NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|578830095|ref|XP_006721658|]
View 

netrin-1 isoform X1 [Homo sapiens]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 11255201)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 46-283 8.19e-131

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: 382.86  E-value: 8.19e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095    46 GHPRRCIPDFVNAAFGKDVRVSSTCGRP-PARYCVVSERGEERlRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSEN 124
Cdd:smart00136   2 GRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQG-KKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095   125 YLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPeSMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCT 204
Cdd:smart00136  81 LSNGPQNVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKGNEDEVICT 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578830095   205 DSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGG 283
Cdd:smart00136 160 SEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYAISDIAVGG 238
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 487-601 1.61e-65

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: 209.80  E-value: 1.61e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095 487 MKKYCKKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPD 566
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSRETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 578830095 567 QSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKC 601
Cdd:cd03579   81 RGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 404-441 8.83e-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: 60.06  E-value: 8.83e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 578830095  404 CDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGY 441
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 284-329 1.34e-09

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: 53.90  E-value: 1.34e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 578830095 284 RCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQR 329
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 341-401 2.51e-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: 41.96  E-value: 2.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578830095  341 CNCNLHA---RRCRFnmelyklsgrkSGGVCLnCRHNTAGRHCHYCKEGYYRDmgkPITHRKAC 401
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
 
Name Accession Description Interval E-value
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 46-283 8.19e-131

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: 382.86  E-value: 8.19e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095    46 GHPRRCIPDFVNAAFGKDVRVSSTCGRP-PARYCVVSERGEERlRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSEN 124
Cdd:smart00136   2 GRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQG-KKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095   125 YLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPeSMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCT 204
Cdd:smart00136  81 LSNGPQNVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKGNEDEVICT 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578830095   205 DSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGG 283
Cdd:smart00136 160 SEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYAISDIAVGG 238
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
51-283 4.27e-126

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 370.37  E-value: 4.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095   51 CIPDFVNAAFGKDVRVSSTCG-RPPARYCVVSERGEERlrSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFP 129
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEGGK--KCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVIQY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095  130 HNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKqNEQEAVCTDSHTD 209
Cdd:pfam00055  79 ENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGI-KDDEVICTSEYSD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578830095  210 MRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARdSYFYAVSDLQVGG 283
Cdd:pfam00055 158 ISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISVGG 230
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 487-601 1.61e-65

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: 209.80  E-value: 1.61e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095 487 MKKYCKKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPD 566
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSRETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 578830095 567 QSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKC 601
Cdd:cd03579   81 RGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 488-594 2.56e-35

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: 128.61  E-value: 2.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095  488 KKYCK-KDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDiaCKCPKIKPLKKYLLLGNAEDSPD 566
Cdd:pfam01759   1 KKACKgSDYVYKVKVLSVEEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD--CRCPQLRLGKEYLIMGKVGDLEG 78

                          90       100
                  ....*....|....*....|....*...
gi 578830095  567 QSGIVADKSSLVIQWRDTWARRLRKFQQ 594
Cdd:pfam01759  79 RGRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
487-594 3.39e-32

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 120.16  E-value: 3.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095   487 MKKYCKK--DYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKI-KPLKKYLLLGNAED 563
Cdd:smart00643   1 LEKACKSdvDYVYKVKVLSVEEEGGFDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCPLLlKLGKSYLIMGKSGD 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 578830095   564 ---SPDQSGIVADKSSLVIQWRDTWARRLRKFQQ 594
Cdd:smart00643  81 lwdAKGRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 404-441 8.83e-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: 60.06  E-value: 8.83e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 578830095  404 CDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGY 441
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 403-451 9.39e-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: 60.06  E-value: 9.39e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578830095 403 ACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPC 451
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
404-441 1.52e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.25  E-value: 1.52e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 578830095   404 CDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGY 441
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 284-329 1.34e-09

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: 53.90  E-value: 1.34e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 578830095 284 RCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQR 329
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 285-326 2.37e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 47.35  E-value: 2.37e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 578830095  285 CKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRP 326
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 341-401 2.51e-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: 41.96  E-value: 2.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578830095  341 CNCNLHA---RRCRFnmelyklsgrkSGGVCLnCRHNTAGRHCHYCKEGYYRDmgkPITHRKAC 401
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
285-328 2.63e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 41.53  E-value: 2.63e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 578830095   285 CKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQ 328
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 340-390 1.48e-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: 1.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578830095 340 ACNCNLHA---RRCRFNmelyklsgrksGGVCLnCRHNTAGRHCHYCKEGYYRD 390
Cdd:cd00055    1 PCDCNGHGslsGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
365-392 1.84e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 36.52  E-value: 1.84e-03
                           10        20
                   ....*....|....*....|....*...
gi 578830095   365 GGVCLnCRHNTAGRHCHYCKEGYYRDMG 392
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 ...
 46-283 8.19e-131

