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Conserved domains on  [gi|587020512|ref|XP_006943612|]
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amelogenin, X isoform isoform X1 [Felis catus]

Protein Classification

Amelogenin domain-containing protein( domain architecture ID 12220051)

Amelogenin domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-192 4.37e-47

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


:

Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 151.87  E-value: 4.37e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512    28 YINFSYEVLTPLKWYQNMIRHPYPSYGYEPMGGWLHHQIIPVlSQQNPPNHALQPHHHIPMVPAQQPVVPQQPMMPVPGQ 107
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512   108 HSMTPTQHHQPNLPLPAQQPFQPQPVQPQPHQPIQPQPPVHPIQPLPPQPPLPP-MFPIQPLPPMLPDLPLEAWPATDKT 186
Cdd:smart00818  80 HSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPLPpMFPMQPLPPLLPDLPLEAWPATDKT 159


                   ....*.
gi 587020512   187 KREEVD 192
Cdd:smart00818 160 KREEVD 165
 
Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-192 4.37e-47

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 151.87  E-value: 4.37e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512    28 YINFSYEVLTPLKWYQNMIRHPYPSYGYEPMGGWLHHQIIPVlSQQNPPNHALQPHHHIPMVPAQQPVVPQQPMMPVPGQ 107
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512   108 HSMTPTQHHQPNLPLPAQQPFQPQPVQPQPHQPIQPQPPVHPIQPLPPQPPLPP-MFPIQPLPPMLPDLPLEAWPATDKT 186
Cdd:smart00818  80 HSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPLPpMFPMQPLPPLLPDLPLEAWPATDKT 159


                   ....*.
gi 587020512   187 KREEVD 192
Cdd:smart00818 160 KREEVD 165
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ...
 28-192 1.86e-39

Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organization and mineralization of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta.


Pssm-ID: 460761 [Multi-domain]  Cd Length: 179  Bit Score: 132.96  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512   28 YINFSYEVLTPLKWYQNMIRHPYPSYGYEPMGGWLHHQIIPVLS----QQNPPNHALQPHHHIPMVPAQQPVV---PQQP 100
Cdd:pfam02948   8 YINFSYEVLTPLKWYQSLIGHAYPRYGFEPMGGWLHHAAGPTLHqttfQQHPPTHSLLPHHHIPPHPALNPHMqpsGHNP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512  101 MMPVPGQHSMTPTQHHQPNLPLPAQQPFQPQPVQPQPHQPIQPQPPVHPIQPLPPQPPLPPMFPIQPLPPMLPDLPLEAW 180
Cdd:pfam02948  88 FGPMPGQHSLIPTQHFQPAHGGPAHHPFQPHAGEPHPHHPMQPGNPVHPMHPLPPANPLPPIFPMQPLPPLIPDLPLEAW 167

                         170
                  ....*....|..
gi 587020512  181 PATDKTKREEVD 192
Cdd:pfam02948 168 PAADKTKQEEVD 179
 
Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-192 4.37e-47

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 151.87  E-value: 4.37e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512    28 YINFSYEVLTPLKWYQNMIRHPYPSYGYEPMGGWLHHQIIPVlSQQNPPNHALQPHHHIPMVPAQQPVVPQQPMMPVPGQ 107
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512   108 HSMTPTQHHQPNLPLPAQQPFQPQPVQPQPHQPIQPQPPVHPIQPLPPQPPLPP-MFPIQPLPPMLPDLPLEAWPATDKT 186
Cdd:smart00818  80 HSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPLPpMFPMQPLPPLLPDLPLEAWPATDKT 159


                   ....*.
gi 587020512   187 KREEVD 192
Cdd:smart00818 160 KREEVD 165
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ...
 28-192 1.86e-39

Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation of crystallites during the secretory stage of tooth enamel development. thought to play a major role in the structural organization and mineralization of developing enamel. They are found in the extracellular matrix. Mutations in X-chromosomal amelogenin can cause Amelogenesis imperfecta.


Pssm-ID: 460761 [Multi-domain]  Cd Length: 179  Bit Score: 132.96  E-value: 1.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512   28 YINFSYEVLTPLKWYQNMIRHPYPSYGYEPMGGWLHHQIIPVLS----QQNPPNHALQPHHHIPMVPAQQPVV---PQQP 100
Cdd:pfam02948   8 YINFSYEVLTPLKWYQSLIGHAYPRYGFEPMGGWLHHAAGPTLHqttfQQHPPTHSLLPHHHIPPHPALNPHMqpsGHNP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587020512  101 MMPVPGQHSMTPTQHHQPNLPLPAQQPFQPQPVQPQPHQPIQPQPPVHPIQPLPPQPPLPPMFPIQPLPPMLPDLPLEAW 180
Cdd:pfam02948  88 FGPMPGQHSLIPTQHFQPAHGGPAHHPFQPHAGEPHPHHPMQPGNPVHPMHPLPPANPLPPIFPMQPLPPLIPDLPLEAW 167

                         170
                  ....*....|..
gi 587020512  181 PATDKTKREEVD 192
Cdd:pfam02948 168 PAADKTKQEEVD 179
 
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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