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Conserved domains on  [gi|119592107|gb|EAW71701|]
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chromosome 1 open reading frame 187, isoform CRA_b [Homo sapiens]

Protein Classification

Draxin domain-containing protein( domain architecture ID 10634678)

Draxin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Draxin pfam15550
Draxin; This family of proteins inhibit Wnt signaling and act as chemorepulsive axon guidance ...
 38-349 8.83e-173

Draxin; This family of proteins inhibit Wnt signaling and act as chemorepulsive axon guidance molecules.


:

Pssm-ID: 464760  Cd Length: 321  Bit Score: 482.81  E-value: 8.83e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107   38 PENHIDLPGPALWTPQASHHRRRGPGKKEWGP-GLPSQ--------AQDGAVVTATRQASRLPEaegllpeQSPAGLLQD 108
Cdd:pfam15550   1 SENHLQHPEPWLQIHRHGHHRRRGGARKERASaGLLSRrplppmfrLQDDGTGLEGLSPVRLEM-------GPPDRLTER 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  109 KDLLLGLALPYPEKENRPPGWE---RTRKRSREHKR--RRDRLRLHQGRALVRGPSSLMKKAELSEAQVLDAAMEESSTS 183
Cdd:pfam15550  74 KEVFLGFDSPYPERENRSPGSEgirKGRKHGREHRKhgRRDRLRHHKGRLSDPEPSSLLKDRESFEDQLNSSSPEEFPSP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  184 LAPTMFFLTTFEAAPATEESLILPVTSLRPQ-QAQPRSDGEVMPTLDMALFDWTDYEDLKP-DGWPSAKKKEKHRGKLSS 261
Cdd:pfam15550 154 LAPTLLFLTALVTTPITEHPPTLPPASTKPQkQGRVRSDGEVMPTLDMALFDWTDYEDMKPvDSWPSSKKKEKRRSKNLS 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  262 DGNETSPAEGEPCDHHQDCLPGTCCDLREHLCTPHNRGLNNKCFDDCMCVEGLRCYAKFHRNRRVTRRKGRCVEPETANG 341
Cdd:pfam15550 234 SGNLTSDAEGEPCDHHLDCLPGSCCDLREHVCKPHNRGLNNKCYDDCMCEEGLRCYAKFHRNRRVTRRKGRCVEPESVNS 313


                  ....*...
gi 119592107  342 DQGSFINV 349
Cdd:pfam15550 314 DQGSFITV 321
 
Name Accession Description Interval E-value
Draxin pfam15550
Draxin; This family of proteins inhibit Wnt signaling and act as chemorepulsive axon guidance ...
 38-349 8.83e-173

Draxin; This family of proteins inhibit Wnt signaling and act as chemorepulsive axon guidance molecules.


Pssm-ID: 464760  Cd Length: 321  Bit Score: 482.81  E-value: 8.83e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107   38 PENHIDLPGPALWTPQASHHRRRGPGKKEWGP-GLPSQ--------AQDGAVVTATRQASRLPEaegllpeQSPAGLLQD 108
Cdd:pfam15550   1 SENHLQHPEPWLQIHRHGHHRRRGGARKERASaGLLSRrplppmfrLQDDGTGLEGLSPVRLEM-------GPPDRLTER 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  109 KDLLLGLALPYPEKENRPPGWE---RTRKRSREHKR--RRDRLRLHQGRALVRGPSSLMKKAELSEAQVLDAAMEESSTS 183
Cdd:pfam15550  74 KEVFLGFDSPYPERENRSPGSEgirKGRKHGREHRKhgRRDRLRHHKGRLSDPEPSSLLKDRESFEDQLNSSSPEEFPSP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  184 LAPTMFFLTTFEAAPATEESLILPVTSLRPQ-QAQPRSDGEVMPTLDMALFDWTDYEDLKP-DGWPSAKKKEKHRGKLSS 261
Cdd:pfam15550 154 LAPTLLFLTALVTTPITEHPPTLPPASTKPQkQGRVRSDGEVMPTLDMALFDWTDYEDMKPvDSWPSSKKKEKRRSKNLS 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  262 DGNETSPAEGEPCDHHQDCLPGTCCDLREHLCTPHNRGLNNKCFDDCMCVEGLRCYAKFHRNRRVTRRKGRCVEPETANG 341
Cdd:pfam15550 234 SGNLTSDAEGEPCDHHLDCLPGSCCDLREHVCKPHNRGLNNKCYDDCMCEEGLRCYAKFHRNRRVTRRKGRCVEPESVNS 313


                  ....*...
gi 119592107  342 DQGSFINV 349
Cdd:pfam15550 314 DQGSFITV 321
Dkk1_Cys2 cd23272
second cysteine-rich (Cys-2) domain of Dickkopf-related protein 1; Dickkopf-1 (Dkk1) is a ...
 270-316 2.73e-03

second cysteine-rich (Cys-2) domain of Dickkopf-related protein 1; Dickkopf-1 (Dkk1) is a secreted protein which directly binds to LRP5/6 (low-density lipoprotein receptor related protein 5 and 6), and is an inhibitor of Wnt/beta-catenin signaling. Elevated expression of Dkk-1 may serve as a negative regulator for modulating the wnt/#-catenin signal pathway. Dkk1 is expressed in various human cancers. It has been studied extensively in mouse models of multiple myeloma that results in osteolytic bone lesions. Studies show that Dkk1 levels in bone marrow plasma and serum inhibit the differentiation of osteoblast precursors. Dkk1 belongs to the Dickkopf (Dkk) family that comprises a discrete class of secreted Wnt inhibitors. The Wnt gene family is a large class of secreted proteins that are expressed in a variety of tissues and organs, and are required for many developmental processes, including segmentation, endoderm development, limb polarity, neural crest differentiation, kidney morphogenesis, sex determination and brain development. Dkks 1-4 each possesses an N-terminal signal peptide and contains two conserved cysteine-rich domains (Cys-1 and Cys-2) separated by a linker region. Each domain possesses 10 conserved cysteine residues. The Cys-2 domain is closely similar to those in the colipase family; it has been suggested that the Cys-2 domain of Dkks may enable interaction with lipids in order to regulate Wnt function. This model corresponds to the Cys-2 domain of Dkk1.


