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Conserved domains on  [gi|2024345906|ref|XP_015139402|]
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netrin-4 isoform X2 [Gallus gallus]

Protein Classification

calcium-binding EGF-like domain-containing protein( domain architecture ID 11080506)

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);
34-258 1.08e-90

Laminin N-terminal (Domain VI);


:

Pssm-ID: 459653  Cd Length: 230  Bit Score: 280.24  E-value: 1.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  34 CNPRLGNLAHGRTLRTETACGSHAAEPFCAYAEDAtlrcKPPTCGHCSGAHAGLAHPPAAMADSPFRLPRTWWQAAGDAP 113
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLE----GGKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 114 Q---ETIQLDLEATFYFTHLILVFKSPRPAAMVLERSQDFGKTWQAYKYFATNCSATFGLEDDVVRR----GAPCTSRYS 186
Cdd:pfam00055  77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGikddEVICTSEYS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024345906 187 SPFPCTGGEVIYRAL-SPPHAAKDPYSAEAQAQLKVTNLRVRLLERQSCPCHPLEPPALPAPY-YAVYDFIVKG 258
Cdd:pfam00055 157 DISPLTGGEVIFSTLeGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYyYAISDISVGG 230
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 514-624 1.26e-71

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: 226.29  E-value: 1.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 514 SKVFCGMKYTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLYPESWTNRGCTCPILNPGLEYLVAGHEDV 593
Cdd:cd03578     1 AKVFCGMKYAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESWTSRGCTCPILNPGLEYLVAGHEDV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2024345906 594 RTGRLIVNMKSFVHQWKSALGRKVLEILKRD 624
Cdd:cd03578    81 RTGRLIVNMKSFVQHWKPSLGRKVMEILKRE 111
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 393-447 3.55e-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: 61.22  E-value: 3.55e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024345906 393 CSCHPLGSaalplgPRTFCDPSTGDCPCKPGVAGPRCDRCLPGYWGFGTSGCRPC 447
Cdd:pfam00053   1 CDCNPHGS------LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 330-390 1.45e-06

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


:

Pssm-ID: 395007  Cd Length: 49  Bit Score: 45.42  E-value: 1.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024345906 330 CKCNGHA---DTCHFdmdawlasgnrSGGVCDnCQHNTEGQHCQRCKPGFYRDlrkPFSAPDAC 390
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 259-318 7.80e-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: 7.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 259 SCFCNGHADHcvpvrgfrpvraAGAFHVVHGKCMCKHNTAGPHCQHCAPLYNDRPWQAAD 318
Cdd:cd00055     1 PCDCNGHGSL------------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
34-258 1.08e-90

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 280.24  E-value: 1.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  34 CNPRLGNLAHGRTLRTETACGSHAAEPFCAYAEDAtlrcKPPTCGHCSGAHAGLAHPPAAMADSPFRLPRTWWQAAGDAP 113
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLE----GGKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 114 Q---ETIQLDLEATFYFTHLILVFKSPRPAAMVLERSQDFGKTWQAYKYFATNCSATFGLEDDVVRR----GAPCTSRYS 186
Cdd:pfam00055  77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGikddEVICTSEYS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024345906 187 SPFPCTGGEVIYRAL-SPPHAAKDPYSAEAQAQLKVTNLRVRLLERQSCPCHPLEPPALPAPY-YAVYDFIVKG 258
Cdd:pfam00055 157 DISPLTGGEVIFSTLeGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYyYAISDISVGG 230
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 514-624 1.26e-71

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: 226.29  E-value: 1.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 514 SKVFCGMKYTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLYPESWTNRGCTCPILNPGLEYLVAGHEDV 593
Cdd:cd03578     1 AKVFCGMKYAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESWTSRGCTCPILNPGLEYLVAGHEDV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2024345906 594 RTGRLIVNMKSFVHQWKSALGRKVLEILKRD 624
Cdd:cd03578    81 RTGRLIVNMKSFVQHWKPSLGRKVMEILKRE 111
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 30-258 7.52e-50

