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Conserved domains on  [gi|7710094|ref|NP_057896|]
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secreted frizzled-related sequence protein 4 precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CRD_FZ super family cl02447
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 20-146 1.70e-94

CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


The actual alignment was detected with superfamily member cd07442:

Pssm-ID: 470581  Cd Length: 127  Bit Score: 276.91  E-value: 1.70e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   20 RGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHDPIKPCKS 99
Cdd:cd07442   1 QGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICTLEFLYDPIKPCRS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7710094  100 VCQRARDDCEPLMKMYNHSWPESLACDELPVYDRGVCISPEAIVTDL 146
Cdd:cd07442  81 VCQRARDGCEPIMRRYNHSWPESLACDDLPVYDRGVCISPEAIVTDL 127
NTR_like super family cl02512
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 188-296 1.36e-54

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.


The actual alignment was detected with superfamily member cd03581:

Pssm-ID: 470599  Cd Length: 111  Bit Score: 174.58  E-value: 1.36e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094  188 ATYLSKNYSYVIHAKIKAVQRsGCNEVTTVVDVKEIFKSLSP-IPRTQVPLITNSSCQCPHILPHQDVLIMCYEW--RSR 264
Cdd:cd03581   1 KTYLKNNYNYVIRAKVKEVKR-GCHEVTAVVEVKEILKSSLVnIPRDTVTLYTNSGCLCPPLTPNEEYIIMGYEDeeRSR 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 7710094  265 MMLLENCLVEKWRDQLSRRSIQWEERLQEQQR 296
Cdd:cd03581  80 LLLVEGSLAEKWKDRLGKKVKRWDQKLQHQRR 111
 
Name Accession Description Interval E-value
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 20-146 1.70e-94

Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 4 (SFRP4), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


Pssm-ID: 143551  Cd Length: 127  Bit Score: 276.91  E-value: 1.70e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   20 RGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHDPIKPCKS 99
Cdd:cd07442   1 QGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICTLEFLYDPIKPCRS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7710094  100 VCQRARDDCEPLMKMYNHSWPESLACDELPVYDRGVCISPEAIVTDL 146
Cdd:cd07442  81 VCQRARDGCEPIMRRYNHSWPESLACDDLPVYDRGVCISPEAIVTDL 127
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
 188-296 1.36e-54

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: 174.58  E-value: 1.36e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094  188 ATYLSKNYSYVIHAKIKAVQRsGCNEVTTVVDVKEIFKSLSP-IPRTQVPLITNSSCQCPHILPHQDVLIMCYEW--RSR 264
Cdd:cd03581   1 KTYLKNNYNYVIRAKVKEVKR-GCHEVTAVVEVKEILKSSLVnIPRDTVTLYTNSGCLCPPLTPNEEYIIMGYEDeeRSR 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 7710094  265 MMLLENCLVEKWRDQLSRRSIQWEERLQEQQR 296
Cdd:cd03581  80 LLLVEGSLAEKWKDRLGKKVKRWDQKLQHQRR 111
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 24-139 2.41e-44

Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)].


Pssm-ID: 214498  Cd Length: 113  Bit Score: 148.23  E-value: 2.41e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094      24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFlhDPIKPCKSVCQR 103
Cdd:smart00063   1 CEPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDL--RPILPCRSLCEA 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 7710094     104 ARDDCEPLMKMYNHSWPESLACDELPVYDrGVCISP 139
Cdd:smart00063  79 AREGCEPLMEKFGFPWPEFLRCDRFPVQE-ELCMDP 113
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 24-131 7.29e-34

Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines.


Pssm-ID: 460190  Cd Length: 116  Bit Score: 121.14  E-value: 7.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094     24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILA-----IEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHDPIK-PC 97
Cdd:pfam01392   1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSlaylvLSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCpPC 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 7710094     98 KSVCQRARDDCEPLMKM--YNHSWPESLACDELPVY 131
Cdd:pfam01392  81 RSLCEEVRYGCEPLLEEakFGFSWPEFLDCDSLPAD 116
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 193-287 5.86e-19

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: 80.85  E-value: 5.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094    193 KNYSYVIHAKIKAVQRSGcNEVTTVVDVKEIFKS-LSPIPR-TQVPLITNSSCQCPHILPHQDVLIM----CYEWRSRMM 266
Cdd:pfam01759   5 KGSDYVYKVKVLSVEEEG-SFDKYTVKVKEVLKEgTDKIQRgKVRLFLKRGDCRCPQLRLGKEYLIMgkvgDLEGRGRYV 83

                          90       100
                  ....*....|....*....|.
gi 7710094    267 LLENCLVEKWRDQLSRRSIQW 287
Cdd:pfam01759  84 LDKNSWVEPWPTKWECKLREL 104
C345C smart00643
Netrin C-terminal Domain;
189-296 9.03e-04

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 38.50  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094     189 TYLSKNYSYVIHAKIKAVQRSGcNEVTTVVDVKEIFKS-LSPIPR---TQVPLITNSSCQCPHIL-PHQDVLIM------ 257
Cdd:smart00643   3 KACKSDVDYVYKVKVLSVEEEG-GFDKYTVKILEVIKSgTDELVRgknKLRVFISRASCRCPLLLkLGKSYLIMgksgdl 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 7710094     258 -CYEWRSRMMLLENCLVEKWRDqlsrrsiQWEERLQEQQR 296
Cdd:smart00643  82 wDAKGRGQYVLGKNSWVEEWPT-------EEECRLRRLQK 114
 
Name Accession Description Interval E-value
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 20-146 1.70e-94

Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 4 (SFRP4), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


Pssm-ID: 143551  Cd Length: 127  Bit Score: 276.91  E-value: 1.70e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   20 RGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHDPIKPCKS 99
Cdd:cd07442   1 QGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAVLAIEQYEELVDTGCSPVLPFFLCAMYAPICTLEFLYDPIKPCRS 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 7710094  100 VCQRARDDCEPLMKMYNHSWPESLACDELPVYDRGVCISPEAIVTDL 146
Cdd:cd07442  81 VCQRARDGCEPIMRRYNHSWPESLACDDLPVYDRGVCISPEAIVTDL 127
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 22-144 6.47e-74

Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt antagonist; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), which plays important roles in embryogenesis and postnatal development as an antagonist of Wnt proteins, key players in a number of fundamental cellular processes. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled proteins (Fz), thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP3 regulates Wnt signaling activity in bone development and homeostasis. It is also involved in the control of planar cell polarity.


Pssm-ID: 143550  Cd Length: 126  Bit Score: 224.54  E-value: 6.47e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   22 APCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHDPIKPCKSVC 101
Cdd:cd07441   2 ASCEPVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQFEGLLGTQCSPDLLFFLCAMYAPICTIDFQHEPIKPCKSVC 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7710094  102 QRARDDCEPLMKMYNHSWPESLACDELPVYDRGVCISPEAIVT 144
Cdd:cd07441  82 ERARAGCEPVLIRYRHTWPESLACEELPVYDRGVCISPEAIVT 124
NTR_Sfrp3_like cd03581
NTR domain, Secreted frizzled-related protein (Sfrp) 3-like subfamily; composed of proteins ...
 188-296 1.36e-54

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: 174.58  E-value: 1.36e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094  188 ATYLSKNYSYVIHAKIKAVQRsGCNEVTTVVDVKEIFKSLSP-IPRTQVPLITNSSCQCPHILPHQDVLIMCYEW--RSR 264
Cdd:cd03581   1 KTYLKNNYNYVIRAKVKEVKR-GCHEVTAVVEVKEILKSSLVnIPRDTVTLYTNSGCLCPPLTPNEEYIIMGYEDeeRSR 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 7710094  265 MMLLENCLVEKWRDQLSRRSIQWEERLQEQQR 296
Cdd:cd03581  80 LLLVEGSLAEKWKDRLGKKVKRWDQKLQHQRR 111
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 24-139 2.41e-44

Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell along the anteroposterior axis. Homologues of the N-terminal region of frizzled exist either as transmembrane or secreted molecules. Frizzled homologues are reported to be receptors for the Wnt growth factors. (Not yet in MEDLINE: the FRI domain occurs in several receptor tyrosine kinases [Xu, Y.K. and Nusse, Curr. Biol. 8 R405-R406 (1998); Masiakowski, P. and Yanopoulos, G.D., Curr. Biol. 8, R407 (1998)].