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: 382.86  E-value: 8.19e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095    46 GHPRRCIPDFVNAAFGKDVRVSSTCGRP-PARYCVVSERGEERlRSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSEN 124
Cdd:smart00136   2 GRPRSCYPPFVNLAFGREVTATSTCGEPgPERYCKLVGHTEQG-KKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSEP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095   125 YLQFPHNVTLTLSLGKKFEVTYVSLQFCSPRPeSMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKQNEQEAVCT 204
Cdd:smart00136  81 LSNGPQNVNLTLDLGKEFHVTYVILKFCSPRP-SLWILERSDFGKTWQPWQYFSSDCRRTFGRPPRGPITKGNEDEVICT 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578830095   205 DSHTDMRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARDSYFYAVSDLQVGG 283
Cdd:smart00136 160 SEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYAISDIAVGG 238
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
51-283 4.27e-126

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 370.37  E-value: 4.27e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095   51 CIPDFVNAAFGKDVRVSSTCG-RPPARYCVVSERGEERlrSCHLCNASDPKKAHPPAFLTDLNNPHNLTCWQSENYLQFP 129
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGlNGPERYCILSGLEGGK--KCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVIQY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095  130 HNVTLTLSLGKKFEVTYVSLQFCSPRPESMAIYKSMDYGRTWVPFQFYSTQCRKMYNRPHRAPITKqNEQEAVCTDSHTD 209
Cdd:pfam00055  79 ENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGI-KDDEVICTSEYSD 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578830095  210 MRPLSGGLIAFSTLDGRPSAHDFDNSPVLQDWVTATDIRVAFSRLHTFGDENEDDSELARdSYFYAVSDLQVGG 283
Cdd:pfam00055 158 ISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLR-KYYYAISDISVGG 230
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 487-601 1.61e-65

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: 209.80  E-value: 1.61e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095 487 MKKYCKKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSPD 566
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSRETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGKDEDSPE 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 578830095 567 QSGIVADKSSLVIQWRDTWARRLRKFQQREKKGKC 601
Cdd:cd03579   81 RGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 488-594 2.56e-35

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: 128.61  E-value: 2.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095  488 KKYCK-KDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDiaCKCPKIKPLKKYLLLGNAEDSPD 566
Cdd:pfam01759   1 KKACKgSDYVYKVKVLSVEEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD--CRCPQLRLGKEYLIMGKVGDLEG 78

                          90       100
                  ....*....|....*....|....*...
gi 578830095  567 QSGIVADKSSLVIQWRDTWARRLRKFQQ 594
Cdd:pfam01759  79 RGRYVLDKNSWVEPWPTKWECKLRELQK 106
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 488-591 1.13e-34

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: 126.82  E-value: 1.13e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095 488 KKYCKKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKIKPLKKYLLLGNAEDSpdQ 567
Cdd:cd03523    1 KAFCKSDYVVRAKIKEIKEENDDVKYEVKIIKIYKTGKAKADKADLRFYYTAPACCPCHPILNPGREYLIMGKEEDS--Q 78

                         90       100
                 ....*....|....*....|....*..
gi 578830095 568 SGIVADKSSLVIQWRD---TWARRLRK 591
Cdd:cd03523   79 GGLVLDPLSFVEPWSPlslRQDRRLRE 105
C345C smart00643
Netrin C-terminal Domain;
487-594 3.39e-32

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 120.16  E-value: 3.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095   487 MKKYCKK--DYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRSRDIACKCPKI-KPLKKYLLLGNAED 563
Cdd:smart00643   1 LEKACKSdvDYVYKVKVLSVEEEGGFDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCPLLlKLGKSYLIMGKSGD 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 578830095   564 ---SPDQSGIVADKSSLVIQWRDTWARRLRKFQQ 594
Cdd:smart00643  81 lwdAKGRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 404-441 8.83e-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: 60.06  E-value: 8.83e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 578830095  404 CDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGY 441
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 403-451 9.39e-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: 60.06  E-value: 9.39e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 578830095 403 ACDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGYQQSRSPIAPC 451
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
404-441 1.52e-11

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 59.25  E-value: 1.52e-11
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 578830095   404 CDCHPVGAAGKTCNQTTGQCPCKDGVTGITCNRCAKGY 441
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 284-329 1.34e-09

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: 53.90  E-value: 1.34e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 578830095 284 RCKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQR 329
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 285-326 2.37e-07

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 47.35  E-value: 2.37e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 578830095  285 CKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRP 326
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP 42
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 488-596 1.33e-06

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: 47.17  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095 488 KKYC--KKDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQSLWIRS-RDIACKCPKIKPLKKYLLLGNAEds 564
Cdd:cd03578    2 KVFCgmKYAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESwTSRGCTCPILNPGLEYLVAGHED-- 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 578830095 565 PDQSGIVADKSSLVIQWRDTWARRLRKFQQRE 596
Cdd:cd03578   80 VRTGRLIVNMKSFVQHWKPSLGRKVMEILKRE 111
NTR_complement_C345C cd03574
NTR/C345C domain; The NTR domains that are found in the C-termini of complement C3, C4 and C5, ...
 487-600 1.30e-05

NTR/C345C domain; The NTR domains that are found in the C-termini of complement C3, C4 and C5, are also called C345C domains. In C5, the domain interacts with various partners during the formation of the membrane attack complex, a fundamental process in the mammalian defense against infection. It's role in component C3 and C4 is not well understood.


Pssm-ID: 239629  Cd Length: 147  Bit Score: 45.46  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095 487 MKKYCK-KDYAVQIHILKADKAGDWWKFTVNIISVYKQGTSRIRRGDQ--SLWIRsrdIACKCPK-IKPLKKYLLLGN-- 560
Cdd:cd03574   16 LDKACTsVDYVYKVKVTSVEEEAGFRIYKARVTEVIKSGSDDVQNGNArrTFIIR---ESCDCPLrLKEGRHYLIMGSdg 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 578830095 561 ----AEDSPDQSGIVADKSSLVIQW-RDTWARRLRKFQQREKKGK 600
Cdd:cd03574   93 afydDRNGEDRYQYVLDSNTWVEEWpTDSKCRNERQQAACDKLKK 137
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 341-401 2.51e-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: 41.96  E-value: 2.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578830095  341 CNCNLHA---RRCRFnmelyklsgrkSGGVCLnCRHNTAGRHCHYCKEGYYRDmgkPITHRKAC 401
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
285-328 2.63e-05

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 41.53  E-value: 2.63e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 578830095   285 CKCNGHAARCVRDRDDSLVCDCRHNTAGPECDRCKPFHYDRPWQ 328
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 340-390 1.48e-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: 1.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 578830095 340 ACNCNLHA---RRCRFNmelyklsgrksGGVCLnCRHNTAGRHCHYCKEGYYRD 390
Cdd:cd00055    1 PCDCNGHGslsGQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
 515-595 1.15e-03

NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins similar to human Sfrp3 and Sfrp4. Sfrps are soluble proteins containing an NTR domain C-terminal to a cysteine-rich Frizzled domain. They show diverse functions and are thought to work in Wnt signaling indirectly, as modulators or antagonists by binding Wnt ligands, and directly, via the Wnt receptor, Frizzled. They participate in regulating the patterning along the anteroposterior axis in vertebrates. Human Sfrp3 may suppress the growth and invasiveness of androgen-independent prostate cancer cells.


Pssm-ID: 239636  Cd Length: 111  Bit Score: 38.99  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578830095 515 VNIISVYKQGTSRIRRGDQSLWIRSrdiACKCPKIKPLKKYLLLGnAEDSpDQSGIVADKSSLVIQWRDTWARRLRKFQQ 594
Cdd:cd03581   30 VEVKEILKSSLVNIPRDTVTLYTNS---GCLCPPLTPNEEYIIMG-YEDE-ERSRLLLVEGSLAEKWKDRLGKKVKRWDQ 104


                 .
gi 578830095 595 R 595
Cdd:cd03581  105 K 105
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
365-392 1.84e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 36.52  E-value: 1.84e-03
                           10        20
                   ....*....|....*....|....*...
gi 578830095   365 GGVCLnCRHNTAGRHCHYCKEGYYRDMG 392
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH