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Conserved domains on  [gi|29244926|ref|NP_006578|]
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atrial natriuretic peptide-converting enzyme isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 802-1033 2.36e-84

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


:

Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 272.23  E-value: 2.36e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  802 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGReNAAVWKVVLGINNLDHPSVFMQTRFVKTIILH 881
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  882 PRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMGNKM--PFKLQEGEVRIISLEHCQS-Y 958
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGplPDVLQEVNVPIVSNAECKRaY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29244926  959 FDMKTITTRMICAGYESGTVDSCMGDSGGPLVCEKPgGRWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVEWIKRQ 1033
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGC-ARPNYPGVYTRVSSYLDWIQKT 232
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 454-575 2.72e-83

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: 264.96  E-value: 2.72e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07888    1 QCEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCLMPDE 575
Cdd:cd07888   81 RNSKERCESVLGIVGLQWPEDTDCAQFPEENSDNQTCLLPDE 122
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 135-263 8.46e-76

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: 244.84  E-value: 8.46e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  135 NTSACMNITHSQCQMLPYHATLTPLLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDSHGLLPCRS 214
Cdd:cd07445    1 NTSACMNITHSQCQMLPYHSTLKPSLLSVKNMEMEKFLKFFSYLHRLSCYQHIMLFGCSLALPECISDGDDRHGLLPCRS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 29244926  215 FCEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTESSNVSR-ICFSPQQEN 263
Cdd:cd07445   81 FCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVENRaLCFSPQQER 130
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
347-377 7.88e-09

Low-density lipoprotein receptor domain class A;


:

Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 7.88e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 29244926    347 EHRCGDGRCIAMEWVCDGDHDCVDKSDEVNC 377
Cdd:pfam00057    7 EFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 580-614 1.59e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 1.59e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  580 CSPSHFKCRSGQCVLASRRCDGQADCDDDSDEENC 614
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 306-340 1.96e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 1.96e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  306 CSENLFHCHTGKCLNYSLVCDGYDDCGDLSDEQNC 340
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 387-414 2.68e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.67  E-value: 2.68e-08
                         10        20
                 ....*....|....*....|....*...
gi 29244926  387 CRNGQCIPSTFQCDGDEDCKDGSDEENC 414
Cdd:cd00112    8 CANGRCIPSSWVCDGEDDCGDGSDEENC 35
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 690-786 8.31e-08

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


:

Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 51.19  E-value: 8.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     690 VTLSINVNSSS-FLMVHRAATEHHVCADGWQEILSQLACKQMGLGEPSVTKL-IQEQEKEPRWLTLHSNWESLNgTTLHE 767
Cdd:smart00202    1 VRLVGGGSPCEgRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsAYFGPGSGPIWLDNVRCSGTE-ASLSD 79

                            90       100
                    ....*....|....*....|..
gi 29244926     768 LLVNGQ---SCESRSKISLLCT 786
Cdd:smart00202   80 CPHSGWgshNCSHGEDAGVVCS 101
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 655-689 1.21e-07

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 48.74  E-value: 1.21e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  655 CQDDELECANHACVSRDLWCDGEADCSDSSDEWDC 689
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 269-304 1.95e-07

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


:

Pssm-ID: 238060  Cd Length: 35  Bit Score: 47.97  E-value: 1.95e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 29244926  269 CGRGEnFLCASGICIPGKLQCNGYNDCDDWSDEAHC 304
Cdd:cd00112    1 CPPNE-FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 802-1033 2.36e-84

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 272.23  E-value: 2.36e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  802 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGReNAAVWKVVLGINNLDHPSVFMQTRFVKTIILH 881
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  882 PRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMGNKM--PFKLQEGEVRIISLEHCQS-Y 958
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGplPDVLQEVNVPIVSNAECKRaY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29244926  959 FDMKTITTRMICAGYESGTVDSCMGDSGGPLVCEKPgGRWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVEWIKRQ 1033
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGC-ARPNYPGVYTRVSSYLDWIQKT 232
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 454-575 2.72e-83

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: 264.96  E-value: 2.72e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07888    1 QCEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCLMPDE 575
Cdd:cd07888   81 RNSKERCESVLGIVGLQWPEDTDCAQFPEENSDNQTCLLPDE 122
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 801-1030 1.92e-81

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 264.15  E-value: 1.92e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     801 RILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGReNAAVWKVVLGINNLDHPSvFMQTRFVKTIIL 880
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     881 HPRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMGN---KMPFKLQEGEVRIISLEHCQS 957
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgagSLPDTLQEVNVPIVSNATCRR 158

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29244926     958 -YFDMKTITTRMICAGYESGTVDSCMGDSGGPLVCEkpGGRWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVEWI 1030
Cdd:smart00020  159 aYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGC-ARPGKPGVYTRVSSYLDWI 229
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 135-263 8.46e-76

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: 244.84  E-value: 8.46e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  135 NTSACMNITHSQCQMLPYHATLTPLLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDSHGLLPCRS 214
Cdd:cd07445    1 NTSACMNITHSQCQMLPYHSTLKPSLLSVKNMEMEKFLKFFSYLHRLSCYQHIMLFGCSLALPECISDGDDRHGLLPCRS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 29244926  215 FCEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTESSNVSR-ICFSPQQEN 263
Cdd:cd07445   81 FCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVENRaLCFSPQQER 130
Trypsin pfam00089
Trypsin;
802-1030 4.64e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.38  E-value: 4.64e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    802 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGRENaavWKVVLGINNLDHPSVFMQTRFVKTIILH 881
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    882 PRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMG-NKMPFKLQEGEVRIISLEHCQSYFD 960
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKtLGPSDTLQEVTVPVVSRETCRSAYG 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    961 mKTITTRMICAGYesGTVDSCMGDSGGPLVCEKPggrwTLFGLTSWGSVCfSKVLGPGVYSNVSYFVEWI 1030
Cdd:pfam00089  158 -GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGC-ASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 794-1034 9.48e-62

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.05  E-value: 9.48e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  794 PAARMNKRILGGRTSRPGRWPWQCSLQSE--PSGHICGCVLIAKKWVLTVAHCFEGRENAAVwKVVLGINNLDHPSVfmQ 871
Cdd:COG5640   23 PAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGG--T 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  872 TRFVKTIILHPRYSRAVVDYDISIVELSEDISEtgyVRPVCLPNPEQWLEPDTYCYITGWGHMGN---KMPFKLQEGEVR 948
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEgpgSQSGTLRKADVP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  949 IISLEHCQSYFDMktITTRMICAGYESGTVDSCMGDSGGPLVcEKPGGRWTLFGLTSWG-SVCFSKvlGPGVYSNVSYFV 1027
Cdd:COG5640  177 VVSDATCAAYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGgGPCAAG--YPGVYTRVSAYR 251


                 ....*..
gi 29244926 1028 EWIKRQI 1034
Cdd:COG5640  252 DWIKSTA 258
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 455-562 4.16e-31

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: 118.05  E-value: 4.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWES---SLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEH--IPPC 529
Cdd:pfam01392    1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYlvlSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKpvCPPC 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 29244926    530 RALCEHSKERCESVLGIV--GLQWPEDTDCSQFPE 562
Cdd:pfam01392   81 RSLCEEVRYGCEPLLEEAkfGFSWPEFLDCDSLPA 115
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 455-564 1.80e-26

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: 104.70  E-value: 1.80e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVntGEH-IPPCRALC 533
Cdd:smart00063    1 CEPITIPLCKDLGYNLTSMPNLLGHTTQEEAGL--ELEQFHPLLNVQCSPDLRFFLCSVYAPICTE--DLRpILPCRSLC 76

                            90       100       110
                    ....*....|....*....|....*....|.
gi 29244926     534 EHSKERCESVLGIVGLQWPEDTDCSQFPEEN 564
Cdd:smart00063   77 EAAREGCEPLMEKFGFPWPEFLRCDRFPVQE 107
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 139-246 7.25e-23

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: 94.56  E-value: 7.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    139 CMNITHSQCQMLPYHATLTPLLSVVRNMEMEKFLKFFTYLH------RLSCYQHIMLFGCTLAFPECIIDGDDSHGLLPC 212
Cdd:pfam01392    1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYLVLSefeplvDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCPPC 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 29244926    213 RSFCEAAKEGCESVLGMVNY--SWPDFLRCSQFRNQ 246
Cdd:pfam01392   81 RSLCEEVRYGCEPLLEEAKFgfSWPEFLDCDSLPAD 116
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 139-243 2.82e-15

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: 72.73  E-value: 2.82e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     139 CMNITHSQCQMLPYHATLTPLLSVVRNM-EMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECiidGDDSHGLLPCRSFCE 217
Cdd:smart00063    1 CEPITIPLCKDLGYNLTSMPNLLGHTTQeEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPIC---TEDLRPILPCRSLCE 77

                            90       100
                    ....*....|....*....|....*.
gi 29244926     218 AAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:smart00063   78 AAREGCEPLMEKFGFPWPEFLRCDRF 103
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
347-377 7.88e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 7.88e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 29244926    347 EHRCGDGRCIAMEWVCDGDHDCVDKSDEVNC 377
Cdd:pfam00057    7 EFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 344-377 1.16e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.44  E-value: 1.16e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 29244926  344 PTTEHRCGDGRCIAMEWVCDGDHDCVDKSDEVNC 377
Cdd:cd00112    2 PPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 580-614 1.59e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 1.59e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  580 CSPSHFKCRSGQCVLASRRCDGQADCDDDSDEENC 614
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 306-340 1.96e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 1.96e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  306 CSENLFHCHTGKCLNYSLVCDGYDDCGDLSDEQNC 340
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
580-614 2.20e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 50.71  E-value: 2.20e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 29244926    580 CSPSHFKCRSGQCVLASRRCDGQADCDDDSDEENC 614
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 387-414 2.68e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.67  E-value: 2.68e-08
                         10        20
                 ....*....|....*....|....*...
gi 29244926  387 CRNGQCIPSTFQCDGDEDCKDGSDEENC 414
Cdd:cd00112    8 CANGRCIPSSWVCDGEDDCGDGSDEENC 35
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 690-786 8.31e-08

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 51.19  E-value: 8.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     690 VTLSINVNSSS-FLMVHRAATEHHVCADGWQEILSQLACKQMGLGEPSVTKL-IQEQEKEPRWLTLHSNWESLNgTTLHE 767
Cdd:smart00202    1 VRLVGGGSPCEgRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsAYFGPGSGPIWLDNVRCSGTE-ASLSD 79

                            90       100
                    ....*....|....*....|..
gi 29244926     768 LLVNGQ---SCESRSKISLLCT 786
Cdd:smart00202   80 CPHSGWgshNCSHGEDAGVVCS 101
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 655-689 1.21e-07

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 48.74  E-value: 1.21e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  655 CQDDELECANHACVSRDLWCDGEADCSDSSDEWDC 689
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
387-414 1.49e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.40  E-value: 1.49e-07
                           10        20
                   ....*....|....*....|....*...
gi 29244926    387 CRNGQCIPSTFQCDGDEDCKDGSDEENC 414
Cdd:pfam00057   10 CGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 269-304 1.95e-07

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 47.97  E-value: 1.95e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 29244926  269 CGRGEnFLCASGICIPGKLQCNGYNDCDDWSDEAHC 304
Cdd:cd00112    1 CPPNE-FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
269-304 3.01e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 47.63  E-value: 3.01e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 29244926    269 CGRGEnFLCASGICIPGKLQCNGYNDCDDWSDEAHC 304
Cdd:pfam00057    3 CSPNE-FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
306-340 3.52e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 47.24  E-value: 3.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 29244926    306 CSENLFHCHTGKCLNYSLVCDGYDDCGDLSDEQNC 340
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 344-374 5.27e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.86  E-value: 5.27e-07
                            10        20        30
                    ....*....|....*....|....*....|.
gi 29244926     344 PTTEHRCGDGRCIAMEWVCDGDHDCVDKSDE 374
Cdd:smart00192    3 PPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 306-337 9.96e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.09  E-value: 9.96e-07
                            10        20        30
                    ....*....|....*....|....*....|..
gi 29244926     306 CSENLFHCHTGKCLNYSLVCDGYDDCGDLSDE 337
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 579-611 1.15e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 45.70  E-value: 1.15e-06
                            10        20        30
                    ....*....|....*....|....*....|...
gi 29244926     579 ECSPSHFKCRSGQCVLASRRCDGQADCDDDSDE 611
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 387-411 1.19e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 45.70  E-value: 1.19e-06
                            10        20
                    ....*....|....*....|....*
gi 29244926     387 CRNGQCIPSTFQCDGDEDCKDGSDE 411
Cdd:smart00192    9 CDNGRCIPSSWVCDGVDDCGDGSDE 33
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 713-794 5.15e-06

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 46.17  E-value: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    713 VCADGWQEILSQLACKQMGLGEPSVTKLIQ----EQEKEPRWLTLHSnweSLNGTTLHELLVNGQSCESRSKISLLCTkq 788
Cdd:pfam15494   19 VCSDDWNPAYGRAACQQLGYLRLTHHKSVNltdiSSNSSQSFMKLNS---SSLNTDLYEALQPRDSCSSGSVVSLRCS-- 93


                   ....*.
gi 29244926    789 DCGRRP 794
Cdd:pfam15494   94 ECGLRS 99
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 269-301 1.92e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 42.24  E-value: 1.92e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 29244926     269 CGRGEnFLCASGICIPGKLQCNGYNDCDDWSDE 301
Cdd:smart00192    2 CPPGE-FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 655-686 2.39e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 42.24  E-value: 2.39e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 29244926     655 CQDDELECANHACVSRDLWCDGEADCSDSSDE 686
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
655-689 9.64e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 9.64e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 29244926    655 CQDDELECANHACVSRDLWCDGEADCSDSSDEWDC 689
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
 
Name Accession Description Interval E-value
Tryp_SPc cd00190
Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens ...
 802-1033 2.36e-84

Trypsin-like serine protease; Many of these are synthesized as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. Alignment contains also inactive enzymes that have substitutions of the catalytic triad residues.


Pssm-ID: 238113 [Multi-domain]  Cd Length: 232  Bit Score: 272.23  E-value: 2.36e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  802 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGReNAAVWKVVLGINNLDHPSVFMQTRFVKTIILH 881
Cdd:cd00190    1 IVGGSEAKIGSFPWQVSLQYTGGRHFCGGSLISPRWVLTAAHCVYSS-APSNYTVRLGSHDLSSNEGGGQVIKVKKVIVH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  882 PRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMGNKM--PFKLQEGEVRIISLEHCQS-Y 958
Cdd:cd00190   80 PNYNPSTYDNDIALLKLKRPVTLSDNVRPICLPSSGYNLPAGTTCTVSGWGRTSEGGplPDVLQEVNVPIVSNAECKRaY 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29244926  959 FDMKTITTRMICAGYESGTVDSCMGDSGGPLVCEKPgGRWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVEWIKRQ 1033
Cdd:cd00190  160 SYGGTITDNMLCAGGLEGGKDACQGDSGGPLVCNDN-GRGVLVGIVSWGSGC-ARPNYPGVYTRVSSYLDWIQKT 232
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 454-575 2.72e-83

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: 264.96  E-value: 2.72e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07888    1 QCEPITLELCMNLPYNTTRYPNYLGHRTQKEASISWESSLFPALVQTNCYKYLMFFACTILVPKCDPVTQQRIPPCRSLC 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCLMPDE 575
Cdd:cd07888   81 RNSKERCESVLGIVGLQWPEDTDCAQFPEENSDNQTCLLPDE 122
Tryp_SPc smart00020
Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens ...
 801-1030 1.92e-81

Trypsin-like serine protease; Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.