Pssm-ID: 214498  Cd Length: 113  Bit Score: 148.23  E-value: 2.41e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094      24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFlhDPIKPCKSVCQR 103
Cdd:smart00063   1 CEPITIPLCKDLGYNLTSMPNLLGHTTQEEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPICTEDL--RPILPCRSLCEA 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 7710094     104 ARDDCEPLMKMYNHSWPESLACDELPVYDrGVCISP 139
Cdd:smart00063  79 AREGCEPLMEKFGFPWPEFLRCDRFPVQE-ELCMDP 113
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 24-129 4.09e-43

Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) and frizzled 8 (Fz8) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143565  Cd Length: 120  Bit Score: 145.23  E-value: 4.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICtLEFLHDPIKPCKSVCQR 103
Cdd:cd07456   2 CEEITIPMCKGIGYNMTYMPNQFNHDTQEEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPIC-LEDYDKPLPPCRSVCER 80

                        90       100
                ....*....|....*....|....*.
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELP 129
Cdd:cd07456  81 ARDGCAPIMRQYGFAWPERMSCDALP 106
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
 24-137 1.60e-42

Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1), frizzled 2 (Fz2), and frizzled 7 (Fz7) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143567  Cd Length: 119  Bit Score: 143.71  E-value: 1.60e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLefLHDPIKPCKSVCQR 103
Cdd:cd07458   3 CEPITIPLCTDIPYNMTIFPNLLGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVCTV--LERPIPPCRSLCES 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELPVY-DRGVCI 137
Cdd:cd07458  81 ARQGCEALMNKFGFQWPESLDCEKFPVHgAGDLCV 115
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 24-140 3.85e-41

CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143549  Cd Length: 119  Bit Score: 140.33  E-value: 3.85e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTlEFLHDPIKPCKSVCQR 103
Cdd:cd07066   2 CEPIPLPLCRGLPYNTTRFPNLLGHESQEEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECT-PDGDRPIPPCRSLCEE 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELPV-YDRGVCISPE 140
Cdd:cd07066  81 VRDSCEPLMLAFGFPWPEPLDCDRFPDsNEEGLCISPP 118
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 24-133 2.48e-39

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 5 (Fz5) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz5 plays critical regulating roles in the yolk sac and placental angiogenesis, in the maturation of the Paneth cell phenotype, in governing the neural potential of progenitors in the developing retina, and in neuronal survival in the parafascicular nucleus.


Pssm-ID: 143569 [Multi-domain]  Cd Length: 127  Bit Score: 135.91  E-value: 2.48e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFlHDPIKPCKSVCQR 103
Cdd:cd07460   5 CQEITVPMCKGIGYNLTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLRFFLCSMYTPICLPDY-RKPLPPCRSVCER 83

                        90       100       110
                ....*....|....*....|....*....|
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELPVYDR 133
Cdd:cd07460  84 AKAGCSPLMRQYGFAWPERMNCDRLPVLGD 113
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 20-149 8.05e-37

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz9 may play a signaling role in lymphoid development and maturation, particularly at points where B cells undergo self-renewal prior to further differentiation.


Pssm-ID: 143572  Cd Length: 127  Bit Score: 129.37  E-value: 8.05e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   20 RGAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTlEFLHDPIKPCKS 99
Cdd:cd07463   1 RAAKCQPVVIPMCRGIGYNLTRMPNFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCT-DQVSTSIPACRP 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 7710094  100 VCQRARDDCEPLMKMYNHSWPESLACDELPVYDrgvciSPEAIVTDLPED 149
Cdd:cd07463  80 MCEQARQKCSPIMEQFNFGWPESLDCSRLPTRN-----DPNALCMEAPEN 124
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 22-129 1.03e-36

Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 9 (Fz9) and frizzled 10 (Fz10) receptors, and similar proteins. This domain is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines.


Pssm-ID: 143566  Cd Length: 121  Bit Score: 128.77  E-value: 1.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   22 APCEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTlEFLHDPIKPCKSVC 101
Cdd:cd07457   1 GKCERITIPMCQGIGYNMTRMPNLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCT-EQVSIPIPACRSMC 79

                        90       100
                ....*....|....*....|....*...
gi 7710094  102 QRARDDCEPLMKMYNHSWPESLACDELP 129
Cdd:cd07457  80 EQARDKCSPIMEQFSFSWPDSLDCDRLP 107
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 24-130 3.45e-36

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 8 (Fz8) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz8 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula.


Pssm-ID: 143570  Cd Length: 125  Bit Score: 127.41  E-value: 3.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICtLEFLHDPIKPCKSVCQR 103
Cdd:cd07461   5 CQEITVPLCKGIGYNYTYMPNQFNHDTQDEAGLEVHQFWPLVEIQCSPDLKFFLCSMYTPIC-LEDYKKPLPPCRSVCER 83

                        90       100
                ....*....|....*....|....*..
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELPV 130
Cdd:cd07461  84 AKAGCAPLMRQYGFPWPDRMRCDLLPE 110
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 24-131 7.29e-34

Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This domain of unknown function has been independently identified by several groups. The domain contains 10 conserved cysteines.


