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Conserved domains on  [gi|755553259|ref|XP_011244145|]
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vitamin K-dependent protein S isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
249-379 3.27e-31

Laminin G domain;


:

Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 117.80  E-value: 3.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259  249 FRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNIN 328
Cdd:pfam00054   1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755553259  329 KLGSlfkpTDGFLD--TKIYFAGLPRKVESALIKPINPRLDGCIRG--WNLMKQG 379
Cdd:pfam00054  81 SPLG----ATTDLDvdGPLYVGGLPSLGVKKRRLAISPSFDGCIRDviVNGKPLD 131
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 85-119 1.42e-07

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: 47.62  E-value: 1.42e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 755553259   85 SNVNGGCSQICDNTPGSYHCSCKRGFAMLPNKKDC 119
Cdd:pfam14670   2 SVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 167-202 3.23e-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: 3.23e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 755553259  167 CSEN--MCAQLCVNFPGGYSCYCDgkKGFKLAQDQKSC 202
Cdd:pfam14670   1 CSVNngGCSHLCLNTPGGYTCSCP--EGYELQDDGRTC 36
EGF_CA pfam07645
Calcium-binding EGF domain;
121-151 7.56e-05

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.91  E-value: 7.56e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 755553259  121 DLDECALKPSVC-GTAVCKNIPGDFECECPDG 151
Cdd:pfam07645   1 DVDECATGTHNCpANTVCVNTIGSFECRCPDG 32
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 146-166 4.72e-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: 37.39  E-value: 4.72e-04
                          10        20
                  ....*....|....*....|.
gi 755553259  146 CECPDGYRYDPSSKSCKDVDE 166
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22
LamG super family cl22861
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 429-566 6.97e-04

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


The actual alignment was detected with superfamily member smart00282:

Pssm-ID: 473984 [Multi-domain]  Cd Length: 132  Bit Score: 40.02  E-value: 6.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259   429 NVTLNIRPSTGTGVMLALVSGGTVPF-ALSLVDSRsgtsqdIVVFVENS---VVARLEAVSLCSDQQSQLKCNVNRNGLE 504
Cdd:smart00282   1 SISFSFRTTSPNGLLLYAGSKGGGDYlALELRDGR------LVLRYDLGsgpARLTSDPTPLNDGQWHRVAVERNGRSVT 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755553259   505 LWTPLRKDVIYSKDLQRQLAVLDKAMkrtvatYLGGIP-DISFSATPVNAFYSGCME-VNINGV 566
Cdd:smart00282  75 LSVDGGNRVSGESPGGLTILNLDGPL------YLGGLPeDLKLPPLPVTPGFRGCIRnLKVNGK 132
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
249-379 3.27e-31

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 117.80  E-value: 3.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259  249 FRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNIN 328
Cdd:pfam00054   1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755553259  329 KLGSlfkpTDGFLD--TKIYFAGLPRKVESALIKPINPRLDGCIRG--WNLMKQG 379
Cdd:pfam00054  81 SPLG----ATTDLDvdGPLYVGGLPSLGVKKRRLAISPSFDGCIRDviVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 232-375 3.41e-25

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 101.73  E-value: 3.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259 232 YLKFRLPDI--TRFSAEFDFRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVE 309
Cdd:cd00110    9 YVRLPTLPAprTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVE 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755553259 310 ELDDSVSIKIAKEAVMNINKLGSLFkptDGFLDTKIYFAGLPRKVESALIkPINPRLDGCIRGWNL 375
Cdd:cd00110   89 RNGRSVTLSVDGERVVESGSPGGSA---LLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
244-375 2.38e-22

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 92.79  E-value: 2.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259   244 SAEFDFRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFS-TQITTGGNVINNGIWNMVSVEELDDSVSIKIAKE 322
Cdd:smart00282   1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755553259   323 AVMNINKLGSlfkPTDGFLDTKIYFAGLPRkVESALIKPINPRLDGCIRGWNL 375
Cdd:smart00282  81 NRVSGESPGG---LTILNLDGPLYLGGLPE-DLKLPPLPVTPGFRGCIRNLKV 129
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 85-119 1.42e-07

