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Conserved domains on  [gi|344198227|ref|NP_001230675|]
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pseudokinase FAM20A isoform b [Homo sapiens]

Protein Classification

FAM20A_C domain-containing protein( domain architecture ID 10180061)

FAM20A_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FAM20A_C cd10469
C-terminal putative kinase domain of FAM20A; Human FAM20A may play a fundamental role in ...
168-384 1.97e-165

C-terminal putative kinase domain of FAM20A; Human FAM20A may play a fundamental role in enamel development and gingival homeostasis as mutations in FAM20A may underlie the pathogenesis of the autosomal recessive Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. It is expressed in ameloblasts and gingivae. AI refers to a heterogeneous group of disorders of biomineralization caused by a lack of normal enamel formation. Mouse FAM20A is a secreted protein and the gene encoding it is differentially expressed in hematopoietic cells undergoing myeloid differentiation. This protein has also been associated with growth disorder in mice. The C-terminal domain of FAM20A is a putative kinase domain, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This subfamily belongs to the FAM20_C (also known as DUF1193) domain family.


:

Pssm-ID: 198460  Cd Length: 217  Bit Score: 462.50  E-value: 1.97e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 168 FVSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQIY 247
Cdd:cd10469    1 FNSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSIPNPWIRSYTFAGKEEWEVNPLYCDTVKEIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 248 PYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQL 327
Cdd:cd10469   81 PYNSGNRLLNIIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLLHLDNARGFGKHSHDEISILSPLSQCCIIKKSTLLRLQL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 344198227 328 LAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCIVAHGQQSVI 384
Cdd:cd10469  161 LAQPDYRLSDVMRESLEKDALQPVLTEPHLLALDRRLQKILRTVERCIRALGKDKVV 217
 
Name Accession Description Interval E-value
FAM20A_C cd10469
C-terminal putative kinase domain of FAM20A; Human FAM20A may play a fundamental role in ...
168-384 1.97e-165

C-terminal putative kinase domain of FAM20A; Human FAM20A may play a fundamental role in enamel development and gingival homeostasis as mutations in FAM20A may underlie the pathogenesis of the autosomal recessive Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. It is expressed in ameloblasts and gingivae. AI refers to a heterogeneous group of disorders of biomineralization caused by a lack of normal enamel formation. Mouse FAM20A is a secreted protein and the gene encoding it is differentially expressed in hematopoietic cells undergoing myeloid differentiation. This protein has also been associated with growth disorder in mice. The C-terminal domain of FAM20A is a putative kinase domain, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This subfamily belongs to the FAM20_C (also known as DUF1193) domain family.


Pssm-ID: 198460  Cd Length: 217  Bit Score: 462.50  E-value: 1.97e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 168 FVSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQIY 247
Cdd:cd10469    1 FNSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSIPNPWIRSYTFAGKEEWEVNPLYCDTVKEIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 248 PYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQL 327
Cdd:cd10469   81 PYNSGNRLLNIIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLLHLDNARGFGKHSHDEISILSPLSQCCIIKKSTLLRLQL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 344198227 328 LAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCIVAHGQQSVI 384
Cdd:cd10469  161 LAQPDYRLSDVMRESLEKDALQPVLTEPHLLALDRRLQKILRTVERCIRALGKDKVV 217
Fam20C pfam06702
Golgi casein kinase, C-terminal, Fam20; Fam20C represents the C-terminus of eukaryotic ...
167-384 6.44e-144

Golgi casein kinase, C-terminal, Fam20; Fam20C represents the C-terminus of eukaryotic secreted Golgi casein kinase proteins. Fam20C is the Golgi casein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. Mutations in Fam20C cause Raine syndrome, an autosomal recessive osteosclerotic bone dysplasia.