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: 173.32  E-value: 7.52e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906   30 CEKACNPRLGNLAHGRTLRTETACGSHAAEPFCAYAEDATLRckpPTCGHCSGAHAGLAHPPAAMADSPFRLPRTWWQAA 109
Cdd:smart00136   3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHTEQG---KKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  110 GD--APQE-TIQLDLEATFYFTHLILVFKSPRPAAMVLERSqDFGKTWQAYKYFATNCSATFGLEDDV-VRRG----APC 181
Cdd:smart00136  80 PLsnGPQNvNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpITKGnedeVIC 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  182 TSRYSSPFPCTGGEVIYRALSP-PHAAKDPYSAEAQAQLKVTNLRVRLLERQSCPCH--PLEPPALPAPYYAVYDFIVKG 258
Cdd:smart00136 159 TSEYSDIVPLEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDElmDDRPEVTRRYYYAISDIAVGG 238
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 517-622 7.62e-26

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: 102.04  E-value: 7.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 517 FCGmKYTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLYPESWTnrgCTCPILNPGLEYLVAGHEDVRTG 596
Cdd:pfam01759   3 ACK-GSDYVYKVKVLSVEEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD---CRCPQLRLGKEYLIMGKVGDLEG 78

                          90       100
                  ....*....|....*....|....*...
gi 2024345906 597 --RLIVNMKSFVHQWKSALGRKVLEILK 622
Cdd:pfam01759  79 rgRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
517-622 9.46e-21

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 87.81  E-value: 9.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  517 FCGMKYTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLYPESWTNRgCTCP-ILNPGLEYLVAG-----H 590
Cdd:smart00643   4 ACKSDVDYVYKVKVLSVEEEGGFDKYTVKILEVIKSGTDELVRGKNKLRVFISRAS-CRCPlLLKLGKSYLIMGksgdlW 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2024345906  591 EDVRTGRLIVNMKSFVHQWKSALGRKVLEILK 622
Cdd:smart00643  83 DAKGRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 393-447 3.55e-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: 61.22  E-value: 3.55e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024345906 393 CSCHPLGSaalplgPRTFCDPSTGDCPCKPGVAGPRCDRCLPGYWGFGTSGCRPC 447
Cdd:pfam00053   1 CDCNPHGS------LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
393-444 4.65e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 4.65e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024345906  393 CSCHPLGSAAlplgprTFCDPSTGDCPCKPGVAGPRCDRCLPGYWGFGTSGC 444
Cdd:smart00180   1 CDCDPGGSAS------GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 392-443 1.68e-11

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: 59.29  E-value: 1.68e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024345906 392 PCSCHPLGSaalplgPRTFCDPSTGDCPCKPGVAGPRCDRCLPGYWGFGTSG 443
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.
 330-390 1.45e-06

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 45.42  E-value: 1.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024345906 330 CKCNGHA---DTCHFdmdawlasgnrSGGVCDnCQHNTEGQHCQRCKPGFYRDlrkPFSAPDAC 390
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 259-318 7.80e-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: 7.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 259 SCFCNGHADHcvpvrgfrpvraAGAFHVVHGKCMCKHNTAGPHCQHCAPLYNDRPWQAAD 318
Cdd:cd00055     1 PCDCNGHGSL------------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 329-379 9.78e-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: 43.11  E-value: 9.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024345906 329 SCKCNGHAD---TCHFDmdawlasgnrsGGVCDnCQHNTEGQHCQRCKPGFYRD 379
Cdd:cd00055     1 PCDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
330-379 2.28e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.22  E-value: 2.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024345906  330 CKCN--GHAD-TCHFDmdawlasgnrsGGVCDnCQHNTEGQHCQRCKPGFYRD 379
Cdd:smart00180   1 CDCDpgGSASgTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGD 41
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
285-315 9.22e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 9.22e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024345906  285 HVVHGKCMCKHNTAGPHCQHCAPLYNDRPWQ 315
Cdd:smart00180  14 DPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 260-319 1.75e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.56  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 260 CFCNGHADHcvpvrgfrpvraAGAFHVVHGKCMCKHNTAGPHCQHCAPLYNDRPWQAADG 319
Cdd:pfam00053   1 CDCNPHGSL------------SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
 
Name Accession Description Interval E-value
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
34-258 1.08e-90

