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Conserved domains on  [gi|6754904|ref|NP_035077|]
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netrin-3 precursor [Mus musculus]

Protein Classification

EGF_Lam and NTR_netrin-1_like domain-containing protein( domain architecture ID 10919287)

protein containing domains Laminin_N, EGF_Lam, and NTR_netrin-1_like

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_N super family cl02806
Laminin N-terminal (Domain VI);
34-253 3.97e-79

Laminin N-terminal (Domain VI);


The actual alignment was detected with superfamily member smart00136:

Pssm-ID: 470680  Cd Length: 238  Bit Score: 249.20  E-value: 3.97e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904      34 AREPRSCIPGLVNAALGREVLASSTCGRSAN----------------RVCDSSDPQRAHSADLLTSAPGTASPLCWRSDL 97
Cdd:smart00136   1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPerycklvghteqgkkcDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904      98 LQQAPFNVTLTVPLGKAFELVFVSLRFCSAPPtSVALLKSQDHGRSWVPLGFFSSSCTLDYGRLPAPADGPsGPGPEALC 177
Cdd:smart00136  81 LSNGPQNVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITK-GNEDEVIC 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904     178 FPAPQA-QPDGGGLLAFSVQDGSPQGLDLDNSPVLQDWVTATDIRIVLTRPAIQGDTRDGG---VTVPYSYSATELQVGG 253
Cdd:smart00136 159 TSEYSDiVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrpeVTRRYYYAISDIAVGG 238
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 456-562 4.32e-34

NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity.


:

Pssm-ID: 239634  Cd Length: 115  Bit Score: 125.05  E-value: 4.32e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904  456 LKKFCRKDYAVQVAVGARgEARGSWTRFPVAVLAVFRSGEERARRGSSALWVPTLDAACGCPRLLPGRRYLLLGGGPGAA 535
Cdd:cd03579   1 LKKYCKKDYAVQAQVLSR-ETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSP 79

                        90       100
                ....*....|....*....|....*..
gi 6754904  536 AGStagrgqGLSAARGSLVLPWRDAWT 562
Cdd:cd03579  80 ERG------GLILDKRSLVIEWRDEWA 100
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 373-422 2.08e-12

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 61.99  E-value: 2.08e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 6754904  373 ACDCHPVGAAGKTCNQTTGQCPCKDGVTGLTCNRCAPGFQQSRSPVAPCV 422
Cdd:cd00055   1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 254-299 5.74e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 46.58  E-value: 5.74e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6754904  254 RCKCNGHAS---RCLLDThghLVCDCQHGTEGPDCSRCKPFYCDRPWQR 299
Cdd:cd00055   1 PCDCNGHGSlsgQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 311-362 1.08e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.03  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6754904    311 CSCNGHA---RRCRFnmelyrlsgrrSGGVCLnCRHNTAGRHCHYCREGFYRDPG 362
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 34-253 3.97e-79

Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.


Pssm-ID: 214532  Cd Length: 238  Bit Score: 249.20  E-value: 3.97e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904      34 AREPRSCIPGLVNAALGREVLASSTCGRSAN----------------RVCDSSDPQRAHSADLLTSAPGTASPLCWRSDL 97
Cdd:smart00136   1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPerycklvghteqgkkcDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904      98 LQQAPFNVTLTVPLGKAFELVFVSLRFCSAPPtSVALLKSQDHGRSWVPLGFFSSSCTLDYGRLPAPADGPsGPGPEALC 177
Cdd:smart00136  81 LSNGPQNVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITK-GNEDEVIC 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904     178 FPAPQA-QPDGGGLLAFSVQDGSPQGLDLDNSPVLQDWVTATDIRIVLTRPAIQGDTRDGG---VTVPYSYSATELQVGG 253
Cdd:smart00136 159 TSEYSDiVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrpeVTRRYYYAISDIAVGG 238
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
40-253 3.01e-53

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 181.24  E-value: 3.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904     40 CIPGLVNAALGREVLASSTCGRSAN---------------RVCDSSDPQRAHSADLLTSAPGTASPLCWRSDLLQQAPFN 104
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGLNGPerycilsgleggkkcFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVIQYEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904    105 VTLTVPLGKAFELVFVSLRFCSAPPTSVALLKSQDHGRSWVPLGFFSSSCTLDYGRlpaPADGPSGPGP-EALC-----F 178
Cdd:pfam00055  81 VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGR---PSGPSRGIKDdEVICtseysD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6754904    179 PAPQaqpdGGGLLAFSVQDGSPQGLDLDNSPVLQDWVTATDIRIVLTRPAIQGDTRDGGVTVP--YSYSATELQVGG 253
Cdd:pfam00055 158 ISPL----TGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLrkYYYAISDISVGG 230
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 456-562 4.32e-34

NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity.