Pssm-ID: 460190  Cd Length: 116  Bit Score: 121.14  E-value: 7.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094     24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILA-----IEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHDPIK-PC 97
Cdd:pfam01392   1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSlaylvLSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCpPC 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 7710094     98 KSVCQRARDDCEPLMKM--YNHSWPESLACDELPVY 131
Cdd:pfam01392  81 RSLCEEVRYGCEPLLEEakFGFSWPEFLDCDSLPAD 116
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 24-137 3.77e-33

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 7 (Fz7) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Xenopus Fz7 is important in Wnt/beta-catenin signaling pathways controlling the transcriptional activation of target genes Siamois and Xnr3 in the animal caps of late blastula.


Pssm-ID: 143575 [Multi-domain]  Cd Length: 125  Bit Score: 119.42  E-value: 3.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLefLHDPIKPCKSVCQR 103
Cdd:cd07466   5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELKFFLCSMYAPVCTV--LEQAIPPCRSLCER 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELPVYDRG-VCI 137
Cdd:cd07466  83 ARQGCEALMNKFGFQWPERLRCENFPVHGAGeICV 117
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
 24-130 5.32e-33

Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 4 (Fz4) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and the Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 4 (Fz4) activates the Ca(2+)/calmodulin-dependent protein kinase II and protein kinase C of the Wnt/Ca(2+) signaling pathway during retinal angiogenesis. Mutations in Fz4 lead to familial exudative vitreoretinopathy (FEVR), a hereditary ocular disorder characterized by failure of the peripheral retinal vascularization. In addition, the interplay between Fz4 and norrin as a receptor-ligand pair plays an important role in vascular development in the retina and inner ear in a Wnt-independent manner.


Pssm-ID: 143557  Cd Length: 126  Bit Score: 119.10  E-value: 5.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTlEFLHDPIKPCKSVCQR 103
Cdd:cd07448   4 CEPIRIEMCQGLGYNVTRMPNLVGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCT-EKVPVPIGPCRPLCLS 82

                        90       100
                ....*....|....*....|....*..
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELPV 130
Cdd:cd07448  83 VKKRCLPVLKEFGFPWPEALNCSKFPP 109
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 24-129 5.79e-32

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 10 (Fz10) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. The cellular functon of Fz10 is unknown.


Pssm-ID: 143571  Cd Length: 127  Bit Score: 116.66  E-value: 5.79e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTlEFLHDPIKPCKSVCQR 103
Cdd:cd07462   5 CQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCT-EQVSTPIPACRVMCEQ 83

                        90       100
                ....*....|....*....|....*.
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELP 129
Cdd:cd07462  84 ARLKCSPIMEQFNFKWPDSLDCSKLP 109
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 24-129 9.06e-32

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 2 (Fz2) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz2 is involved in the Wnt/beta-catenin signaling pathway and in the activation of protein kinase C and calcium/calmodulin-dependent protein kinase (CaM kinase).


Pssm-ID: 143573  Cd Length: 127  Bit Score: 115.95  E-value: 9.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLefLHDPIKPCKSVCQR 103
Cdd:cd07464   5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSLELRFFLCSMYAPVCTV--LEQAIPPCRSICER 82

                        90       100
                ....*....|....*....|....*.
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELP 129
Cdd:cd07464  83 ARQGCEALMNKFGFQWPERLRCENFP 108
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 24-134 1.62e-31

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 1 (Fz1) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata.


Pssm-ID: 143574  Cd Length: 127  Bit Score: 115.54  E-value: 1.62e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLefLHDPIKPCKSVCQR 103
Cdd:cd07465   5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSAELKFFLCSMYAPVCTV--LEQALPPCRSLCER 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELPVYDRG 134
Cdd:cd07465  83 ARQGCEALMNKFGFQWPDTLRCEKFPVHGAG 113
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
 24-139 2.57e-30

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 3 (Fz3) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Fz3 plays a vital role in the anterior-posterior guidance of commissural axons. Knockout mice without Fz3 show defects in fiber tracts in the rostral CNS.