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 280.24  E-value: 1.08e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  34 CNPRLGNLAHGRTLRTETACGSHAAEPFCAYAEDAtlrcKPPTCGHCSGAHAGLAHPPAAMADSPFRLPRTWWQAAGDAP 113
Cdd:pfam00055   1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLE----GGKKCFICDSRDPHNSHPPSNLTDSNNGTNETWWQSETGVI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 114 Q---ETIQLDLEATFYFTHLILVFKSPRPAAMVLERSQDFGKTWQAYKYFATNCSATFGLEDDVVRR----GAPCTSRYS 186
Cdd:pfam00055  77 QyenVNLTLDLGKEFHFTYLILKFKSPRPAAMVLERSTDFGKTWQPYQYFASDCRRTFGRPSGPSRGikddEVICTSEYS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024345906 187 SPFPCTGGEVIYRAL-SPPHAAKDPYSAEAQAQLKVTNLRVRLLERQSCPCHPLEPPALPAPY-YAVYDFIVKG 258
Cdd:pfam00055 157 DISPLTGGEVIFSTLeGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDELLDDPSVLRKYyYAISDISVGG 230
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 514-624 1.26e-71

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: 226.29  E-value: 1.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 514 SKVFCGMKYTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLYPESWTNRGCTCPILNPGLEYLVAGHEDV 593
Cdd:cd03578     1 AKVFCGMKYAYVIKIKVLSAHDKGTHAEVNVKIKKVLKSTKLKLSRGKRTLYPESWTSRGCTCPILNPGLEYLVAGHEDV 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2024345906 594 RTGRLIVNMKSFVHQWKSALGRKVLEILKRD 624
Cdd:cd03578    81 RTGRLIVNMKSFVQHWKPSLGRKVMEILKRE 111
LamNT smart00136
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ...
 30-258 7.52e-50

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: 173.32  E-value: 7.52e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906   30 CEKACNPRLGNLAHGRTLRTETACGSHAAEPFCAYAEDATLRckpPTCGHCSGAHAGLAHPPAAMADSPFRLPRTWWQAA 109
Cdd:smart00136   3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLVGHTEQG---KKCDYCDARNPRRSHPAENLTDGNNPNNPTWWQSE 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  110 GD--APQE-TIQLDLEATFYFTHLILVFKSPRPAAMVLERSqDFGKTWQAYKYFATNCSATFGLEDDV-VRRG----APC 181
Cdd:smart00136  80 PLsnGPQNvNLTLDLGKEFHVTYVILKFCSPRPSLWILERS-DFGKTWQPWQYFSSDCRRTFGRPPRGpITKGnedeVIC 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  182 TSRYSSPFPCTGGEVIYRALSP-PHAAKDPYSAEAQAQLKVTNLRVRLLERQSCPCH--PLEPPALPAPYYAVYDFIVKG 258
Cdd:smart00136 159 TSEYSDIVPLEGGEIAFSLLEGrPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDElmDDRPEVTRRYYYAISDIAVGG 238
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 515-615 4.72e-28

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: 108.33  E-value: 4.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 515 KVFCGMkyTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLK-ILRGKRTLYPESWTNrgCTCPILNPGLEYLVAGHEDV 593
Cdd:cd03523     1 KAFCKS--DYVVRAKIKEIKEENDDVKYEVKIIKIYKTGKAKaDKADLRFYYTAPACC--PCHPILNPGREYLIMGKEED 76

                          90       100
                  ....*....|....*....|..
gi 2024345906 594 RTGRLIVNMKSFVHQWKSALGR 615
Cdd:cd03523    77 SQGGLVLDPLSFVEPWSPLSLR 98
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 517-622 7.62e-26

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: 102.04  E-value: 7.62e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 517 FCGmKYTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLYPESWTnrgCTCPILNPGLEYLVAGHEDVRTG 596
Cdd:pfam01759   3 ACK-GSDYVYKVKVLSVEEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD---CRCPQLRLGKEYLIMGKVGDLEG 78

                          90       100
                  ....*....|....*....|....*...
gi 2024345906 597 --RLIVNMKSFVHQWKSALGRKVLEILK 622
Cdd:pfam01759  79 rgRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
517-622 9.46e-21

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 87.81  E-value: 9.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906  517 FCGMKYTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLYPESWTNRgCTCP-ILNPGLEYLVAG-----H 590
Cdd:smart00643   4 ACKSDVDYVYKVKVLSVEEEGGFDKYTVKILEVIKSGTDELVRGKNKLRVFISRAS-CRCPlLLKLGKSYLIMGksgdlW 82

