGGYRCV 242
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 105-133 4.62e-05

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: 40.30  E-value: 4.62e-05
                          10        20
                  ....*....|....*....|....*....
gi 569005916  105 CQHRCVNLPGSFRCQCEPGFQLGPNNRSC 133
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 94-132 2.66e-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: 41.99  E-value: 2.66e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569005916  94 CVDIDECRY--RYCQHRCVNLPGSFRCQCEPGFQLGPNNRS 132
Cdd:cd01475  184 CVVPDLCATlsHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 135-168 1.26e-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: 36.08  E-value: 1.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 569005916 135 DVNECDMGAPCE--QRCFNSYGTFLCRCNQGYELHR 168
Cdd:cd00054    1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTGRN 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
135-169 1.67e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.69  E-value: 1.67e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 569005916   135 DVNECDMGAPCEQ--RCFNSYGTFLCRCNQGYELHRD 169
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 173-208 1.75e-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 [Multi-domain]  Cd Length: 224  Bit Score: 39.29  E-value: 1.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 569005916 173 CSDIDECGYSSYLCQYRCVNEPGRFSCHCPQGYQLL 208
Cdd:cd01475  184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALL 219
EGF_CA smart00179
Calcium-binding EGF-like domain;
175-206 2.43e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 2.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 569005916   175 DIDECgYSSYLCQY--RCVNEPGRFSCHCPQGYQ 206
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT 33
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 158-178 2.46e-03

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: 35.08  E-value: 2.46e-03
                          10        20
                  ....*....|....*....|.
gi 569005916  158 CRCNQGYELHRDGFSCSDIDE 178
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22
EGF_CA smart00179
Calcium-binding EGF-like domain;
215-242 6.19e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.14  E-value: 6.19e-03
                           10        20
                   ....*....|....*....|....*...
gi 569005916   215 DIDECETGaHQCSEAQTCVNFHGGYRCV 242
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCE 27
 
Name Accession Description Interval E-value
EGF_CA smart00179
Calcium-binding EGF-like domain;
55-95 3.10e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 3.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 569005916    55 DVDECTQaLHDCRPSQDCHNLPGSYQCTCPDGYRkIGPECV 95
Cdd:smart00179   1 DIDECAS-GNPCQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
55-86 3.23e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 43.38  E-value: 3.23e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569005916   55 DVDECTQALHDCRPSQDCHNLPGSYQCTCPDG 86
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 55-95 4.99e-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: 43.01  E-value: 4.99e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569005916  55 DVDECTQAlHDCRPSQDCHNLPGSYQCTCPDGYRkiGPECV 95
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGYT--GRNCE 38
EGF_CA smart00179
Calcium-binding EGF-like domain;
96-129 1.09e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.85  E-value: 1.09e-05
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 569005916    96 DIDEC-RYRYCQH--RCVNLPGSFRCQCEPGFQLGPN 129
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
EGF_CA pfam07645
Calcium-binding EGF domain;
215-242 2.37e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 40.68  E-value: 2.37e-05
                          10        20
                  ....*....|....*....|....*...
gi 569005916  215 DIDECETGAHQCSEAQTCVNFHGGYRCV 242
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECR 28
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 105-133 4.62e-05

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: 40.30  E-value: 4.62e-05
                          10        20
                  ....*....|....*....|....*....
gi 569005916  105 CQHRCVNLPGSFRCQCEPGFQLGPNNRSC 133
Cdd:pfam14670   8 CSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 94-132 2.66e-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: 41.99  E-value: 2.66e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 569005916  94 CVDIDECRY--RYCQHRCVNLPGSFRCQCEPGFQLGPNNRS 132
Cdd:cd01475  184 CVVPDLCATlsHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 96-126 6.46e-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: 36.85  E-value: 6.46e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 569005916  96 DIDECR-YRYCQH--RCVNLPGSFRCQCEPGFQL 126
Cdd:cd00054    1 DIDECAsGNPCQNggTCVNTVGSYRCSCPPGYTG 34
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 117-138 6.61e-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: 36.62  E-value: 6.61e-04
                          10        20
                  ....*....|....*....|..
gi 569005916  117 RCQCEPGFQLGPNNRSCVDVNE 138
Cdd:pfam12662   1 TCSCPPGYQLDPDGRTCVDIDE 22
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 135-168 1.26e-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: 36.08  E-value: 1.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 569005916 135 DVNECDMGAPCE--QRCFNSYGTFLCRCNQGYELHR 168
Cdd:cd00054    1 DIDECASGNPCQngGTCVNTVGSYRCSCPPGYTGRN 36
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 59-94 1.48e-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: 36.04  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 569005916   59 CTQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPEC 94
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
135-169 1.67e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.69  E-value: 1.67e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 569005916   135 DVNECDMGAPCEQ--RCFNSYGTFLCRCNQGYELHRD 169
Cdd:smart00179   1 DIDECASGNPCQNggTCVNTVGSYRCECPPGYTDGRN 37
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 130-170 1.67e-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 [Multi-domain]  Cd Length: 224  Bit Score: 39.29  E-value: 1.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 569005916 130 NRSCVDVNECDMGAP-CEQRCFNSYGTFLCRCNQGYELHRDG 170
Cdd:cd01475  181 GKICVVPDLCATLSHvCQQVCISTPGSYLCACTEGYALLEDN 222
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 173-208 1.75e-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 [Multi-domain]  Cd Length: 224  Bit Score: 39.29  E-value: 1.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 569005916 173 CSDIDECGYSSYLCQYRCVNEPGRFSCHCPQGYQLL 208
Cdd:cd01475  184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALL 219
EGF_CA smart00179
Calcium-binding EGF-like domain;
175-206 2.43e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 35.30  E-value: 2.43e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 569005916   175 DIDECgYSSYLCQY--RCVNEPGRFSCHCPQGYQ 206
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT 33
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 158-178 2.46e-03

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: 35.08  E-value: 2.46e-03
                          10        20
                  ....*....|....*....|.
gi 569005916  158 CRCNQGYELHRDGFSCSDIDE 178
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22
EGF_CA smart00179
Calcium-binding EGF-like domain;
215-242 6.19e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.14  E-value: 6.19e-03
                           10        20
                   ....*....|....*....|....*...
gi 569005916   215 DIDECETGaHQCSEAQTCVNFHGGYRCV 242
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCE 27
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 53-87 6.33e-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 [Multi-domain]  Cd Length: 224  Bit Score: 37.75  E-value: 6.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 569005916  53 CVDVDECTQALHDCRpsQDCHNLPGSYQCTCPDGY 87
Cdd:cd01475  184 CVVPDLCATLSHVCQ--QVCISTPGSYLCACTEGY 216
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 175-207 7.14e-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: 7.14e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 569005916 175 DIDECgYSSYLCQY--RCVNEPGRFSCHCPQGYQL 207
Cdd:cd00054    1 DIDEC-ASGNPCQNggTCVNTVGSYRCSCPPGYTG 34
 
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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