Pssm-ID: 437998  Cd Length: 83  Bit Score: 36.21  E-value: 2.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119592107 270 EGEPCDHHQDCLPGTCCD-----------LRE-HLCTPHNRGLNN--KCFDDCMCVEGLRC 316
Cdd:cd23272    4 EGDTCLRSSDCSEGLCCArhfwskickpvLKEgQVCTKHRRKGSHglEIFQRCDCGDGLSC 64
 
Name Accession Description Interval E-value
Draxin pfam15550
Draxin; This family of proteins inhibit Wnt signaling and act as chemorepulsive axon guidance ...
 38-349 8.83e-173

Draxin; This family of proteins inhibit Wnt signaling and act as chemorepulsive axon guidance molecules.


Pssm-ID: 464760  Cd Length: 321  Bit Score: 482.81  E-value: 8.83e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107   38 PENHIDLPGPALWTPQASHHRRRGPGKKEWGP-GLPSQ--------AQDGAVVTATRQASRLPEaegllpeQSPAGLLQD 108
Cdd:pfam15550   1 SENHLQHPEPWLQIHRHGHHRRRGGARKERASaGLLSRrplppmfrLQDDGTGLEGLSPVRLEM-------GPPDRLTER 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  109 KDLLLGLALPYPEKENRPPGWE---RTRKRSREHKR--RRDRLRLHQGRALVRGPSSLMKKAELSEAQVLDAAMEESSTS 183
Cdd:pfam15550  74 KEVFLGFDSPYPERENRSPGSEgirKGRKHGREHRKhgRRDRLRHHKGRLSDPEPSSLLKDRESFEDQLNSSSPEEFPSP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  184 LAPTMFFLTTFEAAPATEESLILPVTSLRPQ-QAQPRSDGEVMPTLDMALFDWTDYEDLKP-DGWPSAKKKEKHRGKLSS 261
Cdd:pfam15550 154 LAPTLLFLTALVTTPITEHPPTLPPASTKPQkQGRVRSDGEVMPTLDMALFDWTDYEDMKPvDSWPSSKKKEKRRSKNLS 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119592107  262 DGNETSPAEGEPCDHHQDCLPGTCCDLREHLCTPHNRGLNNKCFDDCMCVEGLRCYAKFHRNRRVTRRKGRCVEPETANG 341
Cdd:pfam15550 234 SGNLTSDAEGEPCDHHLDCLPGSCCDLREHVCKPHNRGLNNKCYDDCMCEEGLRCYAKFHRNRRVTRRKGRCVEPESVNS 313


                  ....*...
gi 119592107  342 DQGSFINV 349
Cdd:pfam15550 314 DQGSFITV 321
Dkk1_Cys2 cd23272
second cysteine-rich (Cys-2) domain of Dickkopf-related protein 1; Dickkopf-1 (Dkk1) is a ...
 270-316 2.73e-03

second cysteine-rich (Cys-2) domain of Dickkopf-related protein 1; Dickkopf-1 (Dkk1) is a secreted protein which directly binds to LRP5/6 (low-density lipoprotein receptor related protein 5 and 6), and is an inhibitor of Wnt/beta-catenin signaling. Elevated expression of Dkk-1 may serve as a negative regulator for modulating the wnt/#-catenin signal pathway. Dkk1 is expressed in various human cancers. It has been studied extensively in mouse models of multiple myeloma that results in osteolytic bone lesions. Studies show that Dkk1 levels in bone marrow plasma and serum inhibit the differentiation of osteoblast precursors. Dkk1 belongs to the Dickkopf (Dkk) family that comprises a discrete class of secreted Wnt inhibitors. The Wnt gene family is a large class of secreted proteins that are expressed in a variety of tissues and organs, and are required for many developmental processes, including segmentation, endoderm development, limb polarity, neural crest differentiation, kidney morphogenesis, sex determination and brain development. Dkks 1-4 each possesses an N-terminal signal peptide and contains two conserved cysteine-rich domains (Cys-1 and Cys-2) separated by a linker region. Each domain possesses 10 conserved cysteine residues. The Cys-2 domain is closely similar to those in the colipase family; it has been suggested that the Cys-2 domain of Dkks may enable interaction with lipids in order to regulate Wnt function. This model corresponds to the Cys-2 domain of Dkk1.


Pssm-ID: 437998  Cd Length: 83  Bit Score: 36.21  E-value: 2.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119592107 270 EGEPCDHHQDCLPGTCCD-----------LRE-HLCTPHNRGLNN--KCFDDCMCVEGLRC 316
Cdd:cd23272    4 EGDTCLRSSDCSEGLCCArhfwskickpvLKEgQVCTKHRRKGSHglEIFQRCDCGDGLSC 64
 
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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