NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720837179|ref|XP_030162369|]
View 

amelogenin, Y isoform [Lynx canadensis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 28-204 3.27e-53

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: 174.59  E-value: 3.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179   28 YINFSYEnshfqaiafdgtvlVLTPLKWYQN-IRHPYPSYGYEPMGGWLHHQIIPVlSQQNSPNQALQPHHHIPMVPAQQ 106
Cdd:smart00818   1 YINFSYE--------------VLTPLKWYQSmIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQ 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179  107 PVVPQQPMMPVPGQHSMTPTQRHQPNLPLPAQQPFQPQPVQPQPHQP-IQPQSPMHPIQPLLPQPPLPPMFPIQPLPPML 185
Cdd:smart00818  66 PVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQpMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLL 145

                          170
                   ....*....|....*....
gi 1720837179  186 PDLPLEAWPATDKTKQEEV 204
Cdd:smart00818 146 PDLPLEAWPATDKTKREEV 164
Gag_MA super family cl03116
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 356-398 4.29e-05

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


The actual alignment was detected with superfamily member pfam01140:

Pssm-ID: 426076 [Multi-domain]  Cd Length: 126  Bit Score: 42.75  E-value: 4.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720837179 356 EGPTFNVGWPPEGTLDAPIVQQVWLIVTGNP--GHPDQFPYIDSW 398
Cdd:pfam01140  41 EWPTLNVGWPRDGTFNLTTILQVKTRVFAPGphGHPDQVPYIVTW 85
 
Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-204 3.27e-53

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: 174.59  E-value: 3.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179   28 YINFSYEnshfqaiafdgtvlVLTPLKWYQN-IRHPYPSYGYEPMGGWLHHQIIPVlSQQNSPNQALQPHHHIPMVPAQQ 106
Cdd:smart00818   1 YINFSYE--------------VLTPLKWYQSmIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQ 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179  107 PVVPQQPMMPVPGQHSMTPTQRHQPNLPLPAQQPFQPQPVQPQPHQP-IQPQSPMHPIQPLLPQPPLPPMFPIQPLPPML 185
Cdd:smart00818  66 PVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQpMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLL 145

                          170
                   ....*....|....*....
gi 1720837179  186 PDLPLEAWPATDKTKQEEV 204
Cdd:smart00818 146 PDLPLEAWPATDKTKREEV 164
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ...
 28-204 7.39e-42

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: 145.67  E-value: 7.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179  28 YINFSYEnshfqaiafdgtvlVLTPLKWYQN-IRHPYPSYGYEPMGGWLHHQIIPVLS----QQNSPNQALQPHHHIPMV 102
Cdd:pfam02948   8 YINFSYE--------------VLTPLKWYQSlIGHAYPRYGFEPMGGWLHHAAGPTLHqttfQQHPPTHSLLPHHHIPPH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179 103 PAQQPVV---PQQPMMPVPGQHSMTPTQRHQPNLPLPAQQPFQPQPVQPQPHQPIQPQSPMHPIQPLLPQPPLPPMFPIQ 179
Cdd:pfam02948  74 PALNPHMqpsGHNPFGPMPGQHSLIPTQHFQPAHGGPAHHPFQPHAGEPHPHHPMQPGNPVHPMHPLPPANPLPPIFPMQ 153

                         170       180
                  ....*....|....*....|....*
gi 1720837179 180 PLPPMLPDLPLEAWPATDKTKQEEV 204
Cdd:pfam02948 154 PLPPLIPDLPLEAWPAADKTKQEEV 178
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 356-398 4.29e-05

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


Pssm-ID: 426076 [Multi-domain]  Cd Length: 126  Bit Score: 42.75  E-value: 4.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720837179 356 EGPTFNVGWPPEGTLDAPIVQQVWLIVTGNP--GHPDQFPYIDSW 398
Cdd:pfam01140  41 EWPTLNVGWPRDGTFNLTTILQVKTRVFAPGphGHPDQVPYIVTW 85
 
Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-204 3.27e-53

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: 174.59  E-value: 3.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179   28 YINFSYEnshfqaiafdgtvlVLTPLKWYQN-IRHPYPSYGYEPMGGWLHHQIIPVlSQQNSPNQALQPHHHIPMVPAQQ 106
Cdd:smart00818   1 YINFSYE--------------VLTPLKWYQSmIRHPYPSYGYEPMGGWLHHQIIPV-SQQHPPTHTLQPHHHIPVLPAQQ 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179  107 PVVPQQPMMPVPGQHSMTPTQRHQPNLPLPAQQPFQPQPVQPQPHQP-IQPQSPMHPIQPLLPQPPLPPMFPIQPLPPML 185
Cdd:smart00818  66 PVVPQQPLMPVPGQHSMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQpMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLL 145

                          170
                   ....*....|....*....
gi 1720837179  186 PDLPLEAWPATDKTKQEEV 204
Cdd:smart00818 146 PDLPLEAWPATDKTKREEV 164
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ...
 28-204 7.39e-42

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: 145.67  E-value: 7.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179  28 YINFSYEnshfqaiafdgtvlVLTPLKWYQN-IRHPYPSYGYEPMGGWLHHQIIPVLS----QQNSPNQALQPHHHIPMV 102
Cdd:pfam02948   8 YINFSYE--------------VLTPLKWYQSlIGHAYPRYGFEPMGGWLHHAAGPTLHqttfQQHPPTHSLLPHHHIPPH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720837179 103 PAQQPVV---PQQPMMPVPGQHSMTPTQRHQPNLPLPAQQPFQPQPVQPQPHQPIQPQSPMHPIQPLLPQPPLPPMFPIQ 179
Cdd:pfam02948  74 PALNPHMqpsGHNPFGPMPGQHSLIPTQHFQPAHGGPAHHPFQPHAGEPHPHHPMQPGNPVHPMHPLPPANPLPPIFPMQ 153

                         170       180
                  ....*....|....*....|....*
gi 1720837179 180 PLPPMLPDLPLEAWPATDKTKQEEV 204
Cdd:pfam02948 154 PLPPLIPDLPLEAWPAADKTKQEEV 178
Gag_MA pfam01140
Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved ...
 356-398 4.29e-05

Matrix protein (MA), p15; The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity.


Pssm-ID: 426076 [Multi-domain]  Cd Length: 126  Bit Score: 42.75  E-value: 4.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1720837179 356 EGPTFNVGWPPEGTLDAPIVQQVWLIVTGNP--GHPDQFPYIDSW 398
Cdd:pfam01140  41 EWPTLNVGWPRDGTFNLTTILQVKTRVFAPGphGHPDQVPYIVTW 85
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH