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Conserved domains on  [gi|1958778394|ref|XP_038966656|]
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multiple epidermal growth factor-like domains protein 6 isoform X1 [Rattus norvegicus]

Protein Classification

matrilin; VIT and vWA domain-containing protein( domain architecture ID 10540644)

matrilin acts as the component of the extracellular matrix of cartilage| VIT (vault protein inter-alpha-trypsin) and vWA (von Willebrand factor type A) domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
41-113 1.15e-07

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


:

Pssm-ID: 462204  Cd Length: 69  Bit Score: 50.11  E-value: 1.15e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778394   41 PHVCA--EQKLTLVGHRQPCVQAFSRIVPVWrrtgCAQQAWCigQERRTVYYMSYRQVYATEARTVFRCCPGWSQ 113
Cdd:pfam07546    1 RNVCAykVVSCVVVTGTESYVQPVYKPYLTW----CAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
243-284 5.15e-06

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: 49.31  E-value: 5.15e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958778394  243 KTCEDVDECALGLAQCAHGCLNTQGSFKCVCHAGYELGADGR 284
Cdd:cd01475    182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
127-162 1.28e-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: 43.39  E-value: 1.28e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  127 CRAHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRTC 162
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
297-332 8.27e-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: 41.07  E-value: 8.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  297 CEAGNGGCSHGCSHTSTGPLCTCPRGYELDEDQKTC 332
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
372-411 1.02e-04

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: 45.45  E-value: 1.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958778394  372 CEDVDECASGHGGCEHHCSNLAGSFQCFCEAGYRLDEDRR 411
Cdd:cd01475    184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
196-244 1.39e-04

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: 45.07  E-value: 1.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958778394  196 QLQedGRRCVRRSPCAEGNGGCMHICQELRGLAHCGCHPGYQLAADRKT 244
Cdd:cd01475    178 KFQ--GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
168-204 6.21e-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: 35.68  E-value: 6.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958778394  168 CTLGNGGCQHQCVqLTVTQHRCQCRPQYQLQEDGRRC 204
Cdd:pfam14670    1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
330-369 7.42e-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: 39.68  E-value: 7.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958778394  330 KTCIDIDDCANSP-CCQQACANTPGGYECSCFAGYRLNTDG 369
Cdd:cd01475    182 KICVVPDLCATLShVCQQVCISTPGSYLCACTEGYALLEDN 222
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
41-113 1.15e-07

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 50.11  E-value: 1.15e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778394   41 PHVCA--EQKLTLVGHRQPCVQAFSRIVPVWrrtgCAQQAWCigQERRTVYYMSYRQVYATEARTVFRCCPGWSQ 113
Cdd:pfam07546    1 RNVCAykVVSCVVVTGTESYVQPVYKPYLTW----CAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
243-284 5.15e-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: 49.31  E-value: 5.15e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958778394  243 KTCEDVDECALGLAQCAHGCLNTQGSFKCVCHAGYELGADGR 284
Cdd:cd01475    182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
127-162 1.28e-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: 43.39  E-value: 1.28e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  127 CRAHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRTC 162
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
117-161 1.41e-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: 48.15  E-value: 1.41e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958778394  117 QEGCLSDVDECRAHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRT 161
Cdd:cd01475    180 QGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
297-332 8.27e-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: 41.07  E-value: 8.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  297 CEAGNGGCSHGCSHTSTGPLCTCPRGYELDEDQKTC 332
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
372-411 1.02e-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: 45.45  E-value: 1.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958778394  372 CEDVDECASGHGGCEHHCSNLAGSFQCFCEAGYRLDEDRR 411
Cdd:cd01475    184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
196-244 1.39e-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: 45.07  E-value: 1.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958778394  196 QLQedGRRCVRRSPCAEGNGGCMHICQELRGLAHCGCHPGYQLAADRKT 244
Cdd:cd01475    178 KFQ--GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
210-245 4.10e-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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 39.15  E-value: 4.10e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  210 CAEGNGGCMHICQELRGLAHCGCHPGYQLAADRKTC 245
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
378-413 1.45e-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: 37.61  E-value: 1.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  378 CASGHGGCEHHCSNLAGSFQCFCEAGYRLDEDRRGC 413
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
123-162 1.47e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.61  E-value: 1.47e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1958778394   123 DVDECrAHNGGCQH--RCVNTPGSYLCECKPGFrlhTDGRTC 162
Cdd:smart00179    1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGY---TDGRNC 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
168-204 6.21e-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: 35.68  E-value: 6.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958778394  168 CTLGNGGCQHQCVqLTVTQHRCQCRPQYQLQEDGRRC 204
Cdd:pfam14670    1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
330-369 7.42e-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: 39.68  E-value: 7.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958778394  330 KTCIDIDDCANSP-CCQQACANTPGGYECSCFAGYRLNTDG 369
Cdd:cd01475    182 KICVVPDLCATLShVCQQVCISTPGSYLCACTEGYALLEDN 222
 