Pssm-ID: 143558 [Multi-domain]  Cd Length: 127  Bit Score: 112.02  E-value: 2.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTlEFLHDPIkPCKSVCQR 103
Cdd:cd07449   5 CEPITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEPFHPMVNLECSRDFRPFLCALYAPVCM-EYGRVTL-PCRRLCQR 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELP----VYDRGVCISP 139
Cdd:cd07449  83 AYSECSKLMEMFGVPWPEDMECSRFPdcdePYPRLVDLSL 122
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 22-151 2.60e-24

Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential part of the crescent protein, a member of the secreted frizzled-related protein (SFRP) family, which regulates convergent extension movements (CEMs) during gastrulation and neurulation. Xenopus laevis crescent efficiently forms inhibitory complexes with Wnt5a and Wnt11, but this effect is cancelled in the presence of another member of the SFRP family, Frzb1. A potential role for Crescent in head formation is to regulate a non-canonical Wnt pathway positively in the adjacent posterior mesoderm, and negatively in the overlying anterior neuroectoderm.


Pssm-ID: 143562 [Multi-domain]  Cd Length: 135  Bit Score: 96.55  E-value: 2.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   22 APCeaVRIP----MCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICtlefLHDPIKPC 97
Cdd:cd07453   1 SPC--MRIPksmaLCYDIGYSEMRIPNLLEHETMAEVIQQSSSWLPLLARECHPDARIFLCSLFAPIC----WDRPIYPC 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 7710094   98 KSVCQRARDDCEPLMKMYNHSWPESLACDELPVyDRGVCISPEAIVTDLPEDVK 151
Cdd:cd07453  75 RSLCEAVRSSCAPLMACYGYPWPEILHCDKFPV-DHDLCISPQFIDTLSPERVK 127
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 31-139 2.44e-20

Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential part of the sizzled protein, which regulates bone morphogenetic protein (Bmp) signaling by stabilizing chordin, and plays a critical role in the patterning of vertebrate and invertebrate embryos. Sizzled also functions in the ventral region as a Wnt inhibitor and modulates canonical Wnt signaling. Sizzled proteins belong to the secreted frizzled-related protein family (SFRP), and have be identified in the genomes of birds, fishes and frogs, but not mammals.


Pssm-ID: 143561  Cd Length: 141  Bit Score: 85.70  E-value: 2.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   31 MCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHdpikPCKSVCQRARDDCEP 110
Cdd:cd07452  18 MCQDVGYSEMRLPNLLGHTSMAEVVPKSADWQTLLHTGCHPHARTFLCSLFAPVCLDTFIQ----PCRSMCVAVRDSCAP 93

                        90       100
                ....*....|....*....|....*....
gi 7710094  111 LMKMYNHSWPESLACDELPVyDRGVCISP 139
Cdd:cd07452  94 VLACHGHSWPESLDCDRFPA-GEDMCLAS 121
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 24-140 3.41e-20

One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the second (C-terminal) CRD.


Pssm-ID: 143579 [Multi-domain]  Cd Length: 122  Bit Score: 85.07  E-value: 3.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQ--YEELVDVNCSSVLRFFLCAMYAPICTLEfLHDPIKPCKSVC 101
Cdd:cd07888   2 CEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESslFPALVQTNCYKYLMFFACTILVPKCDPV-TQQRIPPCRSLC 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 7710094  102 QRARDDCEPLMKMYNHSWPESLACDELPV--YDRGVCISPE 140
Cdd:cd07888  81 RNSKERCESVLGIVGLQWPEDTDCAQFPEenSDNQTCLLPD 121
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
 24-129 7.55e-20

Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich domain (CRD) is an essential extracellular portion of the frizzled 6 (Fz6) receptor, and is required for binding Wnt proteins, which play fundamental roles in many aspects of early development, such as cell and tissue polarity, neural synapse formation, and the regulation of proliferation. Fz proteins serve as Wnt receptors for multiple signal transduction pathways, including both beta-catenin dependent and -independent cellular signaling, as well as the planar cell polarity pathway and Ca(2+) modulating signaling pathway. CRD containing Fzs have been found in diverse species from amoebas to mammals. 10 different frizzled proteins are found in vertebrata. Frizzled 6 (Fz6) is expressed in the skin and hair follicles and controls hair patterning in mammals using a Fz-dependent tissue polarity system, which is similar to the one that patterns the Drosophila cuticle.


