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Conserved domains on  [gi|253722323|pdb|1PFX|L]
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Chain L, FACTOR IXA

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain. This domain is ...
9-46 1.50e-09

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain. This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


:

Pssm-ID: 366184  Cd Length: 41  Bit Score: 50.28  E-value: 1.50e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
1PFX_L          9 FVRGNL*R*CI**KCSF**AR*VF*NT*KTN*FWKQYV 46
Cdd:pfam00594   4 LKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
47-83 4.67e-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: 41.08  E-value: 4.67e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
1PFX_L       47 DGDQCE-PNPCLNGGLCK*DINSYECWCQVGFEGKNCE 83
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site. This short domain on coagulation enzyme factor Xa is ...
88-124 1.06e-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: 373209  Cd Length: 36  Bit Score: 37.20  E-value: 1.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
1PFX_L         88 CNIKNGRCKQFCKTGADSKVlCSCTTGYRLAPDQKSC 124
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYKLAEDGKTC 36
 
Name Accession Description Interval E-value
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain. This domain is ...
9-46 1.50e-09

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain. This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 366184  Cd Length: 41  Bit Score: 50.28  E-value: 1.50e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
1PFX_L          9 FVRGNL*R*CI**KCSF**AR*VF*NT*KTN*FWKQYV 46
Cdd:pfam00594   4 LKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
1-46 3.23e-08

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 47.30  E-value: 3.23e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
1PFX_L           1 YNSGKL**FVRGNL*R*CI**KCSF**AR*VF*NT*KTN*FWKQYV 46
Cdd:smart00069  20 ANAFLLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
47-83 4.67e-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: 41.08  E-value: 4.67e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
1PFX_L       47 DGDQCE-PNPCLNGGLCK*DINSYECWCQVGFEGKNCE 83
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site. This short domain on coagulation enzyme factor Xa is ...
88-124 1.06e-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: 373209  Cd Length: 36  Bit Score: 37.20  E-value: 1.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
1PFX_L         88 CNIKNGRCKQFCKTGADSKVlCSCTTGYRLAPDQKSC 124
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYKLAEDGKTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
47-83 3.21e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.07  E-value: 3.21e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
1PFX_L          47 DGDQCE-PNPCLNGGLCK*DINSYECWCQVGFE-GKNCE 83
Cdd:smart00179   1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
77-123 3.57e-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: 38.91  E-value: 3.57e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
1PFX_L       77 FEGKNCELDATCNIKNGRCKQFCKTGADSkVLCSCTTGYRLAPDQKS 123
Cdd:cd01475 179 FQGKICVVPDLCATLSHVCQQVCISTPGS-YLCACTEGYALLEDNKT 224
EGF pfam00008
EGF-like domain. There is no clear separation between noise and signal. pfam00053 is very ...
51-81 7.45e-04

EGF-like domain. There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 333761  Cd Length: 31  Bit Score: 35.06  E-value: 7.45e-04
                          10        20        30
                  ....*....|....*....|....*....|.
1PFX_L         51 CEPNPCLNGGLCK*DINSYECWCQVGFEGKN 81
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
 
Name Accession Description Interval E-value
Gla pfam00594
Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain. This domain is ...
9-46 1.50e-09

Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain. This domain is responsible for the high-affinity binding of calcium ions. This domain contains post-translational modifications of many glutamate residues by Vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla).


Pssm-ID: 366184  Cd Length: 41  Bit Score: 50.28  E-value: 1.50e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
1PFX_L          9 FVRGNL*R*CI**KCSF**AR*VF*NT*KTN*FWKQYV 46
Cdd:pfam00594   4 LKPGNLERECYEEICSYEEAREIFEDDEKTMEFWKKYT 41
GLA smart00069
Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in ...
1-46 3.23e-08

Domain containing Gla (gamma-carboxyglutamate) residues; A hyaluronan-binding domain found in proteins associated with the extracellular matrix, cell adhesion and cell migration.


Pssm-ID: 214503  Cd Length: 65  Bit Score: 47.30  E-value: 3.23e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
1PFX_L           1 YNSGKL**FVRGNL*R*CI**KCSF**AR*VF*NT*KTN*FWKQYV 46
Cdd:smart00069  20 ANAFLLEELRPGNLERECQEEICSLEEAREVFEDNEGTDEFYRRYY 65
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
47-83 4.67e-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: 41.08  E-value: 4.67e-06
                        10        20        30
                ....*....|....*....|....*....|....*...
1PFX_L       47 DGDQCE-PNPCLNGGLCK*DINSYECWCQVGFEGKNCE 83
Cdd:cd00054   1 DIDECAsGNPCQNGGTCVNTVGSYRCSCPPGYTGRNCE 38
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site. This short domain on coagulation enzyme factor Xa is ...
88-124 1.06e-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: 373209  Cd Length: 36  Bit Score: 37.20  E-value: 1.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
1PFX_L         88 CNIKNGRCKQFCKTGADSKVlCSCTTGYRLAPDQKSC 124
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYT-CSCPEGYKLAEDGKTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
47-83 3.21e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542  Cd Length: 39  Bit Score: 36.07  E-value: 3.21e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
1PFX_L          47 DGDQCE-PNPCLNGGLCK*DINSYECWCQVGFE-GKNCE 83
Cdd:smart00179   1 DIDECAsGNPCQNGGTCVNTVGSYRCECPPGYTdGRNCE 39
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
77-123 3.57e-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: 38.91  E-value: 3.57e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
1PFX_L       77 FEGKNCELDATCNIKNGRCKQFCKTGADSkVLCSCTTGYRLAPDQKS 123
Cdd:cd01475 179 FQGKICVVPDLCATLSHVCQQVCISTPGS-YLCACTEGYALLEDNKT 224
EGF pfam00008
EGF-like domain. There is no clear separation between noise and signal. pfam00053 is very ...
51-81 7.45e-04

EGF-like domain. There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.


Pssm-ID: 333761  Cd Length: 31  Bit Score: 35.06  E-value: 7.45e-04
                          10        20        30
                  ....*....|....*....|....*....|.
1PFX_L         51 CEPNPCLNGGLCK*DINSYECWCQVGFEGKN 81
Cdd:pfam00008   1 CAPNPCSNGGTCVDTPGGYTCICPEGYTGKR 31
EGF cd00053
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ...
52-83 7.85e-03

Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.


Pssm-ID: 238010  Cd Length: 36  Bit Score: 32.45  E-value: 7.85e-03
                        10        20        30
                ....*....|....*....|....*....|...
1PFX_L       52 EPNPCLNGGLCK*DINSYECWCQVGFEG-KNCE 83
Cdd:cd00053   4 ASNPCSNGGTCVNTPGSYRCVCPPGYTGdRSCE 36
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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