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Conserved domains on  [gi|118344040|ref|NP_001071843|]
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TSC22 protein [Ciona intestinalis]

Protein Classification

TSC22 domain family protein( domain architecture ID 10471801)

transforming growth factor beta-stimulated clone 22 (TSC22) domain family protein which may be a transcription factor; contains a leucine zipper domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TSC22 pfam01166
TSC-22/dip/bun family;
456-512 1.82e-21

TSC-22/dip/bun family;


:

Pssm-ID: 460093  Cd Length: 57  Bit Score: 88.14  E-value: 1.82e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 118344040  456 MDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQFNIAQQKIS 512
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPEQLEQLSSQLQ 57
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
 525-745 1.11e-07

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 55.48  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  525 AQATTLQQGSNATSGLVTPVQSVPSelflhdntllqGNTPTQHPTnisLLSQPVlnSGVATnsqhmmnaqlqqnaqplfq 604
Cdd:PRK10263  324 AAATTATQSWAAPVEPVTQTPPVAS-----------VDVPPAQPT---VAWQPV--PGPQT------------------- 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  605 qtihGQPVVSPVNSNGHPVMQHPtqQNQIPQQVFLQQNYPQQVGPHHSTNTQQHQGLTSQPLHFPNPTYPQANPLGQQPS 684
Cdd:PRK10263  369 ----GEPVIAPAPEGYPQQSQYA--QPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPV 442

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118344040  685 YTLQSTGLPRQSTV---PNILPRQLAPGTVLNPPYHTQPALVNTPTTTEFDQTSDGTVDTRTPL 745
Cdd:PRK10263  443 AGNAWQAEEQQSTFapqSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPL 506
 
Name Accession Description Interval E-value
TSC22 pfam01166
TSC-22/dip/bun family;
456-512 1.82e-21

TSC-22/dip/bun family;


Pssm-ID: 460093  Cd Length: 57  Bit Score: 88.14  E-value: 1.82e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 118344040  456 MDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQFNIAQQKIS 512
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPEQLEQLSSQLQ 57
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
 455-503 1.08e-19

leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; The TGF-beta-stimulated clone-22 domain (TSC22D) family includes TSC22D1-4 and similar proteins. They have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. All family members contain a conserved leucine zipper (ZIP) domain located at the C-terminus. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409276  Cd Length: 49  Bit Score: 82.61  E-value: 1.08e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 118344040 455 AMDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQ 503
Cdd:cd21936    1 AMDLVKSHLMFAVREEVDVLKEQIAELEERISQLERENSLLRSNAPPEV 49
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 525-745 1.11e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 55.48  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  525 AQATTLQQGSNATSGLVTPVQSVPSelflhdntllqGNTPTQHPTnisLLSQPVlnSGVATnsqhmmnaqlqqnaqplfq 604
Cdd:PRK10263  324 AAATTATQSWAAPVEPVTQTPPVAS-----------VDVPPAQPT---VAWQPV--PGPQT------------------- 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  605 qtihGQPVVSPVNSNGHPVMQHPtqQNQIPQQVFLQQNYPQQVGPHHSTNTQQHQGLTSQPLHFPNPTYPQANPLGQQPS 684
Cdd:PRK10263  369 ----GEPVIAPAPEGYPQQSQYA--QPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPV 442

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118344040  685 YTLQSTGLPRQSTV---PNILPRQLAPGTVLNPPYHTQPALVNTPTTTEFDQTSDGTVDTRTPL 745
Cdd:PRK10263  443 AGNAWQAEEQQSTFapqSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPL 506
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 590-721 1.46e-05

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: 48.49  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  590 MMNAQLQQNAQPlfQQTIHGQPVVSPVNSNGHPVMQHPTQQNQIPQQVFLQQNYPQQVGPHHSTNTQQHQGLTSQPLHFP 669
Cdd:pfam09770 202 AMRAQAKKPAQQ--PAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQP 279

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 118344040  670 NPTYPQANPLGQQPSYTLQSTGLPRQstvPNILPRQLAPGTVlNPPYHTQPA 721
Cdd:pfam09770 280 SIQPQAQQFHQQPPPVPVQPTQILQN---PNRLSAARVGYPQ-NPQPGVQPA 327
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 591-725 7.09e-05

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: 44.01  E-value: 7.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040   591 MNAQLQQNAQPLFQQTIHGQPVVSPvnsngHPVMQHPTQQNQIPQQVFLQQNypqqvGPHHSTNTQQHQGLTSQPLHFP- 669
Cdd:smart00818  31 MGGWLHHQIIPVSQQHPPTHTLQPH-----HHIPVLPAQQPVVPQQPLMPVP-----GQHSMTPTQHHQPNLPQPAQQPf 100

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040   670 NPTYPQaNPLGQQPSYTLQ----STGLPRQSTVPNILPRQLAPGTVLNPPYHTQPALVNT 725
Cdd:smart00818 101 QPQPLQ-PPQPQQPMQPQPpvhpIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPATDKT 159
 
Name Accession Description Interval E-value
TSC22 pfam01166
TSC-22/dip/bun family;
456-512 1.82e-21