Pssm-ID: 143559 [Multi-domain]  Cd Length: 127  Bit Score: 84.05  E-value: 7.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTlEFLHDpIKPCKSVCQR 103
Cdd:cd07450   5 CEPITVPRCLKMPYNMTFFPNLMGHYDQDIAAVEMEPFLPLANLRCSPNVHTFLCQAFVPTCT-EQIHV-VRPCRELCEK 82

                        90       100
                ....*....|....*....|....*.
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELP 129
Cdd:cd07450  83 VYSDCKKLIDTFGISWPEELECDRLQ 108
NTR pfam01759
UNC-6/NTR/C345C module; Sequence similarity between netrin UNC-6 and C345C complement protein ...
 193-287 5.86e-19

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: 80.85  E-value: 5.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094    193 KNYSYVIHAKIKAVQRSGcNEVTTVVDVKEIFKS-LSPIPR-TQVPLITNSSCQCPHILPHQDVLIM----CYEWRSRMM 266
Cdd:pfam01759   5 KGSDYVYKVKVLSVEEEG-SFDKYTVKVKEVLKEgTDKIQRgKVRLFLKRGDCRCPQLRLGKEYLIMgkvgDLEGRGRYV 83

                          90       100
                  ....*....|....*....|.
gi 7710094    267 LLENCLVEKWRDQLSRRSIQW 287
Cdd:pfam01759  84 LDKNSWVEPWPTKWECKLREL 104
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 29-138 7.85e-19

Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related Protein 5 (SFRP5), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs.


Pssm-ID: 143553  Cd Length: 127  Bit Score: 81.53  E-value: 7.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   29 IPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICtlefLHDPIKPCKSVCQRARDDC 108
Cdd:cd07444  14 LPLCHNVGYKRMRLPNLLEHESMAEVKQQASSWVPLLAKRCHADTQVFLCSLFAPVC----LDRPIYPCRSLCEAVRDSC 89

                        90       100       110
                ....*....|....*....|....*....|
gi 7710094  109 EPLMKMYNHSWPESLACDELPVyDRGVCIS 138
Cdd:cd07444  90 APVMESYGFPWPEMLHCHKFPL-DNDLCIA 118
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 20-139 1.33e-17

Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt activity; The cysteine-rich-domain (CRD) is an essential part of the secreted frizzled related protein 2 (SFRP2), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to CRD domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. As a Wnt antagonist, SFRP2 regulates Nkx2.2 expression in the ventral spinal cord and anteroposterior axis elongation. SFRP2 also has a Wnt-independent function as an enhancer of procollagen cleavage by the TLD proteinases. SFRP2 binds both procollagen and TLD, thus facilitating the enzymatic reaction by bringing together the proteinase and its substrate.


Pssm-ID: 143555  Cd Length: 128  Bit Score: 78.03  E-value: 1.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   20 RGAPCEAVRIPM--CRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICtLEFLHDPIKPC 97
Cdd:cd07446   1 KKSNCKPIPANMllCHGIEYTNMRLPNLLGHETMKEVLQQAGSWIPLVQKQCHPDTKKFLCSLFAPVC-LDDLDEAIQPC 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7710094   98 KSVCQRARDDCEPLMKMYNHSWPESLACDELPVyDRGVCISP 139
Cdd:cd07446  80 RSLCEAVKDGCAPVMSAFGFPWPDMLDCTRFPL-DNDLCIPP 120
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 23-138 3.92e-17

Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt activity; The cysteine-rich domain (CRD) is an essential part of the secreted frizzled-related protein 1 (SFRP1), which regulates the activity of Wnt proteins, key players in a number of fundamental cellular processes such as embryogenesis and postnatal development. SFRPs antagonize the activation of Wnt signaling by binding to the CRDs domains of frizzled (Fz) proteins, thereby preventing Wnt proteins from binding to these receptors. SFRPs are also known to have functions unrelated to Wnt, as enhancers of procollagen cleavage by the TLD proteinases. SFRPs and Fz proteins both contain CRD domains, but SFRPs lack the seven-pass transmembrane domain which is an integral part of Fzs. SFRP1 is expressed in many tissues and is involved in the regulation of Wnt signaling in osteoblasts, leading to enhanced trabecular bone formation in adults; it has also been shown to control the growth of retinal ganglion cell axons and the elongation of the antero-posterior axis.


