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Conserved domains on  [gi|291084648|ref|NP_001166997|]
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netrin-5 isoform 2 precursor [Rattus norvegicus]

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 ...
 313-442 3.66e-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: 134.68  E-value: 3.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084648 313 LQKYCQQDYVLHARVAESAQVsassslsslseavgPEWWRLAVHVLAVFKQRAWPVRRGSQEAWVPRADLSCGCLRLRPG 392
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSRETA--------------GEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVG 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291084648 393 ADYLLLGRAAENHtDPAHLILNRHSLALPWRPRWAGPLRRLQQKERGGAC 442
Cdd:cd03579   67 KSYLLLGKDEDSP-ERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 227-276 1.07e-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: 56.59  E-value: 1.07e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 291084648 227 PCQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNHCGPGYQQSRSPRMPCQ 276
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 172-216 4.04e-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: 40.80  E-value: 4.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 291084648 172 RCQCHGHAARCAA-RAQPPRCRCRHHTTGPGCESCRPSHRDWPWRP 216
Cdd:cd00055    1 PCDCNGHGSLSGQcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_N super family cl02806
Laminin N-terminal (Domain VI);
80-123 9.54e-03

Laminin N-terminal (Domain VI);


The actual alignment was detected with superfamily member pfam00055:

Pssm-ID: 470680  Cd Length: 230  Bit Score: 37.56  E-value: 9.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 291084648   80 TLTLDLDGSFLLTSVTLRFCTAGPpalvlsAAWAI------GGPWRPlWR 123
Cdd:pfam00055  82 NLTLDLGKEFHFTYLILKFKSPRP------AAMVLerstdfGKTWQP-YQ 124
 
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 ...
 313-442 3.66e-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: 134.68  E-value: 3.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084648 313 LQKYCQQDYVLHARVAESAQVsassslsslseavgPEWWRLAVHVLAVFKQRAWPVRRGSQEAWVPRADLSCGCLRLRPG 392
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSRETA--------------GEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVG 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291084648 393 ADYLLLGRAAENHtDPAHLILNRHSLALPWRPRWAGPLRRLQQKERGGAC 442
Cdd:cd03579   67 KSYLLLGKDEDSP-ERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 314-435 1.65e-21

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: 88.94  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084648  314 QKYCQQ-DYVLHARVAESAQvsassslsslseavGPEWWRLAVHVLAVFKQRAWPVRRGSQEAWVPRADlsCGCLRLRPG 392
Cdd:pfam01759   1 KKACKGsDYVYKVKVLSVEE--------------EGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD--CRCPQLRLG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291084648  393 ADYLLLGRaAENHTDPAHLILNRHSLALPWRPRWAGPLRRLQQ 435
Cdd:pfam01759  65 KEYLIMGK-VGDLEGRGRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
313-435 4.05e-12

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 62.77  E-value: 4.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084648   313 LQKYCQQ--DYVLHARVAESAQvsassslsslseavGPEWWRLAVHVLAVFKQRAWPVRRGSQEAWVPRADLSCGC-LRL 389
Cdd:smart00643   1 LEKACKSdvDYVYKVKVLSVEE--------------EGGFDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCpLLL 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 291084648   390 RPGADYLLLGR--AAENHTDPAHLILNRHSLALPWRPRWAGPLRRLQQ 435
Cdd:smart00643  67 KLGKSYLIMGKsgDLWDAKGRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 227-276 1.07e-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: 56.59  E-value: 1.07e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 291084648 227 PCQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNHCGPGYQQSRSPRMPCQ 276
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
228-265 1.54e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 1.54e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 291084648   228 CQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNHCGPGY 265
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 228-265 3.62e-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: 52.36  E-value: 3.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 291084648  228 CQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNHCGPGY 265
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 172-216 4.04e-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: 40.80  E-value: 4.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 291084648 172 RCQCHGHAARCAA-RAQPPRCRCRHHTTGPGCESCRPSHRDWPWRP 216
Cdd:cd00055    1 PCDCNGHGSLSGQcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
80-123 9.54e-03

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 37.56  E-value: 9.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 291084648   80 TLTLDLDGSFLLTSVTLRFCTAGPpalvlsAAWAI------GGPWRPlWR 123
Cdd:pfam00055  82 NLTLDLGKEFHFTYLILKFKSPRP------AAMVLerstdfGKTWQP-YQ 124
 