Pssm-ID: 214473  Cd Length: 229  Bit Score: 264.15  E-value: 1.92e-81
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     801 RILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGReNAAVWKVVLGINNLDHPSvFMQTRFVKTIIL 880
Cdd:smart00020    1 RIVGGSEANIGSFPWQVSLQYGGGRHFCGGSLISPRWVLTAAHCVRGS-DPSNIRVRLGSHDLSSGE-EGQVIKVSKVII 78

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     881 HPRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMGN---KMPFKLQEGEVRIISLEHCQS 957
Cdd:smart00020   79 HPNYNPSTYDNDIALLKLKEPVTLSDNVRPICLPSSNYNVPAGTTCTVSGWGRTSEgagSLPDTLQEVNVPIVSNATCRR 158

                           170       180       190       200       210       220       230
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29244926     958 -YFDMKTITTRMICAGYESGTVDSCMGDSGGPLVCEkpGGRWTLFGLTSWGSVCfSKVLGPGVYSNVSYFVEWI 1030
Cdd:smart00020  159 aYSGGGAITDNMLCAGGLEGGKDACQGDSGGPLVCN--DGRWVLVGIVSWGSGC-ARPGKPGVYTRVSSYLDWI 229
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 135-263 8.46e-76

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: 244.84  E-value: 8.46e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  135 NTSACMNITHSQCQMLPYHATLTPLLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDSHGLLPCRS 214
Cdd:cd07445    1 NTSACMNITHSQCQMLPYHSTLKPSLLSVKNMEMEKFLKFFSYLHRLSCYQHIMLFGCSLALPECISDGDDRHGLLPCRS 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 29244926  215 FCEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTESSNVSR-ICFSPQQEN 263
Cdd:cd07445   81 FCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVENRaLCFSPQQER 130
Trypsin pfam00089
Trypsin;
802-1030 4.64e-62

Trypsin;


Pssm-ID: 459667 [Multi-domain]  Cd Length: 219  Bit Score: 210.38  E-value: 4.64e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    802 ILGGRTSRPGRWPWQCSLQSEPSGHICGCVLIAKKWVLTVAHCFEGRENaavWKVVLGINNLDHPSVFMQTRFVKTIILH 881
Cdd:pfam00089    1 IVGGDEAQPGSFPWQVSLQLSSGKHFCGGSLISENWVLTAAHCVSGASD---VKVVLGAHNIVLREGGEQKFDVEKIIVH 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    882 PRYSRAVVDYDISIVELSEDISETGYVRPVCLPNPEQWLEPDTYCYITGWGHMG-NKMPFKLQEGEVRIISLEHCQSYFD 960
Cdd:pfam00089   78 PNYNPDTLDNDIALLKLESPVTLGDTVRPICLPDASSDLPVGTTCTVSGWGNTKtLGPSDTLQEVTVPVVSRETCRSAYG 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    961 mKTITTRMICAGYesGTVDSCMGDSGGPLVCEKPggrwTLFGLTSWGSVCfSKVLGPGVYSNVSYFVEWI 1030
Cdd:pfam00089  158 -GTVTDTMICAGA--GGKDACQGDSGGPLVCSDG----ELIGIVSWGYGC-ASGNYPGVYTPVSSYLDWI 219
COG5640 COG5640
Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, ...
 794-1034 9.48e-62

Secreted trypsin-like serine protease [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444365 [Multi-domain]  Cd Length: 262  Bit Score: 211.05  E-value: 9.48e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  794 PAARMNKRILGGRTSRPGRWPWQCSLQSE--PSGHICGCVLIAKKWVLTVAHCFEGRENAAVwKVVLGINNLDHPSVfmQ 871
Cdd:COG5640   23 PAADAAPAIVGGTPATVGEYPWMVALQSSngPSGQFCGGTLIAPRWVLTAAHCVDGDGPSDL-RVVIGSTDLSTSGG--T 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  872 TRFVKTIILHPRYSRAVVDYDISIVELSEDISEtgyVRPVCLPNPEQWLEPDTYCYITGWGHMGN---KMPFKLQEGEVR 948
Cdd:COG5640  100 VVKVARIVVHPDYDPATPGNDIALLKLATPVPG---VAPAPLATSADAAAPGTPATVAGWGRTSEgpgSQSGTLRKADVP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  949 IISLEHCQSYFDMktITTRMICAGYESGTVDSCMGDSGGPLVcEKPGGRWTLFGLTSWG-SVCFSKvlGPGVYSNVSYFV 1027
Cdd:COG5640  177 VVSDATCAAYGGF--DGGTMLCAGYPEGGKDACQGDSGGPLV-VKDGGGWVLVGVVSWGgGPCAAG--YPGVYTRVSAYR 251


                 ....*..
gi 29244926 1028 EWIKRQI 1034
Cdd:COG5640  252 DWIKSTA 258
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 454-575 3.73e-34

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: 126.85  E-value: 3.73e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07066    1 KCEPIPLPLCRGLPYNTTRFPNLLGHESQEEAEQ--ELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRPIPPCRSLC 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEENsDNQTCLMPDE 575
Cdd:cd07066   79 EEVRDSCEPLMLAFGFPWPEPLDCDRFPDSN-EEGLCISPPG 119
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
 454-571 3.23e-31

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: 118.72  E-value: 3.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESslFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07448    3 RCEPIRIEMCQGLGYNVTRMPNLVGHELQTDAELQLQT--FTPLIQYGCSSQLKFFLCSVYVPMCTEKVPVPIGPCRPLC 80

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCL 571
Cdd:cd07448   81 LSVKKRCLPVLKEFGFPWPEALNCSKFPPQNNHNHMCM 118
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 455-562 4.16e-31

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: 118.05  E-value: 4.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWES---SLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEH--IPPC 529
Cdd:pfam01392    1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYlvlSEFEPLVDLSCSPSLRLFLCSLYFPPCTLGPSPKpvCPPC 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 29244926    530 RALCEHSKERCESVLGIV--GLQWPEDTDCSQFPE 562
Cdd:pfam01392   81 RSLCEEVRYGCEPLLEEAkfGFSWPEFLDCDSLPA 115
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
 453-567 1.22e-29

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: 114.05  E-value: 1.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  453 SQCEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVnTGEHIPPCRAL 532
Cdd:cd07458    1 GKCEPITIPLCTDIPYNMTIFPNLLGHTKQEDAGL--EVHQFYPLVKVQCSPDLKFFLCSVYAPVCTV-LERPIPPCRSL 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 29244926  533 CEHSKERCESVLGIVGLQWPEDTDCSQFPEENSDN 567
Cdd:cd07458   78 CESARQGCEALMNKFGFQWPESLDCEKFPVHGAGD 112
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 455-564 1.80e-26

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: 104.70  E-value: 1.80e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVntGEH-IPPCRALC 533
Cdd:smart00063    1 CEPITIPLCKDLGYNLTSMPNLLGHTTQEEAGL--ELEQFHPLLNVQCSPDLRFFLCSVYAPICTE--DLRpILPCRSLC 76

                            90       100       110
                    ....*....|....*....|....*....|.
gi 29244926     534 EHSKERCESVLGIVGLQWPEDTDCSQFPEEN 564
Cdd:smart00063   77 EAAREGCEPLMEKFGFPWPEFLRCDRFPVQE 107
CRD_FZ cd07066
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain; CRD_FZ is an essential ...
 139-261 9.25e-26

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: 102.97  E-value: 9.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTPLLSVVRNM-EMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDShgLLPCRSFCE 217
Cdd:cd07066    2 CEPIPLPLCRGLPYNTTRFPNLLGHESQeEAEQELESFTPLVNSGCHPDLRFFLCSLYFPECTPDGDRP--IPPCRSLCE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 29244926  218 AAKEGCESVLGMVNYSWPDFLRCSQFRNQTESSNvsriCFSPQQ 261
Cdd:cd07066   80 EVRDSCEPLMLAFGFPWPEPLDCDRFPDSNEEGL----CISPPG 119
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 453-571 2.05e-25

