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Conserved domains on  [gi|388453233|ref|NP_001252984|]
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netrin-4 precursor [Macaca mulatta]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 11080841)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
34-260 3.85e-106

Laminin N-terminal (Domain VI);


:

Pssm-ID: 459653  Cd Length: 230  Bit Score: 319.91  E-value: 3.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   34 CNPRMGNLALGRKLWADTTCGQNATELYCFYSENTDltcrQPKCDKCNAAHPHLAHLPSAMADSSFRFPRTWWQSAEDV- 112
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEG----GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233  113 --HREKIQLDLEAEFYFTHLIMVFKSPRPAAMVLDRSQDFGRTWKPYKYFATNCSATFGLEDD----VGKKGAICTSKYS 186
Cdd:pfam00055  77 qyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGpsrgIKDDEVICTSEYS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388453233  187 SPFPCTGGEVIFKAL-SPPYDTENPYSAKVQEQLKITNLRVQLLKRQSCPCQRNDlNEEPQHFTHYAIYDFIVKG 260
Cdd:pfam00055 157 DISPLTGGEVIFSTLeGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLD-DPSVLRKYYYAISDISVGG 230
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 516-626 6.57e-72

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: 227.06  E-value: 6.57e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 516 AKAFCGMKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPESWTDRGCTCPILNPGLEYLVAGHEDV 595
Cdd:cd03578    1 AKVFCGMKYAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESWTSRGCTCPILNPGLEYLVAGHEDV 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 388453233 596 RTGKLIVNMKSFVQHWKPSLGRKVMDILKRK 626
Cdd:cd03578   81 RTGRLIVNMKSFVQHWKPSLGRKVMEILKRE 111
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
395-446 2.18e-10

Laminin-type epidermal growth factor-like domai;


:

Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.17  E-value: 2.18e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 388453233   395 CSCHPVGSAVlpansvTFCDPSNGDCPCKPGVAGRHCDRCMVGYWGFGDYGC 446
Cdd:smart00180   1 CDCDPGGSAS------GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 332-392 7.61e-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: 46.19  E-value: 7.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388453233  332 CKCNGHA---DTCHFdvnvweasgnrSGGVCDdCQHNTEGQHCQRCKPGFYRDlrrPFSAPDAC 392
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 261-320 1.04e-05

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: 43.11  E-value: 1.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 261 SCFCNGHADQcipvhgfrpvkaPGTFHMVHGKCMCKHNTAGSHCQHCAPLYNDRPWEAAD 320
Cdd:cd00055    1 PCDCNGHGSL------------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
34-260 3.85e-106

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 319.91  E-value: 3.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   34 CNPRMGNLALGRKLWADTTCGQNATELYCFYSENTDltcrQPKCDKCNAAHPHLAHLPSAMADSSFRFPRTWWQSAEDV- 112
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEG----GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233  113 --HREKIQLDLEAEFYFTHLIMVFKSPRPAAMVLDRSQDFGRTWKPYKYFATNCSATFGLEDD----VGKKGAICTSKYS 186
Cdd:pfam00055  77 qyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGpsrgIKDDEVICTSEYS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388453233  187 SPFPCTGGEVIFKAL-SPPYDTENPYSAKVQEQLKITNLRVQLLKRQSCPCQRNDlNEEPQHFTHYAIYDFIVKG 260
Cdd:pfam00055 157 DISPLTGGEVIFSTLeGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLD-DPSVLRKYYYAISDISVGG 230
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 516-626 6.57e-72

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: 227.06  E-value: 6.57e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 516 AKAFCGMKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPESWTDRGCTCPILNPGLEYLVAGHEDV 595
Cdd:cd03578    1 AKVFCGMKYAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESWTSRGCTCPILNPGLEYLVAGHEDV 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 388453233 596 RTGKLIVNMKSFVQHWKPSLGRKVMDILKRK 626
Cdd:cd03578   81 RTGRLIVNMKSFVQHWKPSLGRKVMEILKRE 111
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 28-260 1.43e-62