Pssm-ID: 143552  Cd Length: 124  Bit Score: 76.48  E-value: 3.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   23 PCEAVRIP----MCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICtlefLHDPIKPCK 98
Cdd:cd07443   4 PPQCVDIPadlrLCHNVGYKKMVLPNLLDHETMAEVKQQASSWVPLLNKNCHKGTQVFLCSLFAPVC----LDRPVYPCR 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7710094   99 SVCQRARDDCEPLMKMYNHSWPESLACDELPVYDrgVCIS 138
Cdd:cd07443  80 WLCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEGE--VCIA 117
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 24-139 1.53e-13

Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component of a number of cell surface receptors, which are involved in multiple signal transduction pathways, particularly in modulating the activity of the Wnt proteins, which play a fundamental role in the early development of metazoans. CRD is also found in secreted frizzled related proteins (SFRPs), which lack the transmembrane segment found in the frizzled protein. The CRD domain is also present in the alpha-1 chain of mouse type XVIII collagen, in carboxypeptidase Z, several receptor tyrosine kinases, and the mosaic transmembrane serine protease corin. The CRD domain is well conserved in metazoans - 10 frizzled proteins have been identified in mammals, 4 in Drosophila and 3 in Caenorhabditis elegans. CRD domains have also been identified in multiple tandem copies in a Dictyostelium discoideum protein. Very little is known about the mechanism by which CRD domains interact with their ligands. The domain contains 10 conserved cysteines. The protein lin-17 is involved in cell type specification during Caenorhabditis elegans vulval development.


Pssm-ID: 143563  Cd Length: 124  Bit Score: 66.73  E-value: 1.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTlEFLHDPIKPCKSVCQR 103
Cdd:cd07454   5 CIPIDIELCKDLPYNYTYFPNTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCP-IGMPQAVTSCKSVCEQ 83

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 7710094  104 ARDDCEPLMKMYNHSWPESLACDELPVyDRGVCISP 139
Cdd:cd07454  84 VKADCFSILEEFGIGWPEPLNCAQFPD-PPELCMKP 118
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
 21-139 1.12e-09

Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The cysteine-rich-domain (CRD) is an essential part of carboxypeptidase Z, a member of the carboxypeptidase E family of metallocarboxypeptidases. This is a group of Zn-dependent enzymes implicated in the intra- and extracellular processing of proteins. Carboxypeptidase Z removes C-terminal basic amino acid residues from its substrates, particularly arginine. The CRD acts as a ligand-binding domain for Wnts involved in developmental processes. CPZ binds and may process Wnt-4, CPZ has also been found to enhance the induction of the homeobox gene Cdx1. During vertebrate embryogenesis, the CRD of CPZ upregulates Pax3, a Wnt reporter gene essential for patterning of somites and limb development.


Pssm-ID: 143556  Cd Length: 128  Bit Score: 55.92  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   21 GAPCEAVRIPMCRHMPWNITRMPNHLHHSTQENA-----ILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLhdpIK 95
Cdd:cd07447   1 SATCTDLLLSYCSDVSYTQTTFPNLLGHRSREVTeagaeYLLLSVLHGLLGGECNPDIRLLGCSVLAPRCENDKV---IK 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 7710094   96 PCKSVCQRARDDCEPLMKMYNHSWPESLACDELPVYDRGVCISP 139
Cdd:cd07447  78 PCRSTCEALRKRCSHAFDAIQMAWPYFLDCDRFFAGEQEGCYDP 121
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 24-140 2.36e-08

One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ; The cysteine-rich domain (CRD) is an essential component of corin, a type II transmembrane serine protease which functions as the convertase of the pro-atrial natriuretic peptide (pro-ANP) in the heart. Corin contains two CRDs in its extracellular region, which play an important role in recognition of the physiological substrate, pro-ANP. This model characterizes the first (N-terminal) CRD.


Pssm-ID: 143554  Cd Length: 130  Bit Score: 52.24  E-value: 2.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   24 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAILaIEQYEELVDVNCSSVLRFFLCAMYAPICTLEflHDP---IKPCKSV 100
Cdd:cd07445   5 CMNITHSQCQMLPYHSTLKPSLLSVKNMEMEKF-LKFFSYLHRLSCYQHIMLFGCSLALPECISD--GDDrhgLLPCRSF 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 7710094  101 CQRARDDCEPLMKMYNHSWPESLACD------ELPVYDRGVCISPE 140
Cdd:cd07445  82 CEAAKEGCEPVLGMVNASWPDFLRCSqfrnntETAVENRALCFSPQ 127
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 29-137 2.61e-08

Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain (CRD) is an essential part of the variant 3 of collagen XVIII (V3C18), which regulates major cellular functions such as the differential epithelial morphogenesis of early lung and kidney development. V3C18 is a 170 kD protein, which is proteolotically processed into the CRD-containing 50 kD glucoprotein precursor that binds Wnt3a through its CRD domain and suppresses the Wnt3a-induced stabilization of beta catenin. Full-length V3C18 is unable to inhibit Wnt signaling.