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: 102.19  E-value: 2.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  453 SQCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESslFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRAL 532
Cdd:cd07457    1 GKCERITIPMCQGIGYNMTRMPNLLGHESQSEAAISIHE--FAPLVQYGCAEHLRFFLCSLYAPMCTEQVSIPIPACRSM 78

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 29244926  533 CEHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCL 571
Cdd:cd07457   79 CEQARDKCSPIMEQFSFSWPDSLDCDRLPRKNDPKDLCM 117
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 455-575 2.85e-25

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: 101.71  E-value: 2.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALCE 534
Cdd:cd07456    2 CEEITIPMCKGIGYNMTYMPNQFNHDTQEEAGL--EVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYDKPLPPCRSVCE 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 29244926  535 HSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCLMPDE 575
Cdd:cd07456   80 RARDGCAPIMRQYGFAWPERMSCDALPEGGDPDNLCMDRNN 120
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 453-575 1.67e-24

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: 99.71  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  453 SQCEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRAL 532
Cdd:cd07463    3 AKCQPVVIPMCRGIGYNLTRMPNFLGHDSQREAAI--KLNEFAPLVEYGCHVHLRFFLCSLYAPMCTDQVSTSIPACRPM 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 29244926  533 CEHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCLMPDE 575
Cdd:cd07463   81 CEQARQKCSPIMEQFNFGWPESLDCSRLPTRNDPNALCMEAPE 123
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 454-571 1.81e-24

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: 99.71  E-value: 1.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESslFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07462    4 RCQPIEIPMCKDIGYNMTRMPNLMGHENQREAAIQLHE--FAPLVEYGCHSHLKFFLCSLYAPMCTEQVSTPIPACRVMC 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCL 571
Cdd:cd07462   82 EQARLKCSPIMEQFNFKWPDSLDCSKLPNKNDPNYLCM 119
Fz pfam01392
Fz domain; Also known as the CRD (cysteine rich domain), the C6 box in MuSK receptor. This ...
 139-246 7.25e-23

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: 94.56  E-value: 7.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    139 CMNITHSQCQMLPYHATLTPLLSVVRNMEMEKFLKFFTYLH------RLSCYQHIMLFGCTLAFPECIIDGDDSHGLLPC 212
Cdd:pfam01392    1 CEPITLPMCLGLGYNATVFPNLLGHQTQEEAELSLAYLVLSefeplvDLSCSPSLRLFLCSLYFPPCTLGPSPKPVCPPC 80

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 29244926    213 RSFCEAAKEGCESVLGMVNY--SWPDFLRCSQFRNQ 246
Cdd:pfam01392   81 RSLCEEVRYGCEPLLEEAKFgfSWPEFLDCDSLPAD 116
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
 455-562 1.16e-22

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: 94.31  E-value: 1.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESslFPALVQTNCYKYLMFFSCTILVPKCdVNTGEHIPPCRALCE 534
Cdd:cd07449    5 CEPITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEP--FHPMVNLECSRDFRPFLCALYAPVC-MEYGRVTLPCRRLCQ 81

                         90       100
                 ....*....|....*....|....*...
gi 29244926  535 HSKERCESVLGIVGLQWPEDTDCSQFPE 562
Cdd:cd07449   82 RAYSECSKLMEMFGVPWPEDMECSRFPD 109
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 455-571 4.23e-22

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: 92.84  E-value: 4.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVnTGEHIPPCRALCE 534
Cdd:cd07464    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGL--EVHQFYPLVKVQCSLELRFFLCSMYAPVCTV-LEQAIPPCRSICE 81

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 29244926  535 HSKERCESVLGIVGLQWPEDTDCSQFPEENSDnQTCL 571
Cdd:cd07464   82 RARQGCEALMNKFGFQWPERLRCENFPRHGAE-QICV 117
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 455-561 1.20e-21

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: 91.69  E-value: 1.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVnTGEHIPPCRALCE 534
Cdd:cd07466    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGL--EVHQFYPLVKVQCSPELKFFLCSMYAPVCTV-LEQAIPPCRSLCE 81

                         90       100
                 ....*....|....*....|....*..
gi 29244926  535 HSKERCESVLGIVGLQWPEDTDCSQFP 561
Cdd:cd07466   82 RARQGCEALMNKFGFQWPERLRCENFP 108
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 454-571 1.43e-21

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: 91.20  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07461    4 QCQEITVPLCKGIGYNYTYMPNQFNHDTQDEAGL--EVHQFWPLVEIQCSPDLKFFLCSMYTPICLEDYKKPLPPCRSVC 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCL 571
Cdd:cd07461   82 ERAKAGCAPLMRQYGFPWPDRMRCDLLPEQGNPDTLCM 119
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 455-571 4.47e-21

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: 90.08  E-value: 4.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALCE 534
Cdd:cd07460    5 CQEITVPMCKGIGYNLTYMPNQFNHDTQDEAGL--EVHQFWPLVEIQCSPDLRFFLCSMYTPICLPDYRKPLPPCRSVCE 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 29244926  535 HSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQTCL 571
Cdd:cd07460   83 RAKAGCSPLMRQYGFAWPERMNCDRLPVLGDPETLCM 119
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 452-577 4.54e-21

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: 89.72  E-value: 4.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  452 CSQCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESslFPALVQTNCYKYLMFFSCTILVPKCDVN-TGEHIPPCR 530
Cdd:cd07441    1 AASCEPVRIPMCKSMPWNMTKMPNHLHHSTQANAVLAIEQ--FEGLLGTQCSPDLLFFLCAMYAPICTIDfQHEPIKPCK 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 29244926  531 ALCEHSKERCESVLGIVGLQWPEDTDCSQFPEenSDNQTCLMPDEYV 577
Cdd:cd07441   79 SVCERARAGCEPVLIRYRHTWPESLACEELPV--YDRGVCISPEAIV 123
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 455-561 7.00e-21

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: 89.34  E-value: 7.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASIswESSLFPALVQTNCYKYLMFFSCTILVPKCDVnTGEHIPPCRALCE 534
Cdd:cd07465    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGL--EVHQFYPLVKVQCSAELKFFLCSMYAPVCTV-LEQALPPCRSLCE 81

                         90       100
                 ....*....|....*....|....*..
gi 29244926  535 HSKERCESVLGIVGLQWPEDTDCSQFP 561
Cdd:cd07465   82 RARQGCEALMNKFGFQWPDTLRCEKFP 108
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 453-573 4.06e-18

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: 81.49  E-value: 4.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  453 SQCEPI--TLELCMNLPYNSTSYPNYFGHRTQKEAsISWESSLFPaLVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCR 530
Cdd:cd07446    3 SNCKPIpaNMLLCHGIEYTNMRLPNLLGHETMKEV-LQQAGSWIP-LVQKQCHPDTKKFLCSLFAPVCLDDLDEAIQPCR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 29244926  531 ALCEHSKERCESVLGIVGLQWPEDTDCSQFPEensDNQTCLMP 573
Cdd:cd07446   81 SLCEAVKDGCAPVMSAFGFPWPDMLDCTRFPL---DNDLCIPP 120
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 454-577 1.21e-17

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: 80.21  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFghRTQKEASISWESSLFPALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07454    4 KCIPIDIELCKDLPYNYTYFPNTI--LHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMCPIGMPQAVTSCKSVC 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEENSdnqTCLMPDEYV 577
Cdd:cd07454   82 EQVKADCFSILEEFGIGWPEPLNCAQFPDPPE---LCMKPTEDE 122
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 455-579 1.55e-17

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: 79.69  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESslFPALVQTNCYKYLMFFSCTILVPKCDVN-TGEHIPPCRALC 533
Cdd:cd07442    5 CEAVRIPMCRHMPWNITRMPNHLHHSTQENAVLAIEQ--YEELVDTGCSPVLPFFLCAMYAPICTLEfLYDPIKPCRSVC 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 29244926  534 EHSKERCESVLGIVGLQWPEDTDCSQFPEenSDNQTCLMPDEYVEE 579
Cdd:cd07442   83 QRARDGCEPIMRRYNHSWPESLACDDLPV--YDRGVCISPEAIVTD 126
CRD_corin_1 cd07445
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 451-569 5.23e-16