Pssm-ID: 461992  Cd Length: 218  Bit Score: 407.75  E-value: 6.44e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227  167 FFVSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQI 246
Cdd:pfam06702   1 FFVSPANNTCFYGKCSYYCKTEHAVCGKPDLLEGSLAAFLPDLSLAPRKSWRHPWRRSYSKRKKAEWEVDPDYCDKVKQT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227  247 YPYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQ 326
Cdd:pfam06702  81 PPYDSGRRLLDLIDMAIFDFLIGNMDRHHYETFEKFGNETFLLHLDNGRGFGRPSHDELSILAPLYQCCIIRKSTLLRLL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 344198227  327 LLAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCIVAHGQQSVI 384
Cdd:pfam06702 161 LLSGGPYRLSDLMRESLSSDPLAPILTEPHLEALDRRLLIVLATVQKCIEKKGEDQVL 218
 
Name Accession Description Interval E-value
FAM20A_C cd10469
C-terminal putative kinase domain of FAM20A; Human FAM20A may play a fundamental role in ...
168-384 1.97e-165

C-terminal putative kinase domain of FAM20A; Human FAM20A may play a fundamental role in enamel development and gingival homeostasis as mutations in FAM20A may underlie the pathogenesis of the autosomal recessive Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. It is expressed in ameloblasts and gingivae. AI refers to a heterogeneous group of disorders of biomineralization caused by a lack of normal enamel formation. Mouse FAM20A is a secreted protein and the gene encoding it is differentially expressed in hematopoietic cells undergoing myeloid differentiation. This protein has also been associated with growth disorder in mice. The C-terminal domain of FAM20A is a putative kinase domain, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This subfamily belongs to the FAM20_C (also known as DUF1193) domain family.


Pssm-ID: 198460  Cd Length: 217  Bit Score: 462.50  E-value: 1.97e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 168 FVSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQIY 247
Cdd:cd10469    1 FNSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSIPNPWIRSYTFAGKEEWEVNPLYCDTVKEIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 248 PYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQL 327
Cdd:cd10469   81 PYNSGNRLLNIIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLLHLDNARGFGKHSHDEISILSPLSQCCIIKKSTLLRLQL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 344198227 328 LAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCIVAHGQQSVI 384
Cdd:cd10469  161 LAQPDYRLSDVMRESLEKDALQPVLTEPHLLALDRRLQKILRTVERCIRALGKDKVV 217
Fam20C pfam06702
Golgi casein kinase, C-terminal, Fam20; Fam20C represents the C-terminus of eukaryotic ...
167-384 6.44e-144

Golgi casein kinase, C-terminal, Fam20; Fam20C represents the C-terminus of eukaryotic secreted Golgi casein kinase proteins. Fam20C is the Golgi casein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. Mutations in Fam20C cause Raine syndrome, an autosomal recessive osteosclerotic bone dysplasia.


Pssm-ID: 461992  Cd Length: 218  Bit Score: 407.75  E-value: 6.44e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227  167 FFVSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQI 246
Cdd:pfam06702   1 FFVSPANNTCFYGKCSYYCKTEHAVCGKPDLLEGSLAAFLPDLSLAPRKSWRHPWRRSYSKRKKAEWEVDPDYCDKVKQT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227  247 YPYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQ 326
Cdd:pfam06702  81 PPYDSGRRLLDLIDMAIFDFLIGNMDRHHYETFEKFGNETFLLHLDNGRGFGRPSHDELSILAPLYQCCIIRKSTLLRLL 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 344198227  327 LLAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCIVAHGQQSVI 384
Cdd:pfam06702 161 LLSGGPYRLSDLMRESLSSDPLAPILTEPHLEALDRRLLIVLATVQKCIEKKGEDQVL 218
FAM20_C cd10314
C-terminal putative kinase domain of FAM20 (family with sequence similarity 20) proteins; This ...
168-379 3.08e-127

C-terminal putative kinase domain of FAM20 (family with sequence similarity 20) proteins; This family contains the C-terminal domain of FAM20A, -B, -C and related proteins. FAM20A may participate in enamel development and gingival homeostasis, FAM20B in proteoglycan production, and FAM20C in bone development. FAM20B is a xylose kinase that may regulate the number of glycosaminoglycan chains by phosphorylating the xylose residue in the glycosaminoglycan-protein linkage region of proteoglycans. FAM20C, also called Dentin Matrix Protein 4, is abundant in the dentin matrix, and may participate in the differentiation of mesenchymal precursor cells into functional odontoblast-like cells. Mutations in FAM20C are associated with lethal Osteosclerotic Bone Dysplasia (Raine Syndrome), and mutations in FAM20A with Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. The C-terminal domains of members of this family are putative kinase domains, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This domain family is also known as DUF1193.


Pssm-ID: 198457  Cd Length: 209  Bit Score: 365.05  E-value: 3.08e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 168 FVSPASNVCFFAKCpYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAprLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQIY 247
Cdd:cd10314    1 FISPANNTCFYGKC-YYCKTEEAVCGNPDLLEGSLTAFLPDLSLL--KKWRHPWRRTYHKRKKAEWEVDPDYCDKVKKTP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 248 PYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQL 327
Cdd:cd10314   78 PYDSGRRLLDLIDMAIFDFLIGNMDRHHYETFEKFGNETFLIHLDNGKSFGNPSHDELSILAPLYQCCLIRKSTWLRLQL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 344198227 328 LAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCIVAHG 379
Cdd:cd10314  158 LAKGGGSLSDLLRESLSHDPLSPVLTEPHLDALDRRLLIVLATVEDCIEKNG 209
FAM20_C_like cd10467
C-terminal putative kinase domain of FAM20 (family with sequence similarity 20), Drosophila ...
168-375 2.96e-116

C-terminal putative kinase domain of FAM20 (family with sequence similarity 20), Drosophila Four-jointed (Fj), and related proteins; Drosophila Fj is a Golgi kinase that phosphorylates Ser or Thr residues within extracellular cadherin domains of a transmembrane receptor Fat and its ligand, Dachsous (Ds). The Fat signaling pathway regulates growth, gene expression, and planar cell polarity (PCP). Defects from mutation in the Drosophila fj gene include loss of the intermediate leg joint, and a PCP defect in the eye. Fjx1, the murine homologue of Fj, has been shown to be involved in both the Fat and Hippo signaling pathways, these two pathways intersect at multiple points. The Hippo pathway is important in organ size control and in cancer. FAM20B is a xylose kinase that may regulate the number of glycosaminoglycan chains by phosphorylating the xylose residue in the glycosaminoglycan-protein linkage region of proteoglycans. This domain has homology to a kinase-active site, mutation of three conserved Asp residues at the Drosophila Fj putative active site abolished its ability to phosphorylate Ft and Ds cadherin domains. FAM20A may participate in enamel development and gingival homeostasis, FAM20B in proteoglycan production, and FAM20C in bone development. FAM20C, also called Dentin Matrix Protein 4, is abundant in the dentin matrix, and may participate in the differentiation of mesenchymal precursor cells into functional odontoblast-like cells. Mutations in FAM20C are associated with lethal Osteosclerotic Bone Dysplasia (Raine Syndrome), and mutations in FAM20A with Amelogenesis imperfecta (AI) and Gingival Hyperplasia Syndrome. This model includes the FAM20_C domain family, previously known as DUF1193; FAM20_C appears to be homologous to the catalytic domain of the phosphoinositide 3-kinase (PI3K)-like family.


