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Conserved domains on  [gi|1068403865|ref|XP_018049323|]
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PREDICTED: protein bunched, class 2/F/G isoform [Atta colombica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
 595-643 1.47e-28

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: 108.04  E-value: 1.47e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1068403865 595 AMDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPET 643
Cdd:cd21936     1 AMDLVKSHLMFAVREEVDVLKEQIAELEERISQLERENSLLRSNAPPEV 49
PAT1 super family cl37801
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 420-546 7.31e-04

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


The actual alignment was detected with superfamily member pfam09770:

Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 42.72  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068403865 420 QQTSAPTSQTPNILVTQHQQS--------ESAPCQQPLATQQPQMTQISEPMTAIQGIQSMQSihktagAPQQSQAIAPS 491
Cdd:pfam09770 212 QQPAPAPAQPPAAPPAQQAQQqqqfppqiQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQP------DPAQPSIQPQA 285

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1068403865 492 TQQLQPQTTNGNAPVQITQ--------MTAGCQSAVGGLQQQGNMTFHQSDPEQESISGIVAN 546
Cdd:pfam09770 286 QQFHQQPPPVPVQPTQILQnpnrlsaaRVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITH 348
 
Name Accession Description Interval E-value
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
 595-643 1.47e-28

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: 108.04  E-value: 1.47e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1068403865 595 AMDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPET 643
Cdd:cd21936     1 AMDLVKSHLMFAVREEVDVLKEQIAELEERISQLERENSLLRSNAPPEV 49
TSC22 pfam01166
TSC-22/dip/bun family;
596-650 1.82e-28

TSC-22/dip/bun family;


Pssm-ID: 460093  Cd Length: 57  Bit Score: 107.78  E-value: 1.82e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1068403865 596 MDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPETLAQLSQS 650
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPEQLEQLSSQ 55
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 420-546 7.31e-04

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: 42.72  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068403865 420 QQTSAPTSQTPNILVTQHQQS--------ESAPCQQPLATQQPQMTQISEPMTAIQGIQSMQSihktagAPQQSQAIAPS 491
Cdd:pfam09770 212 QQPAPAPAQPPAAPPAQQAQQqqqfppqiQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQP------DPAQPSIQPQA 285

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1068403865 492 TQQLQPQTTNGNAPVQITQ--------MTAGCQSAVGGLQQQGNMTFHQSDPEQESISGIVAN 546
Cdd:pfam09770 286 QQFHQQPPPVPVQPTQILQnpnrlsaaRVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITH 348
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 409-505 2.67e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068403865  409 LPVQNVCQSTVQQTSAPTSQTPNILVTQHQQSesapcQQPLATQQPQMTQISEPMTAIQGIQSMQSIHKTAGAPQQSQAI 488
Cdd:PRK10263   750 EPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQP-----QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPV 824

                           90
                   ....*....|....*..
gi 1068403865  489 APSTQQLQPQTTNGNAP 505
Cdd:PRK10263   825 APQPQYQQPQQPVAPQP 841
BRLZ smart00338
basic region leucin zipper;
615-659 7.42e-03

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 35.62  E-value: 7.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1068403865  615 KEKIAELMDRINQLEAENSILKAhatpeTLAQLSQSAAKLSQNNS 659
Cdd:smart00338  25 KAEIEELERKVEQLEAENERLKK-----EIERLRRELEKLKSELE 64
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 419-499 7.97e-03

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: 37.85  E-value: 7.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068403865  419 VQQTSAPTSQ--TPNILVTQHQQSESAPCQQPLATQQPQMTQ-ISEPMTAIQGIQSmqSIHKTAGAPQQSQAIAP--STQ 493
Cdd:smart00818  35 LHHQIIPVSQqhPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVpGQHSMTPTQHHQP--NLPQPAQQPFQPQPLQPpqPQQ 112


                   ....*.
gi 1068403865  494 QLQPQT 499
Cdd:smart00818 113 PMQPQP 118
 
Name Accession Description Interval E-value
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
 595-643 1.47e-28

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: 108.04  E-value: 1.47e-28
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1068403865 595 AMDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPET 643
Cdd:cd21936     1 AMDLVKSHLMFAVREEVDVLKEQIAELEERISQLERENSLLRSNAPPEV 49
TSC22 pfam01166
TSC-22/dip/bun family;
596-650 1.82e-28

TSC-22/dip/bun family;


Pssm-ID: 460093  Cd Length: 57  Bit Score: 107.78  E-value: 1.82e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1068403865 596 MDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPETLAQLSQS 650
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPEQLEQLSSQ 55
ZIP_TSC22D4 cd21941
leucine zipper domain found in TSC22 domain family protein 4; TSC22 domain family protein 4 ...
 586-647 2.48e-25

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: 99.63  E-value: 2.48e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1068403865 586 VAIDNKIEQAMDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPETLAQL 647
Cdd:cd21941     1 VAIDNKIEQAMDLVKSHLLFAVREEVEVLKEQIKELSERNAALEQENSLLRSLATPQQLSRL 62
ZIP_TSC22D1 cd21938
leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 ...
 591-647 5.18e-21

