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Conserved domains on  [gi|296011073|ref|NP_001171622|]
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nephronectin isoform E precursor [Homo sapiens]

Protein Classification

EGF_CA and MAM domain-containing protein( domain architecture ID 11235862)

protein containing domains FXa_inhibition, cEGF, EGF_CA, and MAM

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 423-562 6.31e-30

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


:

Pssm-ID: 99706  Cd Length: 157  Bit Score: 115.17  E-value: 6.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073 423 CNFDHGLCGWIREKDNDLHWEPIR--------------DPAGGQYLTVSAAKAPGGKAARLVLPLGRLMhSGDLCLSFRH 488
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSgstpspgtppdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPP-RSSHCLSFWY 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296011073 489 KVTGLHSGTLQVFVRKHGA-HGAALWGRNG--GHGWRQTQITL-RGADIKSVVFKGEKRRGHTGEIGLDDVSLKKGHC 562
Cdd:cd06263   80 HMYGSGVGTLNVYVREEGGgLGTLLWSASGgqGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 248-283 5.91e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


:

Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 51.45  E-value: 5.91e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 296011073  248 CSLGQYQCSSFARCYNIRGSYKCKCKEGYQGDGLTC 283
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA pfam07645
Calcium-binding EGF domain;
199-227 2.77e-06

Calcium-binding EGF domain;


:

Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.15  E-value: 2.77e-06
                          10        20
                  ....*....|....*....|....*....
gi 296011073  199 DVDECATGRASCPRFRQCVNTFGSYICKC 227
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 180-202 4.96e-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: 4.96e-04
                          10        20
                  ....*....|....*....|...
gi 296011073  180 RCQCPsPGLQLAPDGRTCVDVDE 202
Cdd:pfam12662   1 TCSCP-PGYQLDPDGRTCVDIDE 22
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 123-157 5.10e-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: 37.61  E-value: 5.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 296011073  123 CGLKPRPCKHRCMNTYGSYKCYCLNGYMLMPDG-SC 157
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGrTC 36
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 423-562 6.31e-30

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 115.17  E-value: 6.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073 423 CNFDHGLCGWIREKDNDLHWEPIR--------------DPAGGQYLTVSAAKAPGGKAARLVLPLGRLMhSGDLCLSFRH 488
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSgstpspgtppdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPP-RSSHCLSFWY 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296011073 489 KVTGLHSGTLQVFVRKHGA-HGAALWGRNG--GHGWRQTQITL-RGADIKSVVFKGEKRRGHTGEIGLDDVSLKKGHC 562
Cdd:cd06263   80 HMYGSGVGTLNVYVREEGGgLGTLLWSASGgqGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 423-563 4.32e-19

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 84.34  E-value: 4.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073  423 CNFDHG-LCGWIREKDNDLHWE----------PIRD----PAGGQYLTVSAAKAPGGKAARLVLPLgrlMH--SGDLCLS 485
Cdd:pfam00629   1 CDFEDGnLCGWTQDSSDDFDWErvsgpsvktgPSSDhtqgTGSGHFMYVDTSSGAPGQTARLLSPL---LPpsRSPQCLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073  486 FRHKVTGLHSGTLQVFVRKHGAH-GAALWGRNGGHG--WRQTQITL--RGADIKsVVFKGEKRRGHTGEIGLDDVSLKKG 560
Cdd:pfam00629  78 FWYHMSGSGVGTLRVYVRENGGTlDTLLWSISGDQGpsWKEARVTLssSTQPFQ-VVFEGIRGGGSRGGIALDDISLSSG 156


                  ...
gi 296011073  561 HCS 563
Cdd:pfam00629 157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 421-562 3.40e-18