TSC-22/dip/bun family;


Pssm-ID: 460093  Cd Length: 57  Bit Score: 88.14  E-value: 1.82e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 118344040  456 MDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQFNIAQQKIS 512
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPEQLEQLSSQLQ 57
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
 455-503 1.08e-19

leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; The TGF-beta-stimulated clone-22 domain (TSC22D) family includes TSC22D1-4 and similar proteins. They have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. All family members contain a conserved leucine zipper (ZIP) domain located at the C-terminus. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409276  Cd Length: 49  Bit Score: 82.61  E-value: 1.08e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 118344040 455 AMDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQ 503
Cdd:cd21936    1 AMDLVKSHLMFAVREEVDVLKEQIAELEERISQLERENSLLRSNAPPEV 49
ZIP_TSC22D4 cd21941
leucine zipper domain found in TSC22 domain family protein 4; TSC22 domain family protein 4 ...
 446-503 3.86e-15

leucine zipper domain found in TSC22 domain family protein 4; TSC22 domain family protein 4 (TSC22D4), also called TSC22-related-inducible leucine zipper protein 2 (TILZ2), or Tsc-22-like protein THG-1, is a transcriptional repressor that acts as a molecular determinant of insulin signalling and glucose handling. It also functions in hepatic lipid handling by regulating hepatic very-low-density-lipoprotein (VLDL) release and lipogenic gene expression. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D4. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409281  Cd Length: 74  Bit Score: 70.74  E-value: 3.86e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118344040 446 VRIDNKIEAAMDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQ 503
Cdd:cd21941    1 VAIDNKIEQAMDLVKSHLLFAVREEVEVLKEQIKELSERNAALEQENSLLRSLATPQQ 58
ZIP_TSC22D1 cd21938
leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 ...
 451-513 3.66e-12

leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 (TSC22D1) is also called cerebral protein 2, regulatory protein TSC-22, TGFB-stimulated clone 22, or transforming growth factor beta-1-induced transcript 4 protein (TGFB1I4). It is a transcriptional repressor that was reported to be present in both the cytoplasmic and the nuclear fraction. It is activated by transcription growth factor-beta1 and other growth factors of osteoblastic cells. TSC22D1 acts on the C-type natriuretic peptide (CNP) promoter. It enhances c-Myc-mediated activation of the telomerase reverse transcriptase (TERT) promoter. This model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D1. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409278  Cd Length: 79  Bit Score: 62.47  E-value: 3.66e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118344040 451 KIEAAMDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQFNIAQQKISS 513
Cdd:cd21938    1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQT 63
ZIP_TSC22D3 cd21940
leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 ...
 455-515 1.08e-11

leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 (TSC22D3) is also called DSIP-immunoreactive peptide, protein DIP, delta sleep-inducing peptide immunoreactor, glucocorticoid-induced leucine zipper protein (GILZ), TSC-22-like protein, or TSC-22-related protein (TSC-22R). It protects T-cells from IL2 deprivation-induced apoptosis through the inhibition of FOXO3A transcriptional activity that leads to the down-regulation of the pro-apoptotic factor BCL2L11. In macrophages, it plays a role in the anti-inflammatory and immunosuppressive effects of glucocorticoids and IL10. In T-cells, it inhibits anti-CD3-induced NFKB1 nuclear translocation. TSC22D3 contains a leucine zipper motif, a Pro/Glu rich domain, and three potential phosphorylation sites. This model corresponds to the leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409280  Cd Length: 81  Bit Score: 61.12  E-value: 1.08e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118344040 455 AMDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQFNIAQQKISSKV 515
Cdd:cd21940    1 AMDLVKNHLMYAVREEVEVLKEQIKELVEKNSQLERENSLLKTLASPEQLEKFQSRLPSEE 61
ZIP_TSC22D2 cd21939
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
 455-504 1.39e-08

leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 (TSC22D2), also called transforming growth factor beta-stimulated clone 22 domain family member 2, or TSC22-related-inducible leucine zipper protein 4 (TILZ4), may participate in the regulation of cell growth. It interacts with pyruvate kinase isoform M2 (PKM2) and WD repeat domain 77 (WDR77). The model corresponds to the conserved leucine zipper (ZIP) domain located at the C-terminus of TSC22D2. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. Thus, the DNA-binding capability of the ZIP domain is not obvious. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409279  Cd Length: 63  Bit Score: 51.89  E-value: 1.39e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 118344040 455 AMDLVKKHLMLAVRDEVDELKDKIVELQDDNFKIKLENETLKGILTPEQF 504
Cdd:cd21939    1 AMDLVKSHLMYAVREEVEVLKEQIKELIERNSLLERENALLKSLSNNDQL 50
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 525-745 1.11e-07

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 55.48  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  525 AQATTLQQGSNATSGLVTPVQSVPSelflhdntllqGNTPTQHPTnisLLSQPVlnSGVATnsqhmmnaqlqqnaqplfq 604
Cdd:PRK10263  324 AAATTATQSWAAPVEPVTQTPPVAS-----------VDVPPAQPT---VAWQPV--PGPQT------------------- 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  605 qtihGQPVVSPVNSNGHPVMQHPtqQNQIPQQVFLQQNYPQQVGPHHSTNTQQHQGLTSQPLHFPNPTYPQANPLGQQPS 684
Cdd:PRK10263  369 ----GEPVIAPAPEGYPQQSQYA--QPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPV 442