Pssm-ID: 198458  Cd Length: 210  Bit Score: 337.31  E-value: 2.96e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 168 FVSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQIY 247
Cdd:cd10467    1 FFSPANNTCFYGGCGYYCKTEEAACGNPDQIEGSLTSFLPDLLLLLRKKWRHPWQRTYTERKKAEWEVDLDYCDEVKKLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 248 PYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQL 327
Cdd:cd10467   81 PYDSGRRLLDLIDMAIFDFLIGNMDRHHYELFELQWNEGFLIHLDNGKGFGRPSHDELSILAPLYQCCVIRKSTWERLLL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 344198227 328 LAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCI 375
Cdd:cd10467  161 LHRGGGVLSRLLRESLRHDPLLPVLTEPHLQALDRRLDIVLATVEKCI 208
FAM20C_C cd10471
C-terminal putative kinase domain of FAM20C (also known as Dentin Matrix Protein 4, DMP4); ...
168-379 5.54e-99

C-terminal putative kinase domain of FAM20C (also known as Dentin Matrix Protein 4, DMP4); Mouse DMP4 is abundant in the dentin matrix, and is expressed in high levels in odontoblasts. These latter cells synthesize various nucleators or inhibitors of mineralization. The in vivo role of DMP4 in dentinogenesis is unclear. However, gain- and loss-of-function experiments suggest that it participates in the differentiation of mesenchymal precursor cells into functional odontoblast-like cells. In addition to this domain, DMP4 contains a Greek key calcium-binding domain. Human FAM20C participates in bone development; mutations in FAM20C are associated with lethal Osteosclerotic Bone Dysplasia (Raine Syndrome), an autosomal recessive disorder in which affected individuals die within days or weeks of birth, usually due to thoratic malformation resulting in respiratory failure. The C-terminal domain of FAM20C is a putative kinase domain, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This subfamily belongs to the FAM20_C (also known as DUF1193) domain family.


Pssm-ID: 198462  Cd Length: 212  Bit Score: 293.41  E-value: 5.54e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 168 FVSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQIY 247
Cdd:cd10471    1 FISPANNICFYGECSYYCSTEHALCGKPDQIEGSLAAFLPDLSLAKRKTWRNPWRRSYHKRKKAEWEVDPDYCEEVKQTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 248 PYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQL 327
Cdd:cd10471   81 PYDSGTRILDIMDMTVFDFLMGNMDRHHYETFEKFGNETFIIHLDNGRGFGKYSHDELSILVPLTQCCRIRKSTYLRLQL 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 344198227 328 LAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCIVAHG 379
Cdd:cd10471  161 LAKEEYKLSLLMAESLQRDKLAPILYQPHLEALDRRLRIVLKAVSDCVEKDG 212
FAM20B_C cd10470
C-terminal putative kinase domain of FAM20B xylose kinase; Experiments with human FAM20B ...
174-375 3.51e-71

C-terminal putative kinase domain of FAM20B xylose kinase; Experiments with human FAM20B suggest that it is a xylose kinase that participates in proteoglycan production. It may regulate the number of glycosaminoglycan chains by phosphorylating the xylose residue in the glycosaminoglycan-protein linkage region of proteoglycans. The C-terminal domain of FAM20B is a putative kinase domain, based on mutagenesis of the C-terminal domain of Drosophila Four-Jointed, a related Golgi kinase. This subfamily belongs to the FAM20_C (also known as DUF1193) domain family.


Pssm-ID: 198461  Cd Length: 206  Bit Score: 222.24  E-value: 3.51e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 174 NVCFFAKCpYMCKTEYAVCGNPHLLEGSLSAFLPS-LNLAPRLSvpnPWIRSYTLAGKEEWEVNPLYCDTVKQIYPYNNS 252
Cdd:cd10470    7 NTCFYGVC-YYCKEEEPACGEGDIMEGSVTLWLPDvWPLQKHRH---PWQRTYKENKLARWETDEDYCDKVKKKSPYDSG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 344198227 253 QRLLNVIDMAIFDFLIGNMDRHHYEMFTKFgDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQLLAQAd 332
Cdd:cd10470   83 PRLLDLIDTAIFDFLIGNGDRHHYETFQDD-PESMLLLLDNAKSFGNPDLDELSILAPLYQCCIIRKSTWDRLKLLKGG- 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 344198227 333 yRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCI 375
Cdd:cd10470  161 -VLTELLEEATKHDPLSPLLTEPHLRAIERRLLIVYATVEQCV 202
 
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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