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: 207.21  E-value: 1.43e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233    28 SRCEKACNPRMGNLALGRKLWADTTCGQNATELYCfysENTDLTCRQPKCDKCNAAHPHLAHLPSAMADSSFRFPRTWWQ 107
Cdd:smart00136   1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYC---KLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQ 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   108 S---AEDVHREKIQLDLEAEFYFTHLIMVFKSPRPAAMVLDRSqDFGRTWKPYKYFATNCSATFGLEDDVG-KKG----A 179
Cdd:smart00136  78 SeplSNGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPiTKGnedeV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   180 ICTSKYSSPFPCTGGEVIFKALSP-PYDTENPYSAKVQEQLKITNLRVQLLKRQSCPCQRNDLNEEPQHFTHYAIYDFIV 258
Cdd:smart00136 157 ICTSEYSDIVPLEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYAISDIAV 236


                   ..
gi 388453233   259 KG 260
Cdd:smart00136 237 GG 238
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 517-624 1.04e-25

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: 101.65  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233  517 KAFCGmKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPESWTdrgCTCPILNPGLEYLVAGHEDVR 596
Cdd:pfam01759   1 KKACK-GSDYVYKVKVLSVEEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD---CRCPQLRLGKEYLIMGKVGDL 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 388453233  597 TG--KLIVNMKSFVQHWKPSLGRKVMDILK 624
Cdd:pfam01759  77 EGrgRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
517-624 7.30e-20

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 85.11  E-value: 7.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   517 KAFCGMKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPeSWTDRGCTCP-ILNPGLEYLVAG---- 591
Cdd:smart00643   2 EKACKSDVDYVYKVKVLSVEEEGGFDKYTVKILEVIKSGTDELVRGKNKLRV-FISRASCRCPlLLKLGKSYLIMGksgd 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 388453233   592 -HEDVRTGKLIVNMKSFVQHWKPSLGRKVMDILK 624
Cdd:smart00643  81 lWDAKGRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
395-446 2.18e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.17  E-value: 2.18e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 388453233   395 CSCHPVGSAVlpansvTFCDPSNGDCPCKPGVAGRHCDRCMVGYWGFGDYGC 446
Cdd:smart00180   1 CDCDPGGSAS------GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 395-449 2.68e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.82  E-value: 2.68e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 388453233  395 CSCHPVGSavlpanSVTFCDPSNGDCPCKPGVAGRHCDRCMVGYWGFGDYGCRPC 449
Cdd:pfam00053   1 CDCNPHGS------LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 394-445 3.75e-10

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: 55.44  E-value: 3.75e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 388453233 394 PCSCHPVGSavlpanSVTFCDPSNGDCPCKPGVAGRHCDRCMVGYWGFGDYG 445
Cdd:cd00055    1 PCDCNGHGS------LSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 332-392 7.61e-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: 46.19  E-value: 7.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388453233  332 CKCNGHA---DTCHFdvnvweasgnrSGGVCDdCQHNTEGQHCQRCKPGFYRDlrrPFSAPDAC 392
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 332-381 6.12e-06

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: 43.50  E-value: 6.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 388453233 332 CKCNGHAD---TCHFDvnvweasgnrsGGVCDdCQHNTEGQHCQRCKPGFYRD 381
Cdd:cd00055    2 CDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 261-320 1.04e-05

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: 43.11  E-value: 1.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 261 SCFCNGHADQcipvhgfrpvkaPGTFHMVHGKCMCKHNTAGSHCQHCAPLYNDRPWEAAD 320
Cdd:cd00055    1 PCDCNGHGSL------------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
332-381 1.59e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 388453233   332 CKCN--GHAD-TCHFDvnvweasgnrsGGVCDdCQHNTEGQHCQRCKPGFYRD 381
Cdd:smart00180   1 CDCDpgGSASgTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGD 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 262-321 9.19e-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: 37.33  E-value: 9.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233  262 CFCNGHADqcipvhgfrpvkAPGTFHMVHGKCMCKHNTAGSHCQHCAPLYNDRPWEAADG 321
Cdd:pfam00053   1 CDCNPHGS------------LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
287-317 2.55e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 36.14  E-value: 2.55e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 388453233   287 HMVHGKCMCKHNTAGSHCQHCAPLYNDRPWE 317
Cdd:smart00180  14 DPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
34-260 3.85e-106