Pssm-ID: 239634  Cd Length: 115  Bit Score: 125.05  E-value: 4.32e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904  456 LKKFCRKDYAVQVAVGARgEARGSWTRFPVAVLAVFRSGEERARRGSSALWVPTLDAACGCPRLLPGRRYLLLGGGPGAA 535
Cdd:cd03579   1 LKKYCKKDYAVQAQVLSR-ETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSP 79

                        90       100
                ....*....|....*....|....*..
gi 6754904  536 AGStagrgqGLSAARGSLVLPWRDAWT 562
Cdd:cd03579  80 ERG------GLILDKRSLVIEWRDEWA 100
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 457-562 2.66e-17

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 77.77  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904    457 KKFCR-KDYAVQVAVGARgEARGSWTRFPVAVLAVFRSGEERARRGSSALWVPtlDAACGCPRLLPGRRYLLLGGGPGAA 535
Cdd:pfam01759   1 KKACKgSDYVYKVKVLSV-EEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLK--RGDCRCPQLRLGKEYLIMGKVGDLE 77

                          90       100
                  ....*....|....*....|....*..
gi 6754904    536 AGStagrgqGLSAARGSLVLPWRDAWT 562
Cdd:pfam01759  78 GRG------RYVLDKNSWVEPWPTKWE 98
C345C smart00643
Netrin C-terminal Domain;
456-562 1.47e-16

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 75.87  E-value: 1.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904     456 LKKFCRK--DYAVQVAVGARGEaRGSWTRFPVAVLAVFRSGEERARRGSSALWVPTLDAACGCPRLL-PGRRYLLLGGGP 532
Cdd:smart00643   1 LEKACKSdvDYVYKVKVLSVEE-EGGFDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCPLLLkLGKSYLIMGKSG 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 6754904     533 GAAAGSTAGrgqGLSAARGSLVLPWRDAWT 562
Cdd:smart00643  80 DLWDAKGRG---QYVLGKNSWVEEWPTEEE 106
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 373-422 2.08e-12

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 61.99  E-value: 2.08e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 6754904  373 ACDCHPVGAAGKTCNQTTGQCPCKDGVTGLTCNRCAPGFQQSRSPVAPCV 422
Cdd:cd00055   1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 374-411 2.31e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.60  E-value: 2.31e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6754904    374 CDCHPVGAAGKTCNQTTGQCPCKDGVTGLTCNRCAPGF 411
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
374-411 3.31e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 61.17  E-value: 3.31e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 6754904     374 CDCHPVGAAGKTCNQTTGQCPCKDGVTGLTCNRCAPGF 411
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 254-299 5.74e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 46.58  E-value: 5.74e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6754904  254 RCKCNGHAS---RCLLDThghLVCDCQHGTEGPDCSRCKPFYCDRPWQR 299
Cdd:cd00055   1 PCDCNGHGSlsgQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 255-292 6.83e-05

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.41  E-value: 6.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6754904    255 CKCNGHAS---RCLLDThghLVCDCQHGTEGPDCSRCKPFY 292
Cdd:pfam00053   1 CDCNPHGSlsdTCDPET---GQCLCKPGVTGRHCDRCKPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 311-362 1.08e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.03  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6754904    311 CSCNGHA---RRCRFnmelyrlsgrrSGGVCLnCRHNTAGRHCHYCREGFYRDPG 362
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 310-363 1.32e-04

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 39.64  E-value: 1.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6754904  310 ACSCNGHA---RRCRfnmelyrlsgrRSGGVCLnCRHNTAGRHCHYCREGFYRDPGR 363
Cdd:cd00055   1 PCDCNGHGslsGQCD-----------PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
255-298 9.06e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 9.06e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6754904     255 CKCN--GHASR-CLLDThghLVCDCQHGTEGPDCSRCKPFYCDRPWQ 298
Cdd:smart00180   1 CDCDpgGSASGtCDPDT---GQCECKPNVTGRRCDRCAPGYYGDGPP 44
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
335-362 2.90e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 35.75  E-value: 2.90e-03
                           10        20
                   ....*....|....*....|....*...
gi 6754904     335 GGVCLnCRHNTAGRHCHYCREGFYRDPG 362
Cdd:smart00180  17 TGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 34-253 3.97e-79

Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.


