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Conserved domains on  [gi|755509576|ref|XP_011248542|]
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multiple epidermal growth factor-like domains protein 6 isoform X2 [Mus musculus]

Protein Classification

EMI and FXa_inhibition domain-containing protein( domain architecture ID 10540644)

protein containing domains EMI, vWFA, and FXa_inhibition

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 ...
41-112 1.26e-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: 1.26e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509576    41 PHVCA--EQKLTLVGHRQPCVQAFSRVVPVWrsgCGQQAWCvgQERRTVYYMSYRQVYATEARTVFRCCPGWSQ 112
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 ...
153-201 1.42e-07

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: 53.93  E-value: 1.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755509576  153 QLQGdgKTCQDVDECRSHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRT 201
Cdd:cd01475   178 KFQG--KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
283-324 5.74e-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: 5.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755509576  283 KACEDVDECALGLAQCAHGCLNTQGSFKCVCHAGYELGADGR 324
Cdd:cd01475   182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
412-451 6.86e-05

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: 45.84  E-value: 6.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 755509576  412 CEDVDECASGHSGCEHHCSNLAGSFQCFCEAGYRLDEDRR 451
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
337-372 8.33e-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: 8.33e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   337 CEAGNGGCSHGCSHTSTGPLCTCPRGYELDEDQKTC 372
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
126-161 8.93e-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: 8.93e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   126 CANANGGCEGPCCNTVGGFYCRCPPGYQLQGDGKTC 161
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
250-285 3.05e-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: 36.84  E-value: 3.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   250 CADGNGGCMHTCQELRGLAHCGCHPGYQLAADRKAC 285
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
370-409 4.26e-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: 40.45  E-value: 4.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755509576  370 KTCIDIDDCANSP-CCQQVCANTPGGYECSCFAGYRLNTDG 409
Cdd:cd01475   182 KICVVPDLCATLShVCQQVCISTPGSYLCACTEGYALLEDN 222
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
208-244 6.19e-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: 6.19e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 755509576   208 CTLGNGGCQHQCVqLTVTQHRCQCRPQYQLQEDGRRC 244
Cdd:pfam14670    1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
 
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 ...
41-112 1.26e-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: 1.26e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509576    41 PHVCA--EQKLTLVGHRQPCVQAFSRVVPVWrsgCGQQAWCvgQERRTVYYMSYRQVYATEARTVFRCCPGWSQ 112
Cdd:pfam07546    1 RNVCAykVVSCVVVTGTESYVQPVYKPYLTW---CAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
153-201 1.42e-07

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: 53.93  E-value: 1.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755509576  153 QLQGdgKTCQDVDECRSHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRT 201
Cdd:cd01475   178 KFQG--KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
283-324 5.74e-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: 5.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755509576  283 KACEDVDECALGLAQCAHGCLNTQGSFKCVCHAGYELGADGR 324
Cdd:cd01475   182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
167-202 1.37e-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: 1.37e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   167 CRSHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRTC 202
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
412-451 6.86e-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: 45.84  E-value: 6.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 755509576  412 CEDVDECASGHSGCEHHCSNLAGSFQCFCEAGYRLDEDRR 451
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
337-372 8.33e-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: 8.33e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   337 CEAGNGGCSHGCSHTSTGPLCTCPRGYELDEDQKTC 372
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
126-161 8.93e-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: 8.93e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   126 CANANGGCEGPCCNTVGGFYCRCPPGYQLQGDGKTC 161
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
163-202 7.41e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 7.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 755509576    163 DVDECRSHNG-GCQHRCVNTPGSYLCECKPGFrlhTDGRTC 202
Cdd:smart00179    1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGY---TDGRNC 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
250-285 3.05e-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: 36.84  E-value: 3.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   250 CADGNGGCMHTCQELRGLAHCGCHPGYQLAADRKAC 285
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
236-284 3.58e-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: 40.83  E-value: 3.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755509576  236 QLQedGRRCVRRSPCADGNGGCMHTCQELRGLAHCGCHPGYQLAADRKA 284
Cdd:cd01475   178 KFQ--GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
370-409 4.26e-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: 40.45  E-value: 4.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755509576  370 KTCIDIDDCANSP-CCQQVCANTPGGYECSCFAGYRLNTDG 409
Cdd:cd01475   182 KICVVPDLCATLShVCQQVCISTPGSYLCACTEGYALLEDN 222
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
116-160 5.79e-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: 40.06  E-value: 5.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 755509576  116 QEGCLSDVDECANANGGCEGPCCNTVGGFYCRCPPGYQLQGDGKT 160
Cdd:cd01475   180 QGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
208-244 6.19e-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: 6.19e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 755509576   208 CTLGNGGCQHQCVqLTVTQHRCQCRPQYQLQEDGRRC 244
Cdd:pfam14670    1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
 