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 319.91  E-value: 3.85e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   34 CNPRMGNLALGRKLWADTTCGQNATELYCFYSENTDltcrQPKCDKCNAAHPHLAHLPSAMADSSFRFPRTWWQSAEDV- 112
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEG----GKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233  113 --HREKIQLDLEAEFYFTHLIMVFKSPRPAAMVLDRSQDFGRTWKPYKYFATNCSATFGLEDD----VGKKGAICTSKYS 186
Cdd:pfam00055  77 qyENVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGpsrgIKDDEVICTSEYS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 388453233  187 SPFPCTGGEVIFKAL-SPPYDTENPYSAKVQEQLKITNLRVQLLKRQSCPCQRNDlNEEPQHFTHYAIYDFIVKG 260
Cdd:pfam00055 157 DISPLTGGEVIFSTLeGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLD-DPSVLRKYYYAISDISVGG 230
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 516-626 6.57e-72

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: 227.06  E-value: 6.57e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 516 AKAFCGMKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPESWTDRGCTCPILNPGLEYLVAGHEDV 595
Cdd:cd03578    1 AKVFCGMKYAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESWTSRGCTCPILNPGLEYLVAGHEDV 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 388453233 596 RTGKLIVNMKSFVQHWKPSLGRKVMDILKRK 626
Cdd:cd03578   81 RTGRLIVNMKSFVQHWKPSLGRKVMEILKRE 111
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 28-260 1.43e-62

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: 207.21  E-value: 1.43e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233    28 SRCEKACNPRMGNLALGRKLWADTTCGQNATELYCfysENTDLTCRQPKCDKCNAAHPHLAHLPSAMADSSFRFPRTWWQ 107
Cdd:smart00136   1 AGRPRSCYPPFVNLAFGREVTATSTCGEPGPERYC---KLVGHTEQGKKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQ 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   108 S---AEDVHREKIQLDLEAEFYFTHLIMVFKSPRPAAMVLDRSqDFGRTWKPYKYFATNCSATFGLEDDVG-KKG----A 179
Cdd:smart00136  78 SeplSNGPQNVNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGPiTKGnedeV 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   180 ICTSKYSSPFPCTGGEVIFKALSP-PYDTENPYSAKVQEQLKITNLRVQLLKRQSCPCQRNDLNEEPQHFTHYAIYDFIV 258
Cdd:smart00136 157 ICTSEYSDIVPLEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDRPEVTRRYYYAISDIAV 236


                   ..
gi 388453233   259 KG 260
Cdd:smart00136 237 GG 238
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 517-626 4.76e-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: 125.27  E-value: 4.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 517 KAFCGMkySYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLK-IFRGKRTLYPESWTDrgCTCPILNPGLEYLVAGHEDV 595
Cdd:cd03523    1 KAFCKS--DYVVRAKIKEIKEENDDVKYEVKIIKIYKTGKAKaDKADLRFYYTAPACC--PCHPILNPGREYLIMGKEED 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 388453233 596 RTGKLIVNMKSFVQHWKPSLgrKVMDILKRK 626
Cdd:cd03523   77 SQGGLVLDPLSFVEPWSPLS--LRQDRRLRE 105
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 517-624 1.04e-25

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: 101.65  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233  517 KAFCGmKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPESWTdrgCTCPILNPGLEYLVAGHEDVR 596
Cdd:pfam01759   1 KKACK-GSDYVYKVKVLSVEEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD---CRCPQLRLGKEYLIMGKVGDL 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 388453233  597 TG--KLIVNMKSFVQHWKPSLGRKVMDILK 624
Cdd:pfam01759  77 EGrgRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
517-624 7.30e-20

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 85.11  E-value: 7.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233   517 KAFCGMKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYPeSWTDRGCTCP-ILNPGLEYLVAG---- 591
Cdd:smart00643   2 EKACKSDVDYVYKVKVLSVEEEGGFDKYTVKILEVIKSGTDELVRGKNKLRV-FISRASCRCPlLLKLGKSYLIMGksgd 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 388453233   592 -HEDVRTGKLIVNMKSFVQHWKPSLGRKVMDILK 624
Cdd:smart00643  81 lWDAKGRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
 524-619 3.78e-16