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: 47.62  E-value: 1.42e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 755553259   85 SNVNGGCSQICDNTPGSYHCSCKRGFAMLPNKKDC 119
Cdd:pfam14670   2 SVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 167-202 3.23e-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: 3.23e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 755553259  167 CSEN--MCAQLCVNFPGGYSCYCDgkKGFKLAQDQKSC 202
Cdd:pfam14670   1 CSVNngGCSHLCLNTPGGYTCSCP--EGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
77-110 4.05e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.08  E-value: 4.05e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 755553259    77 DVNECKDPSN-VNGGcsqICDNTPGSYHCSCKRGF 110
Cdd:smart00179   1 DIDECASGNPcQNGG---TCVNTVGSYRCECPPGY 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 77-110 6.39e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 40.31  E-value: 6.39e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 755553259  77 DVNECKDPSN-VNGGcsqICDNTPGSYHCSCKRGF 110
Cdd:cd00054    1 DIDECASGNPcQNGG---TCVNTVGSYRCSCPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
121-151 7.56e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.91  E-value: 7.56e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 755553259  121 DLDECALKPSVC-GTAVCKNIPGDFECECPDG 151
Cdd:pfam07645   1 DVDECATGTHNCpANTVCVNTIGSFECRCPDG 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
121-153 1.70e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 1.70e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 755553259   121 DLDECALkPSVCGT-AVCKNIPGDFECECPDGYR 153
Cdd:smart00179   1 DIDECAS-GNPCQNgGTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 121-153 2.79e-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: 38.39  E-value: 2.79e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 755553259 121 DLDECALkPSVCG-TAVCKNIPGDFECECPDGYR 153
Cdd:cd00054    1 DIDECAS-GNPCQnGGTCVNTVGSYRCSCPPGYT 33
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 146-166 4.72e-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: 37.39  E-value: 4.72e-04
                          10        20
                  ....*....|....*....|.
gi 755553259  146 CECPDGYRYDPSSKSCKDVDE 166
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22
LamG smart00282
Laminin G domain;
429-566 6.97e-04

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 40.02  E-value: 6.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259   429 NVTLNIRPSTGTGVMLALVSGGTVPF-ALSLVDSRsgtsqdIVVFVENS---VVARLEAVSLCSDQQSQLKCNVNRNGLE 504
Cdd:smart00282   1 SISFSFRTTSPNGLLLYAGSKGGGDYlALELRDGR------LVLRYDLGsgpARLTSDPTPLNDGQWHRVAVERNGRSVT 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755553259   505 LWTPLRKDVIYSKDLQRQLAVLDKAMkrtvatYLGGIP-DISFSATPVNAFYSGCME-VNINGV 566
Cdd:smart00282  75 LSVDGGNRVSGESPGGLTILNLDGPL------YLGGLPeDLKLPPLPVTPGFRGCIRnLKVNGK 132
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 161-201 8.45e-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: 41.22  E-value: 8.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755553259 161 CKDVDECSE--NMCAQLCVNFPGGYSCYCdgKKGFKLAQDQKS 201
Cdd:cd01475  184 CVVPDLCATlsHVCQQVCISTPGSYLCAC--TEGYALLEDNKT 224
EGF_CA smart00179
Calcium-binding EGF-like domain;
163-203 1.42e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 1.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 755553259   163 DVDEC-SENMCAQ--LCVNFPGGYSCYCdgKKGFklaQDQKSCE 203
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCEC--PPGY---TDGRNCE 39
 
Name Accession Description Interval E-value
Laminin_G_1 pfam00054
Laminin G domain;
249-379 3.27e-31

Laminin G domain;


Pssm-ID: 395008 [Multi-domain]  Cd Length: 131  Bit Score: 117.80  E-value: 3.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259  249 FRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNIN 328
Cdd:pfam00054   1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755553259  329 KLGSlfkpTDGFLD--TKIYFAGLPRKVESALIKPINPRLDGCIRG--WNLMKQG 379
Cdd:pfam00054  81 SPLG----ATTDLDvdGPLYVGGLPSLGVKKRRLAISPSFDGCIRDviVNGKPLD 131
LamG cd00110
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ...
 232-375 3.41e-25

Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.