                           90       100       110
                   ....*....|....*....|....*....|..
gi 2024345906  591 EDVRTGRLIVNMKSFVHQWKSALGRKVLEILK 622
Cdd:smart00643  83 DAKGRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
 522-617 1.29e-18

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: 81.75  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 522 YTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLypesWTNRGCTCPILNPGLEYLVAGHEDVRTGRLIVN 601
Cdd:cd03581     8 YNYVIRAKVKEVKRGCHEVTAVVEVKEILKSSLVNIPRDTVTL----YTNSGCLCPPLTPNEEYIIMGYEDEERSRLLLV 83

                          90
                  ....*....|....*.
gi 2024345906 602 MKSFVHQWKSALGRKV 617
Cdd:cd03581    84 EGSLAEKWKDRLGKKV 99
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 393-447 3.55e-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: 61.22  E-value: 3.55e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2024345906 393 CSCHPLGSaalplgPRTFCDPSTGDCPCKPGVAGPRCDRCLPGYWGFGTSGCRPC 447
Cdd:pfam00053   1 CDCNPHGS------LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
393-444 4.65e-12

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 60.79  E-value: 4.65e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2024345906  393 CSCHPLGSAAlplgprTFCDPSTGDCPCKPGVAGPRCDRCLPGYWGFGTSGC 444
Cdd:smart00180   1 CDCDPGGSAS------GTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 392-443 1.68e-11

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: 59.29  E-value: 1.68e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2024345906 392 PCSCHPLGSaalplgPRTFCDPSTGDCPCKPGVAGPRCDRCLPGYWGFGTSG 443
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 ...
 515-624 6.44e-09

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: 54.17  E-value: 6.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 515 KVFCgmKYTYVIKTKILSAHDKGSHAEVNVKIKKVLKSTKLKILRGKRTLYpESWTNRGCTCPILNPGLEYLVAG--HED 592
Cdd:cd03579     2 KKYC--KKDYAVQAQVLSRETAGEWAKFTVNVQTVYKRGTSRLRRGDQPLW-VPRKDLACKCPKLKVGKSYLLLGkdEDS 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2024345906 593 VRTGRLIVNMKSFVHQWKSALGRKVLEILKRD 624
Cdd:cd03579    79 PERGGLILDKRSLVIEWRDEWARRLRRFQRRE 110
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 330-390 1.45e-06

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 45.42  E-value: 1.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024345906 330 CKCNGHA---DTCHFdmdawlasgnrSGGVCDnCQHNTEGQHCQRCKPGFYRDlrkPFSAPDAC 390
Cdd:pfam00053   1 CDCNPHGslsDTCDP-----------ETGQCL-CKPGVTGRHCDRCKPGYYGL---PSDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 259-318 7.80e-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: 7.80e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 259 SCFCNGHADHcvpvrgfrpvraAGAFHVVHGKCMCKHNTAGPHCQHCAPLYNDRPWQAAD 318
Cdd:cd00055     1 PCDCNGHGSL------------SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 329-379 9.78e-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: 43.11  E-value: 9.78e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2024345906 329 SCKCNGHAD---TCHFDmdawlasgnrsGGVCDnCQHNTEGQHCQRCKPGFYRD 379
Cdd:cd00055     1 PCDCNGHGSlsgQCDPG-----------TGQCE-CKPNTTGRRCDRCAPGYYGL 42
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
330-379 2.28e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.22  E-value: 2.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2024345906  330 CKCN--GHAD-TCHFDmdawlasgnrsGGVCDnCQHNTEGQHCQRCKPGFYRD 379
Cdd:smart00180   1 CDCDpgGSASgTCDPD-----------TGQCE-CKPNVTGRRCDRCAPGYYGD 41
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
285-315 9.22e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 37.29  E-value: 9.22e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 2024345906  285 HVVHGKCMCKHNTAGPHCQHCAPLYNDRPWQ 315
Cdd:smart00180  14 DPDTGQCECKPNVTGRRCDRCAPGYYGDGPP 44
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 260-319 1.75e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 36.56  E-value: 1.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024345906 260 CFCNGHADHcvpvrgfrpvraAGAFHVVHGKCMCKHNTAGPHCQHCAPLYNDRPWQAADG 319
Cdd:pfam00053   1 CDCNPHGSL------------SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
 
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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