Name Accession Description Interval E-value
EMI pfam07546
EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final ...
41-113 1.15e-07

EMI domain; The Pfam alignment is truncated at the C-terminus and does not include the final cysteine defined in Callebaut et al. This is to stop the family overlapping with other domains.


Pssm-ID: 462204  Cd Length: 69  Bit Score: 50.11  E-value: 1.15e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958778394   41 PHVCA--EQKLTLVGHRQPCVQAFSRIVPVWrrtgCAQQAWCigQERRTVYYMSYRQVYATEARTVFRCCPGWSQ 113
Cdd:pfam07546    1 RNVCAykVVSCVVVTGTESYVQPVYKPYLTW----CAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
243-284 5.15e-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: 49.31  E-value: 5.15e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1958778394  243 KTCEDVDECALGLAQCAHGCLNTQGSFKCVCHAGYELGADGR 284
Cdd:cd01475    182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
127-162 1.28e-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: 43.39  E-value: 1.28e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  127 CRAHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRTC 162
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
117-161 1.41e-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: 48.15  E-value: 1.41e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1958778394  117 QEGCLSDVDECRAHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRT 161
Cdd:cd01475    180 QGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
297-332 8.27e-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: 41.07  E-value: 8.27e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  297 CEAGNGGCSHGCSHTSTGPLCTCPRGYELDEDQKTC 332
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
372-411 1.02e-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: 45.45  E-value: 1.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1958778394  372 CEDVDECASGHGGCEHHCSNLAGSFQCFCEAGYRLDEDRR 411
Cdd:cd01475    184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
196-244 1.39e-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: 45.07  E-value: 1.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958778394  196 QLQedGRRCVRRSPCAEGNGGCMHICQELRGLAHCGCHPGYQLAADRKT 244
Cdd:cd01475    178 KFQ--GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
210-245 4.10e-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: 464251 [Multi-domain]  Cd Length: 36  Bit Score: 39.15  E-value: 4.10e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  210 CAEGNGGCMHICQELRGLAHCGCHPGYQLAADRKTC 245
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
378-413 1.45e-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: 37.61  E-value: 1.45e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1958778394  378 CASGHGGCEHHCSNLAGSFQCFCEAGYRLDEDRRGC 413
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
123-162 1.47e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 37.61  E-value: 1.47e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1958778394   123 DVDECrAHNGGCQH--RCVNTPGSYLCECKPGFrlhTDGRTC 162
Cdd:smart00179    1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGY---TDGRNC 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
168-204 6.21e-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: 35.68  E-value: 6.21e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958778394  168 CTLGNGGCQHQCVqLTVTQHRCQCRPQYQLQEDGRRC 204
Cdd:pfam14670    1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
330-369 7.42e-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: 39.68  E-value: 7.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1958778394  330 KTCIDIDDCANSP-CCQQACANTPGGYECSCFAGYRLNTDG 369
Cdd:cd01475    182 KICVVPDLCATLShVCQQVCISTPGSYLCACTEGYALLEDN 222
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
229-250 8.85e-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: 8.85e-03
                           10        20
                   ....*....|....*....|..
gi 1958778394  229 HCGCHPGYQLAADRKTCEDVDE 250
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22
 
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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