Pssm-ID: 214532  Cd Length: 238  Bit Score: 249.20  E-value: 3.97e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904      34 AREPRSCIPGLVNAALGREVLASSTCGRSAN----------------RVCDSSDPQRAHSADLLTSAPGTASPLCWRSDL 97
Cdd:smart00136   1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPerycklvghteqgkkcDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904      98 LQQAPFNVTLTVPLGKAFELVFVSLRFCSAPPtSVALLKSQDHGRSWVPLGFFSSSCTLDYGRLPAPADGPsGPGPEALC 177
Cdd:smart00136  81 LSNGPQNVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITK-GNEDEVIC 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904     178 FPAPQA-QPDGGGLLAFSVQDGSPQGLDLDNSPVLQDWVTATDIRIVLTRPAIQGDTRDGG---VTVPYSYSATELQVGG 253
Cdd:smart00136 159 TSEYSDiVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDrpeVTRRYYYAISDIAVGG 238
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
40-253 3.01e-53

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 181.24  E-value: 3.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904     40 CIPGLVNAALGREVLASSTCGRSAN---------------RVCDSSDPQRAHSADLLTSAPGTASPLCWRSDLLQQAPFN 104
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGLNGPerycilsgleggkkcFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVIQYEN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904    105 VTLTVPLGKAFELVFVSLRFCSAPPTSVALLKSQDHGRSWVPLGFFSSSCTLDYGRlpaPADGPSGPGP-EALC-----F 178
Cdd:pfam00055  81 VNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGR---PSGPSRGIKDdEVICtseysD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6754904    179 PAPQaqpdGGGLLAFSVQDGSPQGLDLDNSPVLQDWVTATDIRIVLTRPAIQGDTRDGGVTVP--YSYSATELQVGG 253
Cdd:pfam00055 158 ISPL----TGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLrkYYYAISDISVGG 230
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 456-562 4.32e-34

NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called domain C in the context of C. elegans netrin UNC-6. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. These proteins may be chemoattractive to some neurons and chemorepellant for others. In the case of netrin-1, attraction and repulsion responses are mediated by the DCC and UNC-5 receptor families. The biological activities of C. elegans UNC-6, which may either attract or repel migrating cells or axons, are mediated by its different domains. The C-terminal NTR domain of UNC-6 has been shown to inhibit axon branching activity.


Pssm-ID: 239634  Cd Length: 115  Bit Score: 125.05  E-value: 4.32e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904  456 LKKFCRKDYAVQVAVGARgEARGSWTRFPVAVLAVFRSGEERARRGSSALWVPTLDAACGCPRLLPGRRYLLLGGGPGAA 535
Cdd:cd03579   1 LKKYCKKDYAVQAQVLSR-ETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSP 79

                        90       100
                ....*....|....*....|....*..
gi 6754904  536 AGStagrgqGLSAARGSLVLPWRDAWT 562
Cdd:cd03579  80 ERG------GLILDKRSLVIEWRDEWA 100
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 457-562 2.66e-17

UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein family members, and hence the existence of the UNC-6 module, was first reported in. Subsequently, many additional members of the family were identified on the basis of sequence similarity between the C-terminal domains of netrins, complement proteins C3, C4, C5, secreted frizzled-related proteins, and type I pro-collagen C-proteinase enhancer proteins (PCOLCEs), which are homologous with the N-terminal domains of tissue inhibitors of metalloproteinases (TIMPs). The TIMPs are classified as a separate family in Pfam (pfam00965). This expanded domain family has been named as the NTR module.


Pssm-ID: 396359  Cd Length: 106  Bit Score: 77.77  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904    457 KKFCR-KDYAVQVAVGARgEARGSWTRFPVAVLAVFRSGEERARRGSSALWVPtlDAACGCPRLLPGRRYLLLGGGPGAA 535
Cdd:pfam01759   1 KKACKgSDYVYKVKVLSV-EEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLK--RGDCRCPQLRLGKEYLIMGKVGDLE 77

                          90       100
                  ....*....|....*....|....*..
gi 6754904    536 AGStagrgqGLSAARGSLVLPWRDAWT 562
Cdd:pfam01759  78 GRG------RYVLDKNSWVEPWPTKWE 98
C345C smart00643
Netrin C-terminal Domain;
456-562 1.47e-16

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 75.87  E-value: 1.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904     456 LKKFCRK--DYAVQVAVGARGEaRGSWTRFPVAVLAVFRSGEERARRGSSALWVPTLDAACGCPRLL-PGRRYLLLGGGP 532
Cdd:smart00643   1 LEKACKSdvDYVYKVKVLSVEE-EGGFDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCPLLLkLGKSYLIMGKSG 79

                           90       100       110
                   ....*....|....*....|....*....|
gi 6754904     533 GAAAGSTAGrgqGLSAARGSLVLPWRDAWT 562
Cdd:smart00643  80 DLWDAKGRG---QYVLGKNSWVEEWPTEEE 106
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 373-422 2.08e-12

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 61.99  E-value: 2.08e-12
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 6754904  373 ACDCHPVGAAGKTCNQTTGQCPCKDGVTGLTCNRCAPGFQQSRSPVAPCV 422
Cdd:cd00055   1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 374-411 2.31e-12

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 61.60  E-value: 2.31e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 6754904    374 CDCHPVGAAGKTCNQTTGQCPCKDGVTGLTCNRCAPGF 411
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
374-411 3.31e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 61.17  E-value: 3.31e-12
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 6754904     374 CDCHPVGAAGKTCNQTTGQCPCKDGVTGLTCNRCAPGF 411
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 457-560 3.47e-09

NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in netrins, complement proteins, tissue inhibitors of metalloproteases (TIMP), and procollagen C-proteinase enhancers (PCOLCE), amongst others. In netrins, the domain plays a role in controlling axon branching in neural development, while the common function of these modules in TIMPs appears to be binding to metzincins. A subset of this family is also known as the C345C domain because it occurs as a C-terminal domain in complement C3, C4 and C5. In C5, the domain interacts with various partners during the formation of the membrane attack complex.


Pssm-ID: 239600  Cd Length: 105  Bit Score: 54.40  E-value: 3.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754904  457 KKFCRKDYAVQVAVGARGEArGSWTRFPVAVLAVFRSGEERARRGSSALWVPTLDAACGCPRLLPGRRYLLLGGGPGAAA 536
Cdd:cd03523   1 KAFCKSDYVVRAKIKEIKEE-NDDVKYEVKIIKIYKTGKAKADKADLRFYYTAPACCPCHPILNPGREYLIMGKEEDSQG 79

                        90       100
                ....*....|....*....|....
gi 6754904  537 gstagrgqGLSAARGSLVLPWRDA 560
Cdd:cd03523  80 --------GLVLDPLSFVEPWSPL 95
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 254-299 5.74e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 46.58  E-value: 5.74e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6754904  254 RCKCNGHAS---RCLLDThghLVCDCQHGTEGPDCSRCKPFYCDRPWQR 299
Cdd:cd00055   1 PCDCNGHGSlsgQCDPGT---GQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 255-292 6.83e-05

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.41  E-value: 6.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6754904    255 CKCNGHAS---RCLLDThghLVCDCQHGTEGPDCSRCKPFY 292
Cdd:pfam00053   1 CDCNPHGSlsdTCDPET---GQCLCKPGVTGRHCDRCKPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 311-362 1.08e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.03  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6754904    311 CSCNGHA---RRCRFnmelyrlsgrrSGGVCLnCRHNTAGRHCHYCREGFYRDPG 362
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGLPS 43
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 310-363 1.32e-04

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 39.64  E-value: 1.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6754904  310 ACSCNGHA---RRCRfnmelyrlsgrRSGGVCLnCRHNTAGRHCHYCREGFYRDPGR 363
Cdd:cd00055   1 PCDCNGHGslsGQCD-----------PGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
255-298 9.06e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 9.06e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 6754904     255 CKCN--GHASR-CLLDThghLVCDCQHGTEGPDCSRCKPFYCDRPWQ 298
Cdd:smart00180   1 CDCDpgGSASGtCDPDT---GQCECKPNVTGRRCDRCAPGYYGDGPP 44
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 457-527 1.75e-03

NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta netrin) and similar proteins. Netrins are secreted proteins that function as tropic cues in the direction of axon growth and cell migration during neural development. Netrin-4 is a basement membrane component that is important in neural, kidney and vascular development. It may also be involved in regulating the outgrowth and shape of epithelial cells during lung branching morphogenesis.


Pssm-ID: 239633  Cd Length: 111  Bit Score: 38.31  E-value: 1.75e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6754904  457 KKFCRKDYAVQVAVGARG-EARGSWTRFPVAVLAVFRSGEERARRGSSALWVPT-LDAACGCPRLLPGRRYLL 527
Cdd:cd03578   2 KVFCGMKYAYVIKIKVLSaHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESwTSRGCTCPILNPGLEYLV 74
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
335-362 2.90e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 35.75  E-value: 2.90e-03
                           10        20
                   ....*....|....*....|....*...
gi 6754904     335 GGVCLnCRHNTAGRHCHYCREGFYRDPG 362
Cdd:smart00180  17 TGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
 
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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