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Conserved domains on  [gi|594150383|ref|NP_001277300|]
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amelogenin, X isoform isoform 3 precursor [Mus musculus]

Protein Classification

type IV secretion system protein( domain architecture ID 12220051)

type IV secretion system (T4SS) protein functions as a virulence factor that plays important roles in mediating intracellular survival and manipulating host immune response to infection

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 ...
 28-172 1.04e-37

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: 127.21  E-value: 1.04e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383    28 YINLSYEVLTPLKWYQSMIRQP-----------------------HPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHH 84
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPypsygyepmggwlhhqiipvsqqHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383    85 SMTPTQHHQPNIPPSAQQPFQQPFQpqaIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPATD 164
Cdd:smart00818  81 SMTPTQHHQPNLPQPAQQPFQPQPL---QPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPATD 157


                   ....*...
gi 594150383   165 KTKREEVD 172
Cdd:smart00818 158 KTKREEVD 165
 
Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-172 1.04e-37

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: 127.21  E-value: 1.04e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383    28 YINLSYEVLTPLKWYQSMIRQP-----------------------HPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHH 84
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPypsygyepmggwlhhqiipvsqqHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383    85 SMTPTQHHQPNIPPSAQQPFQQPFQpqaIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPATD 164
Cdd:smart00818  81 SMTPTQHHQPNLPQPAQQPFQPQPL---QPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPATD 157


                   ....*...
gi 594150383   165 KTKREEVD 172
Cdd:smart00818 158 KTKREEVD 165
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ...
 21-172 1.69e-30

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: 109.08  E-value: 1.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383   21 PHPGSPGYINLSYEVLTPLKWYQSMIR----------------------------QPHPPSHTLQPHHHLPVVPAQQPV- 71
Cdd:pfam02948   1 PHPGHPGYINFSYEVLTPLKWYQSLIGhayprygfepmggwlhhaagptlhqttfQQHPPTHSLLPHHHIPPHPALNPHm 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383   72 --APQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPfqpqAIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLS 149
Cdd:pfam02948  81 qpSGHNPFGPMPGQHSLIPTQHFQPAHGGPAHHPFQPH----AGEPHPHHPMQPGNPVHPMHPLPPANPLPPIFPMQPLP 156

                         170       180
                  ....*....|....*....|...
gi 594150383  150 PILPELPLEAWPATDKTKREEVD 172
Cdd:pfam02948 157 PLIPDLPLEAWPAADKTKQEEVD 179
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 25-130 4.11e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.07  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383   25 SPGYINLSYEVLTPLKWYQSMIRQPHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPghhsmtptQHHQPNIPPSAQQPF 104
Cdd:PRK10263  746 TPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQP--------QYQQPQQPVAPQPQY 817

                          90       100       110
                  ....*....|....*....|....*....|..
gi 594150383  105 QQPFQPQAIPPQSHQPMQPQSP------LHPM 130
Cdd:PRK10263  818 QQPQQPVAPQPQYQQPQQPVAPqpqdtlLHPL 849
 
Name Accession Description Interval E-value
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 28-172 1.04e-37

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: 127.21  E-value: 1.04e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383    28 YINLSYEVLTPLKWYQSMIRQP-----------------------HPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHH 84
Cdd:smart00818   1 YINFSYEVLTPLKWYQSMIRHPypsygyepmggwlhhqiipvsqqHPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVPGQH 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383    85 SMTPTQHHQPNIPPSAQQPFQQPFQpqaIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPATD 164
Cdd:smart00818  81 SMTPTQHHQPNLPQPAQQPFQPQPL---QPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPATD 157


                   ....*...
gi 594150383   165 KTKREEVD 172
Cdd:smart00818 158 KTKREEVD 165
Amelogenin pfam02948
Amelogenin; Amelogenins play a role in biomineralization. They seem to regulate the formation ...
 21-172 1.69e-30

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: 109.08  E-value: 1.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383   21 PHPGSPGYINLSYEVLTPLKWYQSMIR----------------------------QPHPPSHTLQPHHHLPVVPAQQPV- 71
Cdd:pfam02948   1 PHPGHPGYINFSYEVLTPLKWYQSLIGhayprygfepmggwlhhaagptlhqttfQQHPPTHSLLPHHHIPPHPALNPHm 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383   72 --APQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPfqpqAIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLS 149
Cdd:pfam02948  81 qpSGHNPFGPMPGQHSLIPTQHFQPAHGGPAHHPFQPH----AGEPHPHHPMQPGNPVHPMHPLPPANPLPPIFPMQPLP 156

                         170       180
                  ....*....|....*....|...
gi 594150383  150 PILPELPLEAWPATDKTKREEVD 172
Cdd:pfam02948 157 PLIPDLPLEAWPAADKTKQEEVD 179
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 25-130 4.11e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.07  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383   25 SPGYINLSYEVLTPLKWYQSMIRQPHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPghhsmtptQHHQPNIPPSAQQPF 104
Cdd:PRK10263  746 TPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQP--------QYQQPQQPVAPQPQY 817

                          90       100       110
                  ....*....|....*....|....*....|..
gi 594150383  105 QQPFQPQAIPPQSHQPMQPQSP------LHPM 130
Cdd:PRK10263  818 QQPQQPVAPQPQYQQPQQPVAPqpqdtlLHPL 849
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 43-123 2.08e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 37.71  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383   43 QSMIRQPH-PPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGH-HSMTPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSH-Q 119
Cdd:pfam09770 216 PAPAQPPAaPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPgQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQPPpV 295


                  ....
gi 594150383  120 PMQP 123
Cdd:pfam09770 296 PVQP 299
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 52-154 5.04e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 36.60  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594150383   52 PSHTLQPHHHLPVVPAQQPVAPQQPMMPvpghhsmtPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSPLHPMQ 131
Cdd:PRK10263  747 PIVEPVQQPQQPVAPQQQYQQPQQPVAP--------QPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQ 818

                          90       100
                  ....*....|....*....|...
gi 594150383  132 PLAPQPPLPPLFSmQPLSPILPE 154
Cdd:PRK10263  819 QPQQPVAPQPQYQ-QPQQPVAPQ 840
 
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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