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: 74.43  E-value: 3.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 524 YSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLypesWTDRGCTCPILNPGLEYLVAGHEDVRTGKLIVN 603
Cdd:cd03581    8 YNYVIRAKVKEVKRGCHEVTAVVEVKEILKSSLVNIPRDTVTL----YTNSGCLCPPLTPNEEYIIMGYEDEERSRLLLV 83

                         90
                 ....*....|....*.
gi 388453233 604 MKSFVQHWKPSLGRKV 619
Cdd:cd03581   84 EGSLAEKWKDRLGKKV 99
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
395-446 2.18e-10

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 56.17  E-value: 2.18e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 388453233   395 CSCHPVGSAVlpansvTFCDPSNGDCPCKPGVAGRHCDRCMVGYWGFGDYGC 446
Cdd:smart00180   1 CDCDPGGSAS------GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 395-449 2.68e-10

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 55.82  E-value: 2.68e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 388453233  395 CSCHPVGSavlpanSVTFCDPSNGDCPCKPGVAGRHCDRCMVGYWGFGDYGCRPC 449
Cdd:pfam00053   1 CDCNPHGS------LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 394-445 3.75e-10

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: 55.44  E-value: 3.75e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 388453233 394 PCSCHPVGSavlpanSVTFCDPSNGDCPCKPGVAGRHCDRCMVGYWGFGDYG 445
Cdd:cd00055    1 PCDCNGHGS------LSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 517-619 4.05e-08

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: 51.86  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 517 KAFCgmKYSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGKRTLYpESWTDRGCTCPILNPGLEYLVAG--HED 594
Cdd:cd03579    2 KKYC--KKDYAVQAQVLSRETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLW-VPRKDLACKCPKLKVGKSYLLLGkdEDS 78

                         90       100
                 ....*....|....*....|....*
gi 388453233 595 VRTGKLIVNMKSFVQHWKPSLGRKV 619
Cdd:cd03579   79 PERGGLILDKRSLVIEWRDEWARRL 103
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 332-392 7.61e-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: 46.19  E-value: 7.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 388453233  332 CKCNGHA---DTCHFdvnvweasgnrSGGVCDdCQHNTEGQHCQRCKPGFYRDlrrPFSAPDAC 392
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 332-381 6.12e-06

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: 43.50  E-value: 6.12e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 388453233 332 CKCNGHAD---TCHFDvnvweasgnrsGGVCDdCQHNTEGQHCQRCKPGFYRD 381
Cdd:cd00055    2 CDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 261-320 1.04e-05

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: 43.11  E-value: 1.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 261 SCFCNGHADQcipvhgfrpvkaPGTFHMVHGKCMCKHNTAGSHCQHCAPLYNDRPWEAAD 320
Cdd:cd00055    1 PCDCNGHGSL------------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
332-381 1.59e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 1.59e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 388453233   332 CKCN--GHAD-TCHFDvnvweasgnrsGGVCDdCQHNTEGQHCQRCKPGFYRD 381
Cdd:smart00180   1 CDCDpgGSASgTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGD 41
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 262-321 9.19e-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: 37.33  E-value: 9.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233  262 CFCNGHADqcipvhgfrpvkAPGTFHMVHGKCMCKHNTAGSHCQHCAPLYNDRPWEAADG 321
Cdd:pfam00053   1 CDCNPHGS------------LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
287-317 2.55e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 36.14  E-value: 2.55e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 388453233   287 HMVHGKCMCKHNTAGSHCQHCAPLYNDRPWE 317
Cdd:smart00180  14 DPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
NTR_complement_C345C cd03574
NTR/C345C domain; The NTR domains that are found in the C-termini of complement C3, C4 and C5, ...
 524-611 4.47e-03

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: 38.14  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388453233 524 YSYVLKIKILSAHDKGTHVEVNVKIKKVLKSTKLKIFRGK--RTLypesWTDRGCTCPI-LNPGLEYLVAG----HEDVR 596
Cdd:cd03574   23 VDYVYKVKVTSVEEEAGFRIYKARVTEVIKSGSDDVQNGNarRTF----IIRESCDCPLrLKEGRHYLIMGsdgaFYDDR 98

                         90
                 ....*....|....*....
gi 388453233 597 TGKL----IVNMKSFVQHW 611
Cdd:cd03574   99 NGEDryqyVLDSNTWVEEW 117
 
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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