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 82.01  E-value: 3.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073   421 HSCNF-DHGLCGWIREKDNDLHWE----------PIRDPAGGQ--YLTVSAAKAPGGKAARLVLPLGRLMHSGDlCLSFR 487
Cdd:smart00137   4 GNCDFeEGSTCGWHQDSNDDGHWErvssatgipgPNRDHTTGNghFMFFETSSGAEGQTARLLSPPLYENRSTH-CLTFW 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296011073   488 HKVTGLHSGTLQVFVR-KHGAHGAALWGRNG--GHGWRQTQITLRGADIK-SVVFKGEKRRGHTGEIGLDDVSLKKGHC 562
Cdd:smart00137  83 YYMYGSGSGTLNVYVReNNGSQDTLLWSRSGtqGGQWLQAEVALSSWPQPfQVVFEGTRGKGHSGYIALDDILLSNGPC 161
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 248-283 5.91e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 51.45  E-value: 5.91e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 296011073  248 CSLGQYQCSSFARCYNIRGSYKCKCKEGYQGDGLTC 283
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA pfam07645
Calcium-binding EGF domain;
199-227 2.77e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.15  E-value: 2.77e-06
                          10        20
                  ....*....|....*....|....*....
gi 296011073  199 DVDECATGRASCPRFRQCVNTFGSYICKC 227
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
244-284 4.62e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 4.62e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 296011073   244 DIDECSLGQYqCSSFARCYNIRGSYKCKCKEGYQgDGLTCV 284
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 244-279 4.53e-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: 40.70  E-value: 4.53e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 296011073 244 DIDECSLGQyQCSSFARCYNIRGSYKCKCKEGYQGD 279
Cdd:cd00054    1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGYTGR 35
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 194-234 5.92e-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: 44.68  E-value: 5.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 296011073 194 GRTCVDVDECATGRASCPRFrqCVNTFGSYICKCHKGFDLM 234
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQV--CISTPGSYLCACTEGYALL 219
EGF_CA smart00179
Calcium-binding EGF-like domain;
199-231 2.62e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 2.62e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 296011073   199 DVDECATGrASCPRFRQCVNTFGSYICKCHKGF 231
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 32
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 180-202 4.96e-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: 4.96e-04
                          10        20
                  ....*....|....*....|...
gi 296011073  180 RCQCPsPGLQLAPDGRTCVDVDE 202
Cdd:pfam12662   1 TCSCP-PGYQLDPDGRTCVDIDE 22
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 123-157 5.10e-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: 37.61  E-value: 5.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 296011073  123 CGLKPRPCKHRCMNTYGSYKCYCLNGYMLMPDG-SC 157
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGrTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 119-151 4.18e-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: 35.31  E-value: 4.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 296011073 119 DLNECgLKPRPCKH--RCMNTYGSYKCYCLNGYML 151
Cdd:cd00054    1 DIDEC-ASGNPCQNggTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
119-150 4.87e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 4.87e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 296011073   119 DLNECgLKPRPCKH--RCMNTYGSYKCYCLNGYM 150
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT 33
 
Name Accession Description Interval E-value
MAM cd06263
Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular ...
 423-562 6.31e-30

Meprin, A5 protein, and protein tyrosine phosphatase Mu (MAM) domain. MAM is an extracellular domain which mediates protein-protein interactions and is found in a diverse set of proteins, many of which are known to function in cell adhesion. Members include: type IIB receptor protein tyrosine phosphatases (such as RPTPmu), meprins (plasma membrane metalloproteases), neuropilins (receptors of secreted semaphorins), and zonadhesins (sperm-specific membrane proteins which bind to the extracellular matrix of the egg). In meprin A and neuropilin-1 and -2, MAM is involved in homo-oligomerization. In RPTPmu, it has been associated with both homophilic adhesive (trans) interactions and lateral (cis) receptor oligomerization. In a GPI-anchored protein that is expressed in cells in the embryonic chicken spinal chord, MDGA1, the MAM domain has been linked to heterophilic interactions with axon-rich region.