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 ...
41-112 1.26e-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: 1.26e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755509576    41 PHVCA--EQKLTLVGHRQPCVQAFSRVVPVWrsgCGQQAWCvgQERRTVYYMSYRQVYATEARTVFRCCPGWSQ 112
Cdd:pfam07546    1 RNVCAykVVSCVVVTGTESYVQPVYKPYLTW---CAGHRRC--STYRTTYRPAYRQVYKTVTRLEWRCCPGWGG 69
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
153-201 1.42e-07

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: 53.93  E-value: 1.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755509576  153 QLQGdgKTCQDVDECRSHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRT 201
Cdd:cd01475   178 KFQG--KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
283-324 5.74e-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: 5.74e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 755509576  283 KACEDVDECALGLAQCAHGCLNTQGSFKCVCHAGYELGADGR 324
Cdd:cd01475   182 KICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
167-202 1.37e-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: 1.37e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   167 CRSHNGGCQHRCVNTPGSYLCECKPGFRLHTDGRTC 202
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
412-451 6.86e-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: 45.84  E-value: 6.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 755509576  412 CEDVDECASGHSGCEHHCSNLAGSFQCFCEAGYRLDEDRR 451
Cdd:cd01475   184 CVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNK 223
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
337-372 8.33e-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: 8.33e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   337 CEAGNGGCSHGCSHTSTGPLCTCPRGYELDEDQKTC 372
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
126-161 8.93e-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: 8.93e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   126 CANANGGCEGPCCNTVGGFYCRCPPGYQLQGDGKTC 161
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
163-202 7.41e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 7.41e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|.
gi 755509576    163 DVDECRSHNG-GCQHRCVNTPGSYLCECKPGFrlhTDGRTC 202
Cdd:smart00179    1 DIDECASGNPcQNGGTCVNTVGSYRCECPPGY---TDGRNC 38
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
145-166 1.08e-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: 37.77  E-value: 1.08e-03
                           10        20
                   ....*....|....*....|..
gi 755509576   145 YCRCPPGYQLQGDGKTCQDVDE 166
Cdd:pfam12662    1 TCSCPPGYQLDPDGRTCVDIDE 22
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
250-285 3.05e-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: 36.84  E-value: 3.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 755509576   250 CADGNGGCMHTCQELRGLAHCGCHPGYQLAADRKAC 285
Cdd:pfam14670    1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
236-284 3.58e-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: 40.83  E-value: 3.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755509576  236 QLQedGRRCVRRSPCADGNGGCMHTCQELRGLAHCGCHPGYQLAADRKA 284
Cdd:cd01475   178 KFQ--GKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
163-197 4.13e-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: 36.46  E-value: 4.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 755509576  163 DVDECRSHNG-GCQHRCVNTPGSYLCECKPGFRLHT 197
Cdd:cd00054     1 DIDECASGNPcQNGGTCVNTVGSYRCSCPPGYTGRN 36
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
370-409 4.26e-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: 40.45  E-value: 4.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755509576  370 KTCIDIDDCANSP-CCQQVCANTPGGYECSCFAGYRLNTDG 409
Cdd:cd01475   182 KICVVPDLCATLShVCQQVCISTPGSYLCACTEGYALLEDN 222
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
116-160 5.79e-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: 40.06  E-value: 5.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 755509576  116 QEGCLSDVDECANANGGCEGPCCNTVGGFYCRCPPGYQLQGDGKT 160
Cdd:cd01475   180 QGKICVVPDLCATLSHVCQQVCISTPGSYLCACTEGYALLEDNKT 224
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
208-244 6.19e-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: 6.19e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 755509576   208 CTLGNGGCQHQCVqLTVTQHRCQCRPQYQLQEDGRRC 244
Cdd:pfam14670    1 CSVNNGGCSHLCL-NTPGGYTCSCPEGYELQDDGRTC 36
 
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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