Pssm-ID: 238058 [Multi-domain]  Cd Length: 151  Bit Score: 101.73  E-value: 3.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259 232 YLKFRLPDI--TRFSAEFDFRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFSTQITTGGNVINNGIWNMVSVE 309
Cdd:cd00110    9 YVRLPTLPAprTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSVSVE 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755553259 310 ELDDSVSIKIAKEAVMNINKLGSLFkptDGFLDTKIYFAGLPRKVESALIkPINPRLDGCIRGWNL 375
Cdd:cd00110   89 RNGRSVTLSVDGERVVESGSPGGSA---LLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKV 150
LamG smart00282
Laminin G domain;
244-375 2.38e-22

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 92.79  E-value: 2.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259   244 SAEFDFRTYDSEGIILYAESLDHSNWLLIALRDGKIEVQFKNEFS-TQITTGGNVINNGIWNMVSVEELDDSVSIKIAKE 322
Cdd:smart00282   1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGpARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 755553259   323 AVMNINKLGSlfkPTDGFLDTKIYFAGLPRkVESALIKPINPRLDGCIRGWNL 375
Cdd:smart00282  81 NRVSGESPGG---LTILNLDGPLYLGGLPE-DLKLPPLPVTPGFRGCIRNLKV 129
Laminin_G_2 pfam02210
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ...
 249-375 5.34e-12

Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.


Pssm-ID: 460494 [Multi-domain]  Cd Length: 126  Bit Score: 63.21  E-value: 5.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259  249 FRTYDSEGIILYAESLDHSnWLLIALRDGKIEVQFKNEFSTQ-ITTGGNVINNGIWNMVSVEELDDSVSIKIAKEAVMNI 327
Cdd:pfam02210   1 FRTRQPNGLLLYAGGGGSD-FLALELVNGRLVLRYDLGSGPEsLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 755553259  328 NKLGslfKPTDGFLDTKIYFAGLPRKVESALIkPINPRLDGCIRGWNL 375
Cdd:pfam02210  80 LPPG---ESLLLNLNGPLYLGGLPPLLLLPAL-PVRAGFVGCIRDVRV 123
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 85-119 1.42e-07

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: 47.62  E-value: 1.42e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 755553259   85 SNVNGGCSQICDNTPGSYHCSCKRGFAMLPNKKDC 119
Cdd:pfam14670   2 SVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGRTC 36
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 167-202 3.23e-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: 3.23e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 755553259  167 CSEN--MCAQLCVNFPGGYSCYCDgkKGFKLAQDQKSC 202
Cdd:pfam14670   1 CSVNngGCSHLCLNTPGGYTCSCP--EGYELQDDGRTC 36
EGF_CA smart00179
Calcium-binding EGF-like domain;
77-110 4.05e-05

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 41.08  E-value: 4.05e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 755553259    77 DVNECKDPSN-VNGGcsqICDNTPGSYHCSCKRGF 110
Cdd:smart00179   1 DIDECASGNPcQNGG---TCVNTVGSYRCECPPGY 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 77-110 6.39e-05

Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.