Pssm-ID: 143564  Cd Length: 123  Bit Score: 51.74  E-value: 2.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   29 IPMCRHMPWNITRMPNHLHHSTQENAILAIEQYEELVDVNCSSVLRFFLCAMYAPICTLEFLHDPIkPCKSVCQRARDDC 108
Cdd:cd07455  12 LPFCSRLGIRSFWLPNFLNHTSVEEVRAVLAEWAWLLESGCHPSLEWFFCLLLVPSCGGGPPPPPP-PCRQFCEVLQDSC 90

                        90       100
                ....*....|....*....|....*....
gi 7710094  109 EPLMKmyNHSWPesLACDELPVYDRGVCI 137
Cdd:cd07455  91 WNLLE--GGRLP--VACASLPEQEDGYCV 115
NTR_like cd03523
NTR_like domain; a beta barrel with an oligosaccharide/oligonucleotide-binding fold found in ...
 196-285 5.55e-07

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: 47.46  E-value: 5.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094  196 SYVIHAKIKAVQRSgCNEVTTVVDVKEIFKS--LSPIPRTQVPLITNS--SCQCPHILPHQDVLIMCYE--WRSRMMLLE 269
Cdd:cd03523   7 DYVVRAKIKEIKEE-NDDVKYEVKIIKIYKTgkAKADKADLRFYYTAPacCPCHPILNPGREYLIMGKEedSQGGLVLDP 85

                        90
                ....*....|....*.
gi 7710094  270 NCLVEKWRDQLSRRSI 285
Cdd:cd03523  86 LSFVEPWSPLSLRQDR 101
CRD_SMO cd07451
Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The ...
 48-134 2.12e-04

Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The cysteine-rich domain (CRD) is part of the smoothened receptor (Smo), an integral membrane protein and one of the key players in the Hedgehog (Hh) signaling pathway, critical for development, cell growth and migration, as well as stem cell maintenance. The CRD of Smo is conserved in vertebrates and can also be identified in invertebrates. The precise function of the CRD in Smo is unknown. Mutations in the Drosophila CRD disrupt Smo activity in vivo, while deletion of the CRD in mammalian cells does not seem to affect the activity of overexpressed Smo.


Pssm-ID: 143560  Cd Length: 132  Bit Score: 40.81  E-value: 2.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094   48 HSTQENAILAIEQYEELVDV-NCSSVLRFFLCAMYAPIC---TLEFlhdpikPCKSVCQRARDDCEPLmkmYNHS-WPES 122
Cdd:cd07451  31 STTQEEVQEKLHLWSGLRNVpKCWAVIQPLLCALYMPKCengKVEL------PSQEMCQATRGPCKIV---ENERgWPDF 101

                        90
                ....*....|..
gi 7710094  123 LACDELPVYDRG 134
Cdd:cd07451 102 LRCDNDRFPPRG 113
C345C smart00643
Netrin C-terminal Domain;
189-296 9.03e-04

Netrin C-terminal Domain;


Pssm-ID: 214759  Cd Length: 114  Bit Score: 38.50  E-value: 9.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094     189 TYLSKNYSYVIHAKIKAVQRSGcNEVTTVVDVKEIFKS-LSPIPR---TQVPLITNSSCQCPHIL-PHQDVLIM------ 257
Cdd:smart00643   3 KACKSDVDYVYKVKVLSVEEEG-GFDKYTVKILEVIKSgTDELVRgknKLRVFISRASCRCPLLLkLGKSYLIMgksgdl 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 7710094     258 -CYEWRSRMMLLENCLVEKWRDqlsrrsiQWEERLQEQQR 296
Cdd:smart00643  82 wDAKGRGQYVLGKNSWVEEWPT-------EEECRLRRLQK 114
NTR_netrin-1_like cd03579
NTR domain, Netrin-1-like subfamily; The C-terminal NTR domain of netrins is also called ...
 197-296 2.01e-03

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: 37.61  E-value: 2.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710094  197 YVIHAKIKAVQRSGcNEVTTVVDVKEIFK-SLSPIPRTQVPLI---TNSSCQCPHILPHQDVLIMCYE----WRSRMMLL 268
Cdd:cd03579   9 YAVQAQVLSRETAG-EWAKFTVNVQTVYKrGTSRLRRGDQPLWvprKDLACKCPKLKVGKSYLLLGKDedspERGGLILD 87

                        90       100
                ....*....|....*....|....*...
gi 7710094  269 ENCLVEKWRDQLSRRSiqweERLQEQQR 296
Cdd:cd03579  88 KRSLVIEWRDEWARRL----RRFQRRER 111
 
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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