Pssm-ID: 99706  Cd Length: 157  Bit Score: 115.17  E-value: 6.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073 423 CNFDHGLCGWIREKDNDLHWEPIR--------------DPAGGQYLTVSAAKAPGGKAARLVLPLGRLMhSGDLCLSFRH 488
Cdd:cd06263    1 CDFEDGLCGWTQDSTDDFDWTRVSgstpspgtppdhthGTGSGHYLYVESSSGREGQKARLLSPLLPPP-RSSHCLSFWY 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296011073 489 KVTGLHSGTLQVFVRKHGA-HGAALWGRNG--GHGWRQTQITL-RGADIKSVVFKGEKRRGHTGEIGLDDVSLKKGHC 562
Cdd:cd06263   80 HMYGSGVGTLNVYVREEGGgLGTLLWSASGgqGNQWQEAEVTLsASSKPFQVVFEGVRGSGSRGDIALDDISLSPGPC 157
MAM pfam00629
MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain ...
 423-563 4.32e-19

MAM domain, meprin/A5/mu; An extracellular domain found in many receptors. The MAM domain along with the associated Ig domain in type IIB receptor protein tyrosine phosphatases forms a structural unit (termed MIg) with a seamless interdomain interface. It plays a major role in homodimerization of the phosphatase ectoprotein and in cell adhesion. MAM is a beta-sandwich consisting of two five-stranded antiparallel beta-sheets rotated away from each other by approx 25 degrees, and plays a similar role in meprin metalloproteinases.


Pssm-ID: 459878 [Multi-domain]  Cd Length: 159  Bit Score: 84.34  E-value: 4.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073  423 CNFDHG-LCGWIREKDNDLHWE----------PIRD----PAGGQYLTVSAAKAPGGKAARLVLPLgrlMH--SGDLCLS 485
Cdd:pfam00629   1 CDFEDGnLCGWTQDSSDDFDWErvsgpsvktgPSSDhtqgTGSGHFMYVDTSSGAPGQTARLLSPL---LPpsRSPQCLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073  486 FRHKVTGLHSGTLQVFVRKHGAH-GAALWGRNGGHG--WRQTQITL--RGADIKsVVFKGEKRRGHTGEIGLDDVSLKKG 560
Cdd:pfam00629  78 FWYHMSGSGVGTLRVYVRENGGTlDTLLWSISGDQGpsWKEARVTLssSTQPFQ-VVFEGIRGGGSRGGIALDDISLSSG 156


                  ...
gi 296011073  561 HCS 563
Cdd:pfam00629 157 PCP 159
MAM smart00137
Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an ...
 421-562 3.40e-18

Domain in meprin, A5, receptor protein tyrosine phosphatase mu (and others); Likely to have an adhesive function. Mutations in the meprin MAM domain affect noncovalent associations within meprin oligomers. In receptor tyrosine phosphatase mu-like molecules the MAM domain is important for homophilic cell-cell interactions.


Pssm-ID: 214533 [Multi-domain]  Cd Length: 161  Bit Score: 82.01  E-value: 3.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296011073   421 HSCNF-DHGLCGWIREKDNDLHWE----------PIRDPAGGQ--YLTVSAAKAPGGKAARLVLPLGRLMHSGDlCLSFR 487
Cdd:smart00137   4 GNCDFeEGSTCGWHQDSNDDGHWErvssatgipgPNRDHTTGNghFMFFETSSGAEGQTARLLSPPLYENRSTH-CLTFW 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296011073   488 HKVTGLHSGTLQVFVR-KHGAHGAALWGRNG--GHGWRQTQITLRGADIK-SVVFKGEKRRGHTGEIGLDDVSLKKGHC 562
Cdd:smart00137  83 YYMYGSGSGTLNVYVReNNGSQDTLLWSRSGtqGGQWLQAEVALSSWPQPfQVVFEGTRGKGHSGYIALDDILLSNGPC 161
EGF_3 pfam12947
EGF domain; This family includes a variety of EGF-like domain homologs. This family includes ...
 248-283 5.91e-09

EGF domain; This family includes a variety of EGF-like domain homologs. This family includes the C-terminal domain of the malaria parasite MSP1 protein.