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: 75.35  E-value: 5.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  451 NCSQCEPITLELCMNLPYNSTSYPNYFGHRtqkeaSISWESSL--FPALVQTNCYKYLMFFSCTILVPKC--DVNTGEHI 526
Cdd:cd07445    1 NTSACMNITHSQCQMLPYHSTLKPSLLSVK-----NMEMEKFLkfFSYLHRLSCYQHIMLFGCSLALPECisDGDDRHGL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 29244926  527 PPCRALCEHSKERCESVLGIVGLQWPEDTDCSQFPEENSDNQT 569
Cdd:cd07445   76 LPCRSFCEAAKEGCEPVLGMVNASWPDFLRCSQFRNNTETAVE 118
CRD_corin_2 cd07888
One of two cysteine-rich domains of the corin protein, a type II transmembrane serine protease ...
 139-261 1.35e-15

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: 74.28  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTPLLSVVRNMEMEKFL---KFFTYLHRLSCYQHIMLFGCTLAFPECiiDGDDSHGLLPCRSF 215
Cdd:cd07888    2 CEPITLELCMNLPYNTTRYPNYLGHRTQKEASISwesSLFPALVQTNCYKYLMFFACTILVPKC--DPVTQQRIPPCRSL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 29244926  216 CEAAKEGCESVLGMVNYSWPDFLRCSQFrnqTESSNVSRICFSPQQ 261
Cdd:cd07888   80 CRNSKERCESVLGIVGLQWPEDTDCAQF---PEENSDNQTCLLPDE 122
FRI smart00063
Frizzled; Drosophila melanogaster frizzled mediates signalling that polarises a precursor cell ...
 139-243 2.82e-15

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: 72.73  E-value: 2.82e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     139 CMNITHSQCQMLPYHATLTPLLSVVRNM-EMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECiidGDDSHGLLPCRSFCE 217
Cdd:smart00063    1 CEPITIPLCKDLGYNLTSMPNLLGHTTQeEAGLELEQFHPLLNVQCSPDLRFFLCSVYAPIC---TEDLRPILPCRSLCE 77

                            90       100
                    ....*....|....*....|....*.
gi 29244926     218 AAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:smart00063   78 AAREGCEPLMEKFGFPWPEFLRCDRF 103
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
 455-561 8.75e-15

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: 72.11  E-value: 8.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  455 CEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWESslFPALVQTNCYKYLMFFSCTILVPKCDVNTGEhIPPCRALCE 534
Cdd:cd07450    5 CEPITVPRCLKMPYNMTFFPNLMGHYDQDIAAVEMEP--FLPLANLRCSPNVHTFLCQAFVPTCTEQIHV-VRPCRELCE 81

                         90       100
                 ....*....|....*....|....*..
gi 29244926  535 HSKERCESVLGIVGLQWPEDTDCSQFP 561
Cdd:cd07450   82 KVYSDCKKLIDTFGISWPEELECDRLQ 108
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 453-573 2.67e-13

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: 67.98  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  453 SQCEPITLE--LCMNLPYNSTSYPNYFGHRTQKEASISweSSLFPALVQTNCYKYLMFFSCTILVPKCdvnTGEHIPPCR 530
Cdd:cd07452    7 TKCVPIPPEmsMCQDVGYSEMRLPNLLGHTSMAEVVPK--SADWQTLLHTGCHPHARTFLCSLFAPVC---LDTFIQPCR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 29244926  531 ALCEHSKERCESVLGIVGLQWPEDTDCSQFPEENSDnqtCLMP 573
Cdd:cd07452   82 SMCVAVRDSCAPVLACHGHSWPESLDCDRFPAGEDM---CLAS 121
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
 454-560 2.77e-13

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: 67.47  E-value: 2.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  454 QCEPITLELCMNLPYNSTSYPNYFGHRTQKEASISWES---SLFPALVQTNCYKYLMFFSCTILVPKCDvnTGEHIPPCR 530
Cdd:cd07447    3 TCTDLLLSYCSDVSYTQTTFPNLLGHRSREVTEAGAEYlllSVLHGLLGGECNPDIRLLGCSVLAPRCE--NDKVIKPCR 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 29244926  531 ALCEHSKERCESVLGIVGLQWPEDTDCSQF 560
Cdd:cd07447   81 STCEALRKRCSHAFDAIQMAWPYFLDCDRF 110
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 457-563 3.89e-13

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: 67.23  E-value: 3.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  457 PITLELCMNLPYNSTSYPNYFGHRTQKEasISWESSLFPALVQTNCYKYLMFFSCTILVPKCdvnTGEHIPPCRALCEHS 536
Cdd:cd07443   11 PADLRLCHNVGYKKMVLPNLLDHETMAE--VKQQASSWVPLLNKNCHKGTQVFLCSLFAPVC---LDRPVYPCRWLCEAV 85

                         90       100
                 ....*....|....*....|....*..
gi 29244926  537 KERCESVLGIVGLQWPEDTDCSQFPEE 563
Cdd:cd07443   86 RDSCEPVMQFFGFYWPEMLKCDKFPEG 112
CRD_FZ4 cd07448
Cysteine-rich Wnt-binding domain of the frizzled 4 (Fz4) receptor; The cysteine-rich domain ...
 139-265 5.57e-12

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: 64.02  E-value: 5.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTP-LLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDSHGllPCRSFCE 217
Cdd:cd07448    4 CEPIRIEMCQGLGYNVTRMPnLVGHELQTDAELQLQTFTPLIQYGCSSQLKFFLCSVYVPMCTEKVPVPIG--PCRPLCL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 29244926  218 AAKEGCESVLGMVNYSWPDFLRCSQFRNQtesSNVSRICFSPQQENGK 265
Cdd:cd07448   82 SVKKRCLPVLKEFGFPWPEALNCSKFPPQ---NNHNHMCMEGPGDEEV 126
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 453-571 9.04e-12

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: 63.43  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  453 SQCE--PITLELCMNLPYNSTSYPNYFGHRTQKEASiSWESSLFPALVQtNCYKYLMFFSCTILVPKCdvnTGEHIPPCR 530
Cdd:cd07444    5 PQCVdiPADLPLCHNVGYKRMRLPNLLEHESMAEVK-QQASSWVPLLAK-RCHADTQVFLCSLFAPVC---LDRPIYPCR 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 29244926  531 ALCEHSKERCESVLGIVGLQWPEDTDCSQFPeenSDNQTCL 571
Cdd:cd07444   80 SLCEAVRDSCAPVMESYGFPWPEMLHCHKFP---LDNDLCI 117
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 457-589 2.69e-11

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: 62.27  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  457 PITLELCMNLPYNSTSYPNYFGHRTQKEAsISWESSLFPaLVQTNCYKYLMFFSCTILVPKCdvnTGEHIPPCRALCEHS 536
Cdd:cd07453    7 PKSMALCYDIGYSEMRIPNLLEHETMAEV-IQQSSSWLP-LLARECHPDARIFLCSLFAPIC---WDRPIYPCRSLCEAV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 29244926  537 KERCESVLGIVGLQWPEDTDCSQFPEensDNQTCLMPdEYVEECSPSHFKCRS 589
Cdd:cd07453   82 RSSCAPLMACYGYPWPEILHCDKFPV---DHDLCISP-QFIDTLSPERVKPRA 130
CRD_FZ3 cd07449
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 3 (Fz3) receptor; The cysteine-rich ...
 138-249 3.43e-11