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: 87.51  E-value: 5.18e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1068403865 591 KIEQAMDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPETLAQL 647
Cdd:cd21938     1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQF 57
ZIP_TSC22D3 cd21940
leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 ...
 595-659 2.59e-18

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: 80.00  E-value: 2.59e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1068403865 595 AMDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPEtlaQLSQSAAKLSQNNS 659
Cdd:cd21940     1 AMDLVKNHLMYAVREEVEVLKEQIKELVEKNSQLERENSLLKTLASPE---QLEKFQSRLPSEET 62
ZIP_TSC22D2 cd21939
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
 595-652 2.76e-17

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: 76.16  E-value: 2.76e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1068403865 595 AMDLVKSHLMFAVREEVEVLKEKIAELMDRINQLEAENSILKAHATPETLAQLSQSAA 652
Cdd:cd21939     1 AMDLVKSHLMYAVREEVEVLKEQIKELIERNSLLERENALLKSLSNNDQLSQLSTQQG 58
ZIP_TSC22D-like cd21927
leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding ...
 596-642 1.96e-11

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: 59.45  E-value: 1.96e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1068403865 596 MDLVKSHLMFAVREE--VEVLKEKIAELMDRINQLEAENSILKAHATPE 642
Cdd:cd21927     2 LDFLKHHLGAATPENpeIELLRLELAEMKEKYEAIVEENKKLKAKLAQY 50
ZIP_MycBP-like cd21937
leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called ...
 595-637 2.84e-04

leucine zipper domain found in c-Myc-binding protein and similar proteins; 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. This model corresponds to the conserved region that shows high sequence similarity with the leucine zipper (ZIP) domain located at the C-terminus of TGF-beta-stimulated clone-22 domain (TSC22D) family transcription factors. The first helix of ZIP 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: 409277 [Multi-domain]  Cd Length: 53  Bit Score: 39.07  E-value: 2.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1068403865 595 AMDLVKSHLMFA--VREEVEVLKEKIAELMDRINQLEAENSILKA 637
Cdd:cd21937     3 ALDFIKQHLGAPgpEDADVEALRLENEELKQKNEELEEENKELKA 47
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 420-546 7.31e-04

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: 42.72  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068403865 420 QQTSAPTSQTPNILVTQHQQS--------ESAPCQQPLATQQPQMTQISEPMTAIQGIQSMQSihktagAPQQSQAIAPS 491
Cdd:pfam09770 212 QQPAPAPAQPPAAPPAQQAQQqqqfppqiQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQP------DPAQPSIQPQA 285

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1068403865 492 TQQLQPQTTNGNAPVQITQ--------MTAGCQSAVGGLQQQGNMTFHQSDPEQESISGIVAN 546
Cdd:pfam09770 286 QQFHQQPPPVPVQPTQILQnpnrlsaaRVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITH 348
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 583-628 1.02e-03

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 38.06  E-value: 1.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1068403865 583 TSAVAIDN--KIEQAMDLVKS---HLMFAVREEVE-----VLKEKIAELMDRINQL 628
Cdd:cd02656    11 KQAVKEDEdgNYEEALELYKEaldYLLQALKAEKEpklrkLLRKKVKEYLDRAEFL 66
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 409-505 2.67e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.22  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068403865  409 LPVQNVCQSTVQQTSAPTSQTPNILVTQHQQSesapcQQPLATQQPQMTQISEPMTAIQGIQSMQSIHKTAGAPQQSQAI 488
Cdd:PRK10263   750 EPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQP-----QQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPV 824

                           90
                   ....*....|....*..
gi 1068403865  489 APSTQQLQPQTTNGNAP 505
Cdd:PRK10263   825 APQPQYQQPQQPVAPQP 841
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 591-637 3.51e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 36.48  E-value: 3.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1068403865 591 KIEQAMDLVkSHLmfavREEVEVLKEKIAELMDRINQLEAENSILKA 637
Cdd:pfam06005  12 KIQAAVDTI-ALL----QMENEELKEENEELKEEANELEEENQQLKQ 53
BRLZ smart00338
basic region leucin zipper;
615-659 7.42e-03

basic region leucin zipper;


Pssm-ID: 197664 [Multi-domain]  Cd Length: 65  Bit Score: 35.62  E-value: 7.42e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1068403865  615 KEKIAELMDRINQLEAENSILKAhatpeTLAQLSQSAAKLSQNNS 659
Cdd:smart00338  25 KAEIEELERKVEQLEAENERLKK-----EIERLRRELEKLKSELE 64
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 419-499 7.97e-03

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: 37.85  E-value: 7.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1068403865  419 VQQTSAPTSQ--TPNILVTQHQQSESAPCQQPLATQQPQMTQ-ISEPMTAIQGIQSmqSIHKTAGAPQQSQAIAP--STQ 493
Cdd:smart00818  35 LHHQIIPVSQqhPPTHTLQPHHHIPVLPAQQPVVPQQPLMPVpGQHSMTPTQHHQP--NLPQPAQQPFQPQPLQPpqPQQ 112


                   ....*.
gi 1068403865  494 QLQPQT 499
Cdd:smart00818 113 PMQPQP 118
 
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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