Pssm-ID: 463759 [Multi-domain]  Cd Length: 36  Bit Score: 51.45  E-value: 5.91e-09
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 296011073  248 CSLGQYQCSSFARCYNIRGSYKCKCKEGYQGDGLTC 283
Cdd:pfam12947   1 CSDNNGGCHPNATCTNTGGSFTCTCNDGYTGDGVTC 36
EGF_CA pfam07645
Calcium-binding EGF domain;
199-227 2.77e-06

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 44.15  E-value: 2.77e-06
                          10        20
                  ....*....|....*....|....*....
gi 296011073  199 DVDECATGRASCPRFRQCVNTFGSYICKC 227
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRC 29
EGF_CA smart00179
Calcium-binding EGF-like domain;
244-284 4.62e-06

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 43.39  E-value: 4.62e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 296011073   244 DIDECSLGQYqCSSFARCYNIRGSYKCKCKEGYQgDGLTCV 284
Cdd:smart00179   1 DIDECASGNP-CQNGGTCVNTVGSYRCECPPGYT-DGRNCE 39
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 244-279 4.53e-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: 40.70  E-value: 4.53e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 296011073 244 DIDECSLGQyQCSSFARCYNIRGSYKCKCKEGYQGD 279
Cdd:cd00054    1 DIDECASGN-PCQNGGTCVNTVGSYRCSCPPGYTGR 35
vWA_Matrilin cd01475
VWA_Matrilin: In cartilaginous plate, extracellular matrix molecules mediate cell-matrix and ...
 194-234 5.92e-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: 44.68  E-value: 5.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 296011073 194 GRTCVDVDECATGRASCPRFrqCVNTFGSYICKCHKGFDLM 234
Cdd:cd01475  181 GKICVVPDLCATLSHVCQQV--CISTPGSYLCACTEGYALL 219
EGF_CA pfam07645
Calcium-binding EGF domain;
244-275 1.12e-04

Calcium-binding EGF domain;


Pssm-ID: 429571  Cd Length: 32  Bit Score: 39.53  E-value: 1.12e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 296011073  244 DIDECSLGQYQCSSFARCYNIRGSYKCKCKEG 275
Cdd:pfam07645   1 DVDECATGTHNCPANTVCVNTIGSFECRCPDG 32
EGF_CA smart00179
Calcium-binding EGF-like domain;
199-231 2.62e-04

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 38.38  E-value: 2.62e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 296011073   199 DVDECATGrASCPRFRQCVNTFGSYICKCHKGF 231
Cdd:smart00179   1 DIDECASG-NPCQNGGTCVNTVGSYRCECPPGY 32
cEGF pfam12662
Complement Clr-like EGF-like; cEGF, or complement Clr-like EGF, domains have six conserved ...
 180-202 4.96e-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: 4.96e-04
                          10        20
                  ....*....|....*....|...
gi 296011073  180 RCQCPsPGLQLAPDGRTCVDVDE 202
Cdd:pfam12662   1 TCSCP-PGYQLDPDGRTCVDIDE 22
FXa_inhibition pfam14670
Coagulation Factor Xa inhibitory site; This short domain on coagulation enzyme factor Xa is ...
 123-157 5.10e-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: 37.61  E-value: 5.10e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 296011073  123 CGLKPRPCKHRCMNTYGSYKCYCLNGYMLMPDG-SC 157
Cdd:pfam14670   1 CSVNNGGCSHLCLNTPGGYTCSCPEGYELQDDGrTC 36
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 199-231 2.04e-03

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


Pssm-ID: 238011  Cd Length: 38  Bit Score: 36.08  E-value: 2.04e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 296011073 199 DVDECATGrASCPRFRQCVNTFGSYICKCHKGF 231
Cdd:cd00054    1 DIDECASG-NPCQNGGTCVNTVGSYRCSCPPGY 32
EGF_CA cd00054
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ...
 119-151 4.18e-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: 35.31  E-value: 4.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 296011073 119 DLNECgLKPRPCKH--RCMNTYGSYKCYCLNGYML 151
Cdd:cd00054    1 DIDEC-ASGNPCQNggTCVNTVGSYRCSCPPGYTG 34
EGF_CA smart00179
Calcium-binding EGF-like domain;
119-150 4.87e-03

Calcium-binding EGF-like domain;


Pssm-ID: 214542 [Multi-domain]  Cd Length: 39  Bit Score: 34.92  E-value: 4.87e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 296011073   119 DLNECgLKPRPCKH--RCMNTYGSYKCYCLNGYM 150
Cdd:smart00179   1 DIDEC-ASGNPCQNggTCVNTVGSYRCECPPGYT 33
 
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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