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: 61.56  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  138 ACMNITHSQCQMLPYHATLTP-LLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDShglLPCRSFC 216
Cdd:cd07449    4 SCEPITLRMCQDLPYNTTFMPnLLNHYDQQTAALAMEPFHPMVNLECSRDFRPFLCALYAPVCMEYGRVT---LPCRRLC 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 29244926  217 EAAKEGCESVLGMVNYSWPDFLRCSQFRNQTES 249
Cdd:cd07449   81 QRAYSECSKLMEMFGVPWPEDMECSRFPDCDEP 113
CRD_FZ1_like cd07458
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 1; The cysteine-rich ...
 139-243 6.68e-11

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: 60.50  E-value: 6.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTP-LLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDgddSHGLLPCRSFCE 217
Cdd:cd07458    3 CEPITIPLCTDIPYNMTIFPnLLGHTKQEDAGLEVHQFYPLVKVQCSPDLKFFLCSVYAPVCTVL---ERPIPPCRSLCE 79

                         90       100
                 ....*....|....*....|....*.
gi 29244926  218 AAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07458   80 SARQGCEALMNKFGFQWPESLDCEKF 105
CRD_LIN_17 cd07454
Cysteine-rich domain (CRD) of LIN_17; A cysteine-rich domain (CRD) is an essential component ...
 139-265 1.31e-09

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: 57.10  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTP-LLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECiiDGDDSHGLLPCRSFCE 217
Cdd:cd07454    5 CIPIDIELCKDLPYNYTYFPnTILHNDQHTLQTHTEHFKPLMKTKCHPHIHFFICSVFAPMC--PIGMPQAVTSCKSVCE 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 29244926  218 AAKEGCESVLGMVNYSWPDFLRCSQFRNQTEssnvsrICFSPQQENGK 265
Cdd:cd07454   83 QVKADCFSILEEFGIGWPEPLNCAQFPDPPE------LCMKPTEDEIT 124
CRD_FZ2 cd07464
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 2 (Fz2) receptor; The cysteine-rich ...
 139-243 2.34e-09

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: 56.25  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTPLLSVVRNMEMEKF-LKFFTYLHRLSCYQHIMLFGCTLAFPECIIDgddSHGLLPCRSFCE 217
Cdd:cd07464    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLeVHQFYPLVKVQCSLELRFFLCSMYAPVCTVL---EQAIPPCRSICE 81

                         90       100
                 ....*....|....*....|....*.
gi 29244926  218 AAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07464   82 RARQGCEALMNKFGFQWPERLRCENF 107
CRD_FZ7 cd07466
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 7 (Fz7) receptor; The cysteine-rich ...
 139-243 2.96e-09

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: 56.25  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTPLLSVVRNMEMEKF-LKFFTYLHRLSCYQHIMLFGCTLAFPECIIDgddSHGLLPCRSFCE 217
Cdd:cd07466    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLeVHQFYPLVKVQCSPELKFFLCSMYAPVCTVL---EQAIPPCRSLCE 81

                         90       100
                 ....*....|....*....|....*.
gi 29244926  218 AAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07466   82 RARQGCEALMNKFGFQWPERLRCENF 107
CRD_FZ1 cd07465
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 1 (Fz1) receptor; The cysteine-rich ...
 139-243 3.27e-09

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: 55.83  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTPLLSVVRNMEMEKF-LKFFTYLHRLSCYQHIMLFGCTLAFPECIIDgddSHGLLPCRSFCE 217
Cdd:cd07465    5 CQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLeVHQFYPLVKVQCSAELKFFLCSMYAPVCTVL---EQALPPCRSLCE 81

                         90       100
                 ....*....|....*....|....*.
gi 29244926  218 AAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07465   82 RARQGCEALMNKFGFQWPDTLRCEKF 107
CRD_FZ5_like cd07456
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 5; The cysteine-rich ...
 175-259 3.32e-09

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: 55.87  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  175 FTYLHRLSCYQHIMLFGCTLAFPECIIDGDdsHGLLPCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQFrnqTESSNVSR 254
Cdd:cd07456   39 FWPLVEIQCSPDLKFFLCSMYTPICLEDYD--KPLPPCRSVCERARDGCAPIMRQYGFAWPERMSCDAL---PEGGDPDN 113


                 ....*
gi 29244926  255 ICFSP 259
Cdd:cd07456  114 LCMDR 118
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
347-377 7.88e-09

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 51.87  E-value: 7.88e-09
                           10        20        30
                   ....*....|....*....|....*....|.
gi 29244926    347 EHRCGDGRCIAMEWVCDGDHDCVDKSDEVNC 377
Cdd:pfam00057    7 EFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 344-377 1.16e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.44  E-value: 1.16e-08
                         10        20        30
                 ....*....|....*....|....*....|....
gi 29244926  344 PTTEHRCGDGRCIAMEWVCDGDHDCVDKSDEVNC 377
Cdd:cd00112    2 PPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
eMpr COG3591
V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, ...
 817-1008 1.38e-08

V8-like Glu-specific endopeptidase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442810 [Multi-domain]  Cd Length: 194  Bit Score: 55.84  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  817 CSLQSEPSGHICGCVLIAKKWVLTVAHCFEGRENAA---VWKVVLGINNLDHPSVfmqtrFVKTIILHPRY-SRAVVDYD 892
Cdd:COG3591    3 GRLETDGGGGVCTGTLIGPNLVLTAGHCVYDGAGGGwatNIVFVPGYNGGPYGTA-----TATRFRVPPGWvASGDAGYD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  893 ISIVELSEDISE-TGYVRpvcLPNPEQWLEPDTYcYITGWGhmGNKMPFKLQEGEVRIISLEhcQSYFDMKTITTRmica 971
Cdd:COG3591   78 YALLRLDEPLGDtTGWLG---LAFNDAPLAGEPV-TIIGYP--GDRPKDLSLDCSGRVTGVQ--GNRLSYDCDTTG---- 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 29244926  972 gyesgtvdscmGDSGGPLVCEKPGGrWTLFGLTSWGS 1008
Cdd:COG3591  146 -----------GSSGSPVLDDSDGG-GRVVGVHSAGG 170
CRD_SFRP3 cd07441
Cysteine-rich domain of the secreted frizzled-related protein 3 (SFRP3, alias FRZB), a Wnt ...
 136-243 1.58e-08

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: 53.90  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  136 TSACMNITHSQCQMLPYHATLTP---LLSVVRN--MEMEKFLKFFTylhrLSCYQHIMLFGCTLAFPECIIDGDdSHGLL 210
Cdd:cd07441    1 AASCEPVRIPMCKSMPWNMTKMPnhlHHSTQANavLAIEQFEGLLG----TQCSPDLLFFLCAMYAPICTIDFQ-HEPIK 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 29244926  211 PCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07441   76 PCKSVCERARAGCEPVLIRYRHTWPESLACEEL 108
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 580-614 1.59e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 1.59e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  580 CSPSHFKCRSGQCVLASRRCDGQADCDDDSDEENC 614
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 306-340 1.96e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 51.05  E-value: 1.96e-08
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  306 CSENLFHCHTGKCLNYSLVCDGYDDCGDLSDEQNC 340
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
580-614 2.20e-08

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 50.71  E-value: 2.20e-08
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 29244926    580 CSPSHFKCRSGQCVLASRRCDGQADCDDDSDEENC 614
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CRD_SFRP2 cd07446
Cysteine-rich domain of the secreted frizzled-related protein 2 (SFRP2), a regulator of Wnt ...
 183-243 2.44e-08

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: 53.37  E-value: 2.44e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29244926  183 CYQHIMLFGCTLAFPECIIDGDDShgLLPCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07446   52 CHPDTKKFLCSLFAPVCLDDLDEA--IQPCRSLCEAVKDGCAPVMSAFGFPWPDMLDCTRF 110
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 387-414 2.68e-08

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 50.67  E-value: 2.68e-08
                         10        20
                 ....*....|....*....|....*...
gi 29244926  387 CRNGQCIPSTFQCDGDEDCKDGSDEENC 414
Cdd:cd00112    8 CANGRCIPSSWVCDGEDDCGDGSDEENC 35
CRD_FZ8 cd07461
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 8 (Fz8) receptor; The cysteine-rich ...
 138-246 3.48e-08