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 ...
 313-442 3.66e-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: 134.68  E-value: 3.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084648 313 LQKYCQQDYVLHARVAESAQVsassslsslseavgPEWWRLAVHVLAVFKQRAWPVRRGSQEAWVPRADLSCGCLRLRPG 392
Cdd:cd03579    1 LKKYCKKDYAVQAQVLSRETA--------------GEWAKFTVNVQTVYKRGTSRLRRGDQPLWVPRKDLACKCPKLKVG 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 291084648 393 ADYLLLGRAAENHtDPAHLILNRHSLALPWRPRWAGPLRRLQQKERGGAC 442
Cdd:cd03579   67 KSYLLLGKDEDSP-ERGGLILDKRSLVIEWRDEWARRLRRFQRRERRGKC 115
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 314-435 1.65e-21

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: 88.94  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084648  314 QKYCQQ-DYVLHARVAESAQvsassslsslseavGPEWWRLAVHVLAVFKQRAWPVRRGSQEAWVPRADlsCGCLRLRPG 392
Cdd:pfam01759   1 KKACKGsDYVYKVKVLSVEE--------------EGSFDKYTVKVKEVLKEGTDKIQRGKVRLFLKRGD--CRCPQLRLG 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291084648  393 ADYLLLGRaAENHTDPAHLILNRHSLALPWRPRWAGPLRRLQQ 435
Cdd:pfam01759  65 KEYLIMGK-VGDLEGRGRYVLDKNSWVEPWPTKWECKLRELQK 106
C345C smart00643
Netrin C-terminal Domain;
313-435 4.05e-12

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 62.77  E-value: 4.05e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084648   313 LQKYCQQ--DYVLHARVAESAQvsassslsslseavGPEWWRLAVHVLAVFKQRAWPVRRGSQEAWVPRADLSCGC-LRL 389
Cdd:smart00643   1 LEKACKSdvDYVYKVKVLSVEE--------------EGGFDKYTVKILEVIKSGTDELVRGKNKLRVFISRASCRCpLLL 66

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 291084648   390 RPGADYLLLGR--AAENHTDPAHLILNRHSLALPWRPRWAGPLRRLQQ 435
Cdd:smart00643  67 KLGKSYLIMGKsgDLWDAKGRGQYVLGKNSWVEEWPTEEECRLRRLQK 114
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 314-433 6.78e-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: 59.02  E-value: 6.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084648 314 QKYCQQDYVLHARVAESAQVsassslsslseavgPEWWRLAVHVLAVFKQRAWPVRRGSQEAWVPRADLSCGCLRLRPGA 393
Cdd:cd03523    1 KAFCKSDYVVRAKIKEIKEE--------------NDDVKYEVKIIKIYKTGKAKADKADLRFYYTAPACCPCHPILNPGR 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 291084648 394 DYLLLGRAAENHtdpAHLILNRHSLALPWRPRWAGPLRRL 433
Cdd:cd03523   67 EYLIMGKEEDSQ---GGLVLDPLSFVEPWSPLSLRQDRRL 103
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 227-276 1.07e-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: 56.59  E-value: 1.07e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 291084648 227 PCQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNHCGPGYQQSRSPRMPCQ 276
Cdd:cd00055    1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
228-265 1.54e-09

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 53.47  E-value: 1.54e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 291084648   228 CQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNHCGPGY 265
Cdd:smart00180   1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 228-265 3.62e-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: 52.36  E-value: 3.62e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 291084648  228 CQCHPIGATGGMCNQTSGQCSCKLGVTGLTCNHCGPGY 265
Cdd:pfam00053   1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 172-216 4.04e-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: 40.80  E-value: 4.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 291084648 172 RCQCHGHAARCAA-RAQPPRCRCRHHTTGPGCESCRPSHRDWPWRP 216
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 ...
 355-424 6.34e-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: 39.47  E-value: 6.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291084648 355 VHVLAVFKQRAWPVRRGSQ----EAWVPRAdlsCGCLRLRPGADYLLLGraaENHTDPAHLILNRHSLALPWRP 424
Cdd:cd03578   31 VKIKKVLKSTKLKLSRGKRtlypESWTSRG---CTCPILNPGLEYLVAG---HEDVRTGRLIVNMKSFVQHWKP 98
Laminin_N pfam00055
Laminin N-terminal (Domain VI);
80-123 9.54e-03

Laminin N-terminal (Domain VI);


Pssm-ID: 459653  Cd Length: 230  Bit Score: 37.56  E-value: 9.54e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 291084648   80 TLTLDLDGSFLLTSVTLRFCTAGPpalvlsAAWAI------GGPWRPlWR 123
Cdd:pfam00055  82 NLTLDLGKEFHFTYLILKFKSPRP------AAMVLerstdfGKTWQP-YQ 124
 
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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