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118344040  685 YTLQSTGLPRQSTV---PNILPRQLAPGTVLNPPYHTQPALVNTPTTTEFDQTSDGTVDTRTPL 745
Cdd:PRK10263  443 AGNAWQAEEQQSTFapqSTYQTEQTYQQPAAQEPLYQQPQPVEQQPVVEPEPVVEETKPARPPL 506
ZIP_TSC22D-like cd21927
leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding ...
 456-503 1.17e-06

leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding protein, and similar proteins; The family includes TGF-beta-stimulated clone-22 domain (TSC22D) leucine zipper transcription factors, TSC22D1-4, as well as c-Myc-binding protein (MycBP). TSC22D proteins have diverse physiological functions, including cell growth, development, homeostasis, and immune regulation. MycBP, also called associate of Myc 1 (AMY-1), is a novel c-Myc binding protein that may control the transcriptional activity of Myc. It stimulates the activation of E box-dependent transcription by Myc. Members of this family contain a conserved leucine zipper (ZIP) domain. Its first helix is not basic and does not contain the consensus sequence, NXX(A)(A)XX(C/S)R, found in most basic region/leucine zipper (bZIP) proteins. In the bZIP family of transcription factors, the leucine zipper acts as a dimerization domain and the upstream basic region as a DNA-binding domain. However, DNA-binding capability of TSC22D family proteins is not obvious, due to the lack of the basic region found in the original bZIP DNA-binding domains. Similar to bZIP, ZIP forms homo- and heterodimers, resulting in many dimers that may have different effects on transcription.


Pssm-ID: 409275  Cd Length: 51  Bit Score: 45.97  E-value: 1.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 118344040 456 MDLVKKHLMLAVRDE--VDELKDKIVELQDDNFKIKLENETLKGILTPEQ 503
Cdd:cd21927    2 LDFLKHHLGAATPENpeIELLRLELAEMKEKYEAIVEENKKLKAKLAQYE 51
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 590-721 1.46e-05

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: 48.49  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  590 MMNAQLQQNAQPlfQQTIHGQPVVSPVNSNGHPVMQHPTQQNQIPQQVFLQQNYPQQVGPHHSTNTQQHQGLTSQPLHFP 669
Cdd:pfam09770 202 AMRAQAKKPAQQ--PAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAQP 279

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 118344040  670 NPTYPQANPLGQQPSYTLQSTGLPRQstvPNILPRQLAPGTVlNPPYHTQPA 721
Cdd:pfam09770 280 SIQPQAQQFHQQPPPVPVQPTQILQN---PNRLSAARVGYPQ-NPQPGVQPA 327
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 591-725 7.09e-05

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: 44.01  E-value: 7.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040   591 MNAQLQQNAQPLFQQTIHGQPVVSPvnsngHPVMQHPTQQNQIPQQVFLQQNypqqvGPHHSTNTQQHQGLTSQPLHFP- 669
Cdd:smart00818  31 MGGWLHHQIIPVSQQHPPTHTLQPH-----HHIPVLPAQQPVVPQQPLMPVP-----GQHSMTPTQHHQPNLPQPAQQPf 100

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040   670 NPTYPQaNPLGQQPSYTLQ----STGLPRQSTVPNILPRQLAPGTVLNPPYHTQPALVNT 725
Cdd:smart00818 101 QPQPLQ-PPQPQQPMQPQPpvhpIPPLPPQPPLPPMFPMQPLPPLLPDLPLEAWPATDKT 159
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 560-675 2.56e-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: 41.17  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040  560 QGNTPTQHPTNISLLSQPVLNSGVATNSQHMMNAQLQ-QNAQPLFQQTIHGQPVVSPVNSNGHPVMQHPTQ--QN---QI 633
Cdd:pfam09770 231 QQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQrPQSPQPDPAQPSIQPQAQQFHQQPPPVPVQPTQilQNpnrLS 310

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 118344040  634 PQQVFLQQNYPQQVGPHHSTNTQQHQGLTSQPLHFpnPTYPQ 675
Cdd:pfam09770 311 AARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPI--ITHPQ 350
PRK10927 PRK10927
cell division protein FtsN;
625-721 2.99e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 40.43  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118344040 625 QHPTQQNQIPqqvfLQQNYPQQVGPHHSTNTQQHQGLTSQPLHFPnPTYPQANPlgQQPSYTLQSTGLPRQSTVPNILPR 704
Cdd:PRK10927 131 QQPTQLVEVP----WNEQTPEQRQQTLQRQRQAQQLAEQQRLAQQ-SRTTEQSW--QQQTRTSQAAPVQAQPRQSKPAST 203

                         90
                 ....*....|....*....
gi 118344040 705 QLAPGTVLNPPYHT--QPA 721
Cdd:PRK10927 204 QQPYQDLLQTPAHTtaQSK 222
 
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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