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Conserved domains on  [gi|157816925|ref|NP_001102493|]
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pinin [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pinin_SDK_N pfam04697
pinin/SDK conserved region; SDK2/3 is localized in nuclear speckles where as pinin is known to ...
 1-130 1.34e-42

pinin/SDK conserved region; SDK2/3 is localized in nuclear speckles where as pinin is known to localize at the desmosomes where it is thought to be involved in anchoring intermediate filaments to the desmosomal plaque. The role of SDK2/3 in the nucleus is thought to be concerned with modulation of alternative pre-mRNA splicing. pinin has also been implicated as a tumour suppressor. The conserved region is found at the N-terminus of the member proteins.


:

Pssm-ID: 461397  Cd Length: 132  Bit Score: 150.77  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816925    1 MAVAVRALQEQLEKAKESLKNVDENIRKLTGRDPNDVRPIQARLLALSGPGGGRGRGSLLLRRGFS-DSGGGPPAKQRDL 79
Cdd:pfam04697   1 MAVAVRALQEQIEKAKENLKGVDENIKKLTGRDPNERRPGAARRLELQMSGPGRGRGRGQVLLRRGwSDSGGPPVKRRDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157816925   80 EGAVSRLGGERRTRRESRQESDPEDDD-VKKPALQSSVVATSKERTRRDLIQ 130
Cdd:pfam04697  81 GGAVRRLAGNRRARRDSRRDDSEEEDDlPKKPALQSSVVATSKERTRKDLID 132
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 136-261 1.19e-23

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


:

Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 96.98  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816925  136 EKGKQRNRRIFGLLMGTLQKFKQESTVATERQKRRQEIEQKLEVQAEEER----KQVENERRELFEERRAKQTELRLLEQ 211
Cdd:pfam04696   1 EEEKKRNRRLFGGLLGTLQKFKKEESKQKEKEERRAEIEKRLEEKAKQEKeeleERKREEREELFEERRAEQIELRALEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 157816925  212 KVELAQLQEEWNEHNAKIIKYIRTKTKPHLFYIPGRMCPATQKLIEESQR 261
Cdd:pfam04696  81 KLELKELMETWHENLKALANFLKTKTEPPIYYLPWKLTEKTEELLEEQIE 130
Amelogenin super family cl33250
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 491-556 2.69e-04

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.


The actual alignment was detected with superfamily member smart00818:

Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 42.08  E-value: 2.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157816925   491 HSQPHSQPHSQPQPalQSQPLSQPEALPLAVLQPPPQVIQEQGNLPPERKDFPVE--AIKLPEVPVEP 556
Cdd:smart00818  87 HHQPNLPQPAQQPF--QPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQplPPLLPDLPLEA 152
 
Name Accession Description Interval E-value
Pinin_SDK_N pfam04697
pinin/SDK conserved region; SDK2/3 is localized in nuclear speckles where as pinin is known to ...
 1-130 1.34e-42

pinin/SDK conserved region; SDK2/3 is localized in nuclear speckles where as pinin is known to localize at the desmosomes where it is thought to be involved in anchoring intermediate filaments to the desmosomal plaque. The role of SDK2/3 in the nucleus is thought to be concerned with modulation of alternative pre-mRNA splicing. pinin has also been implicated as a tumour suppressor. The conserved region is found at the N-terminus of the member proteins.


Pssm-ID: 461397  Cd Length: 132  Bit Score: 150.77  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816925    1 MAVAVRALQEQLEKAKESLKNVDENIRKLTGRDPNDVRPIQARLLALSGPGGGRGRGSLLLRRGFS-DSGGGPPAKQRDL 79
Cdd:pfam04697   1 MAVAVRALQEQIEKAKENLKGVDENIKKLTGRDPNERRPGAARRLELQMSGPGRGRGRGQVLLRRGwSDSGGPPVKRRDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157816925   80 EGAVSRLGGERRTRRESRQESDPEDDD-VKKPALQSSVVATSKERTRRDLIQ 130
Cdd:pfam04697  81 GGAVRRLAGNRRARRDSRRDDSEEEDDlPKKPALQSSVVATSKERTRKDLID 132
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 136-261 1.19e-23

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 96.98  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816925  136 EKGKQRNRRIFGLLMGTLQKFKQESTVATERQKRRQEIEQKLEVQAEEER----KQVENERRELFEERRAKQTELRLLEQ 211
Cdd:pfam04696   1 EEEKKRNRRLFGGLLGTLQKFKKEESKQKEKEERRAEIEKRLEEKAKQEKeeleERKREEREELFEERRAEQIELRALEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 157816925  212 KVELAQLQEEWNEHNAKIIKYIRTKTKPHLFYIPGRMCPATQKLIEESQR 261
Cdd:pfam04696  81 KLELKELMETWHENLKALANFLKTKTEPPIYYLPWKLTEKTEELLEEQIE 130
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 491-556 2.69e-04

