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Conserved domains on  [gi|568947885|ref|XP_006540956|]
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netrin-5 isoform X9 [Mus musculus]

Protein Classification

calcium-binding EGF-like domain-containing protein; attractin family protein( domain architecture ID 10043567)

calcium-binding epidermal growth factor (EGF)-like domain-containing protein may play a crucial role in numerous protein-protein interactions| attractin family protein similar to middle and C-terminal regions of Homo sapiens attractin that is involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 247-372 1.19e-38

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: 134.30  E-value: 1.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885 247 LQRYCQQDYVLHAQVSASssqpsEAVGpEWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADLICGCLRLRPGADYLLLGR 326
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSR-----ETAG-EWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGK 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568947885 327 aaqthDDDNYDPARLILNRHGLALPWRPRWARPLRRLQQKERGGAC 372
Cdd:cd03579   75 -----DEDSPERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 153-202 1.10e-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: 53.51  E-value: 1.10e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568947885 153 ACQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNRCGPGYQQSRSPRMPCQ 202
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 90-144 7.86e-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: 40.03  E-value: 7.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947885  90 PCSCNQHA---RRCRFNSelfrlsggrsgGVCErCRHHTAGRHCHYCQPGFWRDPSQP 144
Cdd:cd00055    1 PCDCNGHGslsGQCDPGT-----------GQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 35-79 1.25e-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: 39.26  E-value: 1.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568947885  35 RCQCHGHAARCAT-RAQPPRCRCRHHTTGPGCESCRPSHRDWPWRP 79
Cdd:cd00055    1 PCDCNGHGSLSGQcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
 
Name Accession Description Interval E-value
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 247-372 1.19e-38

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: 134.30  E-value: 1.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885 247 LQRYCQQDYVLHAQVSASssqpsEAVGpEWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADLICGCLRLRPGADYLLLGR 326
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSR-----ETAG-EWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGK 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568947885 327 aaqthDDDNYDPARLILNRHGLALPWRPRWARPLRRLQQKERGGAC 372
Cdd:cd03579   75 -----DEDSPERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 248-365 9.38e-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: 97.03  E-value: 9.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885  248 QRYCQQ-DYVLHAQVsasssqPSEAVGPEWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADliCGCLRLRPGADYLLLGr 326
Cdd:pfam01759   1 KKACKGsDYVYKVKV------LSVEEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD--CRCPQLRLGKEYLIMG- 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568947885  327 aaqtHDDDNYDPARLILNRHGLALPWRPRWARPLRRLQQ 365
Cdd:pfam01759  72 ----KVGDLEGRGRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
254-365 3.39e-13

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 65.47  E-value: 3.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885   254 DYVLHAQVSASSSQPSeavgpeWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADLICGC-LRLRPGADYLLLGRAAQTHD 332
Cdd:smart00643  10 DYVYKVKVLSVEEEGG------FDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCpLLLKLGKSYLIMGKSGDLWD 83

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568947885   333 DDnyDPARLILNRHGLALPWRPRWARPLRRLQQ 365
Cdd:smart00643  84 AK--GRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 153-202 1.10e-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: 53.51  E-value: 1.10e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568947885 153 ACQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNRCGPGYQQSRSPRMPCQ 202
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
154-191 5.23e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 5.23e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568947885   154 CQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNRCGPGY 191
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 154-191 9.32e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 50.81  E-value: 9.32e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568947885  154 CQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNRCGPGY 191
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 90-144 7.86e-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: 40.03  E-value: 7.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947885  90 PCSCNQHA---RRCRFNSelfrlsggrsgGVCErCRHHTAGRHCHYCQPGFWRDPSQP 144
Cdd:cd00055    1 PCDCNGHGslsGQCDPGT-----------GQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 35-79 1.25e-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: 39.26  E-value: 1.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568947885  35 RCQCHGHAARCAT-RAQPPRCRCRHHTTGPGCESCRPSHRDWPWRP 79
Cdd:cd00055    1 PCDCNGHGSLSGQcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 113-144 2.73e-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: 38.49  E-value: 2.73e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568947885  113 RSGGVCeRCRHHTAGRHCHYCQPGFWRDPSQP 144
Cdd:pfam00053  15 PETGQC-LCKPGVTGRHCDRCKPGYYGLPSDP 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
115-141 3.98e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 34.98  E-value: 3.98e-03
                           10        20
                   ....*....|....*....|....*..
gi 568947885   115 GGVCErCRHHTAGRHCHYCQPGFWRDP 141
Cdd:smart00180  17 TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
 
Name Accession Description Interval E-value
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 247-372 1.19e-38

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: 134.30  E-value: 1.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885 247 LQRYCQQDYVLHAQVSASssqpsEAVGpEWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADLICGCLRLRPGADYLLLGR 326
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSR-----ETAG-EWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVGKSYLLLGK 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 568947885 327 aaqthDDDNYDPARLILNRHGLALPWRPRWARPLRRLQQKERGGAC 372
Cdd:cd03579   75 -----DEDSPERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 248-365 9.38e-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: 97.03  E-value: 9.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885  248 QRYCQQ-DYVLHAQVsasssqPSEAVGPEWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADliCGCLRLRPGADYLLLGr 326
Cdd:pfam01759   1 KKACKGsDYVYKVKV------LSVEEEGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD--CRCPQLRLGKEYLIMG- 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 568947885  327 aaqtHDDDNYDPARLILNRHGLALPWRPRWARPLRRLQQ 365
Cdd:pfam01759  72 ----KVGDLEGRGRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
254-365 3.39e-13

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 65.47  E-value: 3.39e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885   254 DYVLHAQVSASSSQPSeavgpeWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADLICGC-LRLRPGADYLLLGRAAQTHD 332
Cdd:smart00643  10 DYVYKVKVLSVEEEGG------FDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCpLLLKLGKSYLIMGKSGDLWD 83

                           90       100       110
                   ....*....|....*....|....*....|...
gi 568947885   333 DDnyDPARLILNRHGLALPWRPRWARPLRRLQQ 365
Cdd:smart00643  84 AK--GRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 248-363 7.08e-11

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: 58.64  E-value: 7.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885 248 QRYCQQDYVLHAQVSasssqpSEAVGPEWWRLAVHVLAVFKQRAWPVRRGGQEAWVPRADLICGCLRLRPGADYLLLGRA 327
Cdd:cd03523    1 KAFCKSDYVVRAKIK------EIKEENDDVKYEVKIIKIYKTGKAKADKADLRFYYTAPACCPCHPILNPGREYLIMGKE 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 568947885 328 aqthdDDNYDpaRLILNRHGLALPWRPRWARPLRRL 363
Cdd:cd03523   75 -----EDSQG--GLVLDPLSFVEPWSPLSLRQDRRL 103
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 153-202 1.10e-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: 53.51  E-value: 1.10e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 568947885 153 ACQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNRCGPGYQQSRSPRMPCQ 202
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
154-191 5.23e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 51.54  E-value: 5.23e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 568947885   154 CQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNRCGPGY 191
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 154-191 9.32e-09

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 50.81  E-value: 9.32e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568947885  154 CQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNRCGPGY 191
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 90-144 7.86e-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: 40.03  E-value: 7.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947885  90 PCSCNQHA---RRCRFNSelfrlsggrsgGVCErCRHHTAGRHCHYCQPGFWRDPSQP 144
Cdd:cd00055    1 PCDCNGHGslsGQCDPGT-----------GQCE-CKPNTTGRRCDRCAPGYYGLPSQG 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 35-79 1.25e-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: 39.26  E-value: 1.25e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568947885  35 RCQCHGHAARCAT-RAQPPRCRCRHHTTGPGCESCRPSHRDWPWRP 79
Cdd:cd00055    1 PCDCNGHGSLSGQcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
NTR_netrin-4_like cd03578
NTR domain, Netrin-4-like subfamily; composed of the C-terminal NTR domains of netrin-4 (beta ...
 255-367 1.86e-04

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: 40.62  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947885 255 YVLHAQVSASSSQPSEAVgpewwrLAVHVLAVFKQRAWPVRRGGQ----EAWVPRAdliCGCLRLRPGADYLLLGraaqt 330
Cdd:cd03578   11 YVIKIKVLSAHDKGTHAE------VNVKIKKVLKSTKLKLSRGKRtlypESWTSRG---CTCPILNPGLEYLVAG----- 76

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 568947885 331 HDDdnYDPARLILNRHGLALPWRPRWARPLRRLQQKE 367
Cdd:cd03578   77 HED--VRTGRLIVNMKSFVQHWKPSLGRKVMEILKRE 111
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 113-144 2.73e-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: 38.49  E-value: 2.73e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 568947885  113 RSGGVCeRCRHHTAGRHCHYCQPGFWRDPSQP 144
Cdd:pfam00053  15 PETGQC-LCKPGVTGRHCDRCKPGYYGLPSDP 45
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
115-141 3.98e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 34.98  E-value: 3.98e-03
                           10        20
                   ....*....|....*....|....*..
gi 568947885   115 GGVCErCRHHTAGRHCHYCQPGFWRDP 141
Cdd:smart00180  17 TGQCE-CKPNVTGRRCDRCAPGYYGDG 42
 
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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