Pssm-ID: 238011  Cd Length: 38  Bit Score: 40.31  E-value: 6.39e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 755553259  77 DVNECKDPSN-VNGGcsqICDNTPGSYHCSCKRGF 110
Cdd:cd00054    1 DIDECASGNPcQNGG---TCVNTVGSYRCSCPPGY 32
EGF_CA pfam07645
Calcium-binding EGF domain;
121-151 7.56e-05

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.91  E-value: 7.56e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 755553259  121 DLDECALKPSVC-GTAVCKNIPGDFECECPDG 151
Cdd:pfam07645   1 DVDECATGTHNCpANTVCVNTIGSFECRCPDG 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
121-153 1.70e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 39.15  E-value: 1.70e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 755553259   121 DLDECALkPSVCGT-AVCKNIPGDFECECPDGYR 153
Cdd:smart00179   1 DIDECAS-GNPCQNgGTCVNTVGSYRCECPPGYT 33
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 121-153 2.79e-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: 38.39  E-value: 2.79e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 755553259 121 DLDECALkPSVCG-TAVCKNIPGDFECECPDGYR 153
Cdd:cd00054    1 DIDECAS-GNPCQnGGTCVNTVGSYRCSCPPGYT 33
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 90-117 3.13e-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: 42.37  E-value: 3.13e-04
                         10        20
                 ....*....|....*....|....*...
gi 755553259  90 GCSQICDNTPGSYHCSCKRGFAMLPNKK 117
Cdd:cd01475  196 VCQQVCISTPGSYLCACTEGYALLEDNK 223
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 146-166 4.72e-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: 37.39  E-value: 4.72e-04
                          10        20
                  ....*....|....*....|.
gi 755553259  146 CECPDGYRYDPSSKSCKDVDE 166
Cdd:pfam12662   2 CSCPPGYQLDPDGRTCVDIDE 22
EGF_CA pfam07645
Calcium-binding EGF domain;
77-109 6.31e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 37.22  E-value: 6.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 755553259   77 DVNECKDPSNVnggCSQ--ICDNTPGSYHCSCKRG 109
Cdd:pfam07645   1 DVDECATGTHN---CPAntVCVNTIGSFECRCPDG 32
LamG smart00282
Laminin G domain;
429-566 6.97e-04

Laminin G domain;


Pssm-ID: 214598 [Multi-domain]  Cd Length: 132  Bit Score: 40.02  E-value: 6.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755553259   429 NVTLNIRPSTGTGVMLALVSGGTVPF-ALSLVDSRsgtsqdIVVFVENS---VVARLEAVSLCSDQQSQLKCNVNRNGLE 504
Cdd:smart00282   1 SISFSFRTTSPNGLLLYAGSKGGGDYlALELRDGR------LVLRYDLGsgpARLTSDPTPLNDGQWHRVAVERNGRSVT 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755553259   505 LWTPLRKDVIYSKDLQRQLAVLDKAMkrtvatYLGGIP-DISFSATPVNAFYSGCME-VNINGV 566
Cdd:smart00282  75 LSVDGGNRVSGESPGGLTILNLDGPL------YLGGLPeDLKLPPLPVTPGFRGCIRnLKVNGK 132
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 161-201 8.45e-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: 41.22  E-value: 8.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755553259 161 CKDVDECSE--NMCAQLCVNFPGGYSCYCdgKKGFKLAQDQKS 201
Cdd:cd01475  184 CVVPDLCATlsHVCQQVCISTPGSYLCAC--TEGYALLEDNKT 224
EGF_CA smart00179
Calcium-binding EGF-like domain;
163-203 1.42e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 36.46  E-value: 1.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 755553259   163 DVDEC-SENMCAQ--LCVNFPGGYSCYCdgKKGFklaQDQKSCE 203
Cdd:smart00179   1 DIDECaSGNPCQNggTCVNTVGSYRCEC--PPGY---TDGRNCE 39
EGF_CA pfam07645
Calcium-binding EGF domain;
163-188 6.24e-03

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 34.52  E-value: 6.24e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 755553259  163 DVDECSE--NMCAQ--LCVNFPGGYSCYCD 188
Cdd:pfam07645   1 DVDECATgtHNCPAntVCVNTIGSFECRCP 30
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 163-203 6.98e-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: 34.53  E-value: 6.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 755553259 163 DVDEC-SENMCA--QLCVNFPGGYSCYCDgkKGFKLaqdqKSCE 203
Cdd:cd00054    1 DIDECaSGNPCQngGTCVNTVGSYRCSCP--PGYTG----RNCE 38
 
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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