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: 42.08  E-value: 2.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157816925   491 HSQPHSQPHSQPQPalQSQPLSQPEALPLAVLQPPPQVIQEQGNLPPERKDFPVE--AIKLPEVPVEP 556
Cdd:smart00818  87 HHQPNLPQPAQQPF--QPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQplPPLLPDLPLEA 152
PHA03247 PHA03247
large tegument protein UL36; Provisional
 493-556 1.56e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157816925  493 QPHSQPHSQPQPALQSQPLSQPEALPLAVLQPPPQviqeqgnlPPERKDFPVEAIKLPEVPVEP 556
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP--------PPPRPQPPLAPTTDPAGAGEP 2955
 
Name Accession Description Interval E-value
Pinin_SDK_N pfam04697
pinin/SDK conserved region; SDK2/3 is localized in nuclear speckles where as pinin is known to ...
 1-130 1.34e-42

pinin/SDK conserved region; SDK2/3 is localized in nuclear speckles where as pinin is known to localize at the desmosomes where it is thought to be involved in anchoring intermediate filaments to the desmosomal plaque. The role of SDK2/3 in the nucleus is thought to be concerned with modulation of alternative pre-mRNA splicing. pinin has also been implicated as a tumour suppressor. The conserved region is found at the N-terminus of the member proteins.


Pssm-ID: 461397  Cd Length: 132  Bit Score: 150.77  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816925    1 MAVAVRALQEQLEKAKESLKNVDENIRKLTGRDPNDVRPIQARLLALSGPGGGRGRGSLLLRRGFS-DSGGGPPAKQRDL 79
Cdd:pfam04697   1 MAVAVRALQEQIEKAKENLKGVDENIKKLTGRDPNERRPGAARRLELQMSGPGRGRGRGQVLLRRGwSDSGGPPVKRRDL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157816925   80 EGAVSRLGGERRTRRESRQESDPEDDD-VKKPALQSSVVATSKERTRRDLIQ 130
Cdd:pfam04697  81 GGAVRRLAGNRRARRDSRRDDSEEEDDlPKKPALQSSVVATSKERTRKDLID 132
Pinin_SDK_memA pfam04696
pinin/SDK/memA/ protein conserved region; Members of this family have very varied ...
 136-261 1.19e-23

pinin/SDK/memA/ protein conserved region; Members of this family have very varied localizations within the eukaryotic cell. pinin is known to localize at the desmosomes and is implicated in anchoring intermediate filaments to the desmosomal plaque. SDK2/3 is a dynamically localized nuclear protein thought to be involved in modulation of alternative pre-mRNA splicing. memA is a tumour marker preferentially expressed in human melanoma cell lines. A common feature of the members of this family is that they may all participate in regulating protein-protein interactions.


Pssm-ID: 461396 [Multi-domain]  Cd Length: 130  Bit Score: 96.98  E-value: 1.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157816925  136 EKGKQRNRRIFGLLMGTLQKFKQESTVATERQKRRQEIEQKLEVQAEEER----KQVENERRELFEERRAKQTELRLLEQ 211
Cdd:pfam04696   1 EEEKKRNRRLFGGLLGTLQKFKKEESKQKEKEERRAEIEKRLEEKAKQEKeeleERKREEREELFEERRAEQIELRALEE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 157816925  212 KVELAQLQEEWNEHNAKIIKYIRTKTKPHLFYIPGRMCPATQKLIEESQR 261
Cdd:pfam04696  81 KLELKELMETWHENLKALANFLKTKTEPPIYYLPWKLTEKTEELLEEQIE 130
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 491-556 2.69e-04

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: 42.08  E-value: 2.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157816925   491 HSQPHSQPHSQPQPalQSQPLSQPEALPLAVLQPPPQVIQEQGNLPPERKDFPVE--AIKLPEVPVEP 556
Cdd:smart00818  87 HHQPNLPQPAQQPF--QPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPLPPMFPMQplPPLLPDLPLEA 152
PHA03247 PHA03247
large tegument protein UL36; Provisional
 493-556 1.56e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157816925  493 QPHSQPHSQPQPALQSQPLSQPEALPLAVLQPPPQviqeqgnlPPERKDFPVEAIKLPEVPVEP 556
Cdd:PHA03247 2900 LPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP--------PPPRPQPPLAPTTDPAGAGEP 2955
 
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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