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: 53.06  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  138 ACMNITHSQCQMLPYHATLTPLlSVVRNMEMEKFLKF--FTYLHRLSCYQHIMLFGCTLAFPECIidGDDSHGLLPCRSF 215
Cdd:cd07461    4 QCQEITVPLCKGIGYNYTYMPN-QFNHDTQDEAGLEVhqFWPLVEIQCSPDLKFFLCSMYTPICL--EDYKKPLPPCRSV 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 29244926  216 CEAAKEGCESVLGMVNYSWPDFLRCSQFRNQ 246
Cdd:cd07461   81 CERAKAGCAPLMRQYGFPWPDRMRCDLLPEQ 111
CRD_Collagen_XVIII cd07455
Cysteine-rich domain of the variant 3 of collagen XVIII (V3C18 ); The cysteine-rich domain ...
 457-564 4.97e-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: 52.51  E-value: 4.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  457 PITLELCMNLPYNSTSYPNYFGHRTQKE---ASISWEsslfpALVQTNCYKYLMFFSCTILVPKCDVNTGEHIPPCRALC 533
Cdd:cd07455    9 PSSLPFCSRLGIRSFWLPNFLNHTSVEEvraVLAEWA-----WLLESGCHPSLEWFFCLLLVPSCGGGPPPPPPPCRQFC 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 29244926  534 EHSKERCESVLGivGLQWPedTDCSQFPEEN 564
Cdd:cd07455   84 EVLQDSCWNLLE--GGRLP--VACASLPEQE 110
CRD_FZ10 cd07462
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 10 (Fz10) receptor; The cysteine-rich ...
 139-248 6.59e-08

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: 52.33  E-value: 6.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTP-LLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIidGDDSHGLLPCRSFCE 217
Cdd:cd07462    5 CQPIEIPMCKDIGYNMTRMPnLMGHENQREAAIQLHEFAPLVEYGCHSHLKFFLCSLYAPMCT--EQVSTPIPACRVMCE 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 29244926  218 AAKEGCESVLGMVNYSWPDFLRCSQFRNQTE 248
Cdd:cd07462   83 QARLKCSPIMEQFNFKWPDSLDCSKLPNKND 113
SR smart00202
Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR ...
 690-786 8.31e-08

Scavenger receptor Cys-rich; The sea urchin egg peptide speract contains 4 repeats of SR domains that contain 6 conserved cysteines. May bind bacterial antigens in the protein MARCO.


Pssm-ID: 214555 [Multi-domain]  Cd Length: 101  Bit Score: 51.19  E-value: 8.31e-08
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926     690 VTLSINVNSSS-FLMVHRAATEHHVCADGWQEILSQLACKQMGLGEPSVTKL-IQEQEKEPRWLTLHSNWESLNgTTLHE 767
Cdd:smart00202    1 VRLVGGGSPCEgRVEVYHNGQWGTVCDDGWDLRDANVVCRQLGFGGAVSASGsAYFGPGSGPIWLDNVRCSGTE-ASLSD 79

                            90       100
                    ....*....|....*....|..
gi 29244926     768 LLVNGQ---SCESRSKISLLCT 786
Cdd:smart00202   80 CPHSGWgshNCSHGEDAGVVCS 101
CRD_FZ9_like cd07457
Cysteine-rich Wnt-binding domain (CRD) of receptors similar to frizzled 9; The cysteine-rich ...
 137-252 9.09e-08

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: 51.73  E-value: 9.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  137 SACMNITHSQCQMLPYHATLTP-LLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDShgLLPCRSF 215
Cdd:cd07457    1 GKCERITIPMCQGIGYNMTRMPnLLGHESQSEAAISIHEFAPLVQYGCAEHLRFFLCSLYAPMCTEQVSIP--IPACRSM 78

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 29244926  216 CEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTESSNV 252
Cdd:cd07457   79 CEQARDKCSPIMEQFSFSWPDSLDCDRLPRKNDPKDL 115
CRD_FZ9 cd07463
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 9 (Fz9) receptor; The cysteine-rich ...
 139-243 1.10e-07

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: 51.56  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTP-LLSVVRNMEMEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIidgDDSHGLLP-CRSFC 216
Cdd:cd07463    5 CQPVVIPMCRGIGYNLTRMPnFLGHDSQREAAIKLNEFAPLVEYGCHVHLRFFLCSLYAPMCT---DQVSTSIPaCRPMC 81

                         90       100
                 ....*....|....*....|....*..
gi 29244926  217 EAAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07463   82 EQARQKCSPIMEQFNFGWPESLDCSRL 108
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 655-689 1.21e-07

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 48.74  E-value: 1.21e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 29244926  655 CQDDELECANHACVSRDLWCDGEADCSDSSDEWDC 689
Cdd:cd00112    1 CPPNEFRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
387-414 1.49e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 48.40  E-value: 1.49e-07
                           10        20
                   ....*....|....*....|....*...
gi 29244926    387 CRNGQCIPSTFQCDGDEDCKDGSDEENC 414
Cdd:pfam00057   10 CGSGECIPRSWVCDGDPDCGDGSDEENC 37
LDLa cd00112
Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central ...
 269-304 1.95e-07

Low Density Lipoprotein Receptor Class A domain, a cysteine-rich repeat that plays a central role in mammalian cholesterol metabolism; the receptor protein binds LDL and transports it into cells by endocytosis; 7 successive cysteine-rich repeats of about 40 amino acids are present in the N-terminal of this multidomain membrane protein; other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement; the binding of calcium is required for in vitro formation of the native disulfide isomer and is necessary in establishing and maintaining the modular structure


Pssm-ID: 238060  Cd Length: 35  Bit Score: 47.97  E-value: 1.95e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 29244926  269 CGRGEnFLCASGICIPGKLQCNGYNDCDDWSDEAHC 304
Cdd:cd00112    1 CPPNE-FRCANGRCIPSSWVCDGEDDCGDGSDEENC 35
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
269-304 3.01e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 47.63  E-value: 3.01e-07
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 29244926    269 CGRGEnFLCASGICIPGKLQCNGYNDCDDWSDEAHC 304
Cdd:pfam00057    3 CSPNE-FQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
306-340 3.52e-07

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 47.24  E-value: 3.52e-07
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 29244926    306 CSENLFHCHTGKCLNYSLVCDGYDDCGDLSDEQNC 340
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CRD_FZ6 cd07450
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 6 (Fz6) receptor; The cysteine-rich ...
 139-253 4.39e-07

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: 49.76  E-value: 4.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTPLL-----SVVRNMEMEKFLKfftyLHRLSCYQHIMLFGCTLAFPECIidgDDSHGLLPCR 213
Cdd:cd07450    5 CEPITVPRCLKMPYNMTFFPNLmghydQDIAAVEMEPFLP----LANLRCSPNVHTFLCQAFVPTCT---EQIHVVRPCR 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 29244926  214 SFCEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTESSNVS 253
Cdd:cd07450   78 ELCEKVYSDCKKLIDTFGISWPEELECDRLQYCDETVPDT 117
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 344-374 5.27e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.86  E-value: 5.27e-07
                            10        20        30
                    ....*....|....*....|....*....|.
gi 29244926     344 PTTEHRCGDGRCIAMEWVCDGDHDCVDKSDE 374
Cdd:smart00192    3 PPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CRD_SFRP1 cd07443
Cysteine-rich domain of the secreted frizzled-related protein 1 (SFRP1), a regulator of Wnt ...
 182-243 7.96e-07

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: 49.13  E-value: 7.96e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29244926  182 SCYQHIMLFGCTLAFPECIidgddSHGLLPCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07443   53 NCHKGTQVFLCSLFAPVCL-----DRPVYPCRWLCEAVRDSCEPVMQFFGFYWPEMLKCDKF 109
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 306-337 9.96e-07

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 46.09  E-value: 9.96e-07
                            10        20        30
                    ....*....|....*....|....*....|..
gi 29244926     306 CSENLFHCHTGKCLNYSLVCDGYDDCGDLSDE 337
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
CRD_SFRP5 cd07444
Cysteine-rich domain of the secreted frizzled-related protein 5 (SFRP5), a regulator of Wnt ...
 183-243 1.06e-06

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: 48.79  E-value: 1.06e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29244926  183 CYQHIMLFGCTLAFPECIidgddSHGLLPCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07444   54 CHADTQVFLCSLFAPVCL-----DRPIYPCRSLCEAVRDSCAPVMESYGFPWPEMLHCHKF 109
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 579-611 1.15e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 45.70  E-value: 1.15e-06
                            10        20        30
                    ....*....|....*....|....*....|...
gi 29244926     579 ECSPSHFKCRSGQCVLASRRCDGQADCDDDSDE 611
Cdd:smart00192    1 TCPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 387-411 1.19e-06

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 45.70  E-value: 1.19e-06
                            10        20
                    ....*....|....*....|....*
gi 29244926     387 CRNGQCIPSTFQCDGDEDCKDGSDE 411
Cdd:smart00192    9 CDNGRCIPSSWVCDGVDDCGDGSDE 33
CRD_FZ5 cd07460
Cysteine-rich Wnt-binding domain (CRD) of the frizzled 5 (Fz5) receptor.proteins; The ...
 139-243 1.48e-06

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: 48.47  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTPLlSVVRNMEMEKFLKF--FTYLHRLSCYQHIMLFGCTLAFPECIidGDDSHGLLPCRSFC 216
Cdd:cd07460    5 CQEITVPMCKGIGYNLTYMPN-QFNHDTQDEAGLEVhqFWPLVEIQCSPDLRFFLCSMYTPICL--PDYRKPLPPCRSVC 81

                         90       100
                 ....*....|....*....|....*..
gi 29244926  217 EAAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07460   82 ERAKAGCSPLMRQYGFAWPERMNCDRL 108
CRD_Carboxypeptidase_Z cd07447
Cysteine-rich domain of carboxypeptidase Z, a member of the carboxypeptidase E family; The ...
 139-243 2.47e-06

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: 47.83  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  139 CMNITHSQCQMLPYHATLTPLLSVVRN---MEMEKFLKFFTYLHRL---SCYQHIMLFGCTLAFPECiidgDDSHGLLPC 212
Cdd:cd07447    4 CTDLLLSYCSDVSYTQTTFPNLLGHRSrevTEAGAEYLLLSVLHGLlggECNPDIRLLGCSVLAPRC----ENDKVIKPC 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 29244926  213 RSFCEAAKEGCESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07447   80 RSTCEALRKRCSHAFDAIQMAWPYFLDCDRF 110
SRCR_2 pfam15494
Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain ...
 713-794 5.15e-06

Scavenger receptor cysteine-rich domain; SRCR_2 is a scavenger receptor cysteine-rich domain family found largely on vertebrate sequences up-stream of the trypsin-like transmembrane serine protease, Spinesin.


Pssm-ID: 464747  Cd Length: 99  Bit Score: 46.17  E-value: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926    713 VCADGWQEILSQLACKQMGLGEPSVTKLIQ----EQEKEPRWLTLHSnweSLNGTTLHELLVNGQSCESRSKISLLCTkq 788
Cdd:pfam15494   19 VCSDDWNPAYGRAACQQLGYLRLTHHKSVNltdiSSNSSQSFMKLNS---SSLNTDLYEALQPRDSCSSGSVVSLRCS-- 93


                   ....*.
gi 29244926    789 DCGRRP 794
Cdd:pfam15494   94 ECGLRS 99
CRD_SFRP4 cd07442
Cysteine-rich domain of the secreted frizzled-related protein 4 (SFRP4), a Wnt antagonist; The ...
 183-260 6.38e-06

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: 46.56  E-value: 6.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29244926  183 CYQHIMLFGCTLAFPECIIDGDDShGLLPCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTESsnvsrICFSPQ 260
Cdd:cd07442   50 CSPVLPFFLCAMYAPICTLEFLYD-PIKPCRSVCQRARDGCEPIMRRYNHSWPESLACDDLPVYDRG-----VCISPE 121
CRD_sizzled cd07452
Cysteine-rich domain of the sizzled protein; The cysteine-rich domain (CRD) is an essential ...
 145-243 6.58e-06

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: 46.80  E-value: 6.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  145 SQCQMLPYHATLTPLLSVVRNMEmEKFLKFFTYLHRL--SCYQHIMLFGCTLAFPECIidgddSHGLLPCRSFCEAAKEG 222
Cdd:cd07452   17 SMCQDVGYSEMRLPNLLGHTSMA-EVVPKSADWQTLLhtGCHPHARTFLCSLFAPVCL-----DTFIQPCRSMCVAVRDS 90

                         90       100
                 ....*....|....*....|.
gi 29244926  223 CESVLGMVNYSWPDFLRCSQF 243
Cdd:cd07452   91 CAPVLACHGHSWPESLDCDRF 111
CRD_crescent cd07453
Cysteine-rich domain of the crescent protein; The cysteine-rich domain (CRD) is an essential ...
 183-263 1.54e-05

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: 45.70  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  183 CYQHIMLFGCTLAFPECIidgdDSHgLLPCRSFCEAAKEGCESVLGMVNYSWPDFLRCSQFRNQTEssnvsrICFSPQQE 262
Cdd:cd07453   50 CHPDARIFLCSLFAPICW----DRP-IYPCRSLCEAVRSSCAPLMACYGYPWPEILHCDKFPVDHD------LCISPQFI 118


                 .
gi 29244926  263 N 263
Cdd:cd07453  119 D 119
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 269-301 1.92e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 42.24  E-value: 1.92e-05
                            10        20        30
                    ....*....|....*....|....*....|...
gi 29244926     269 CGRGEnFLCASGICIPGKLQCNGYNDCDDWSDE 301
Cdd:smart00192    2 CPPGE-FQCDNGRCIPSSWVCDGVDDCGDGSDE 33
LDLa smart00192
Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density ...
 655-686 2.39e-05

Low-density lipoprotein receptor domain class A; Cysteine-rich repeat in the low-density lipoprotein (LDL) receptor that plays a central role in mammalian cholesterol metabolism. The N-terminal type A repeats in LDL receptor bind the lipoproteins. Other homologous domains occur in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. Mutations in the LDL receptor gene cause familial hypercholesterolemia.


Pssm-ID: 197566  Cd Length: 33  Bit Score: 42.24  E-value: 2.39e-05
                            10        20        30
                    ....*....|....*....|....*....|..
gi 29244926     655 CQDDELECANHACVSRDLWCDGEADCSDSSDE 686
Cdd:smart00192    2 CPPGEFQCDNGRCIPSSWVCDGVDDCGDGSDE 33
Ldl_recept_a pfam00057
Low-density lipoprotein receptor domain class A;
655-689 9.64e-05

Low-density lipoprotein receptor domain class A;


Pssm-ID: 395011  Cd Length: 37  Bit Score: 40.31  E-value: 9.64e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 29244926    655 CQDDELECANHACVSRDLWCDGEADCSDSSDEWDC 689
Cdd:pfam00057    3 CSPNEFQCGSGECIPRSWVCDGDPDCGDGSDEENC 37
CRD_SMO cd07451
Cysteine-rich domain of the smoothened receptor (Smo) integral membrane protein; The ...
 150-240 1.84e-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: 42.35  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29244926  150 LPYHATLTPLLSVVRNME--MEKFLKFFTYLHRLSCYQHIMLFGCTLAFPECIIDGDDshglLPCRSFCEAAKEGCESVL 227
Cdd:cd07451   18 LPYTYTSLDLVPDSTTQEevQEKLHLWSGLRNVPKCWAVIQPLLCALYMPKCENGKVE----LPSQEMCQATRGPCKIVE 93

                         90
                 ....*....|...
gi 29244926  228 gmVNYSWPDFLRC 240
Cdd:cd07451   94 --NERGWPDFLRC 104
 
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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