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Conserved domains on  [gi|41056193|ref|NP_956403|]
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TSC22 domain family protein 2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZIP_TSC22D2 cd21939
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
 465-527 1.10e-35

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: 127.77  E-value: 1.10e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41056193 465 AMDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQLTQLTTQIHNPSST 527
Cdd:cd21939   1 AMDLVKSHLMYAVREEVEVLKEQIKELIERNSLLERENALLKSLSNNDQLSQLSTQQGNPSST 63
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 198-335 3.98e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


The actual alignment was detected with superfamily member TIGR01628:

Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 39.79  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056193   198 PHTDSGYISAPSNPPVElQQHPFGIAPQNPFGDAKSPSMPSTTQPQPFYAGKPLQKPVQVLQTLVTDYRAQHQPPGSPVV 277
Cdd:TIGR01628 385 LPMGSPMGGAMGQPPYY-GQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVM 463

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41056193   278 ---SVATLPLVTPLTQgpspimtPAAGGVHLLGMGLPISQPEHA-VQPGMGMVAQALAPLIQ 335
Cdd:TIGR01628 464 yppNYQSLPLSQDLPQ-------PQSTASQGGQNKKLAQVLASAtPQMQKQVLGERLFPLVE 518
 
Name Accession Description Interval E-value
ZIP_TSC22D2 cd21939
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
 465-527 1.10e-35

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: 127.77  E-value: 1.10e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41056193 465 AMDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQLTQLTTQIHNPSST 527
Cdd:cd21939   1 AMDLVKSHLMYAVREEVEVLKEQIKELIERNSLLERENALLKSLSNNDQLSQLSTQQGNPSST 63
TSC22 pfam01166
TSC-22/dip/bun family;
466-522 1.71e-28

TSC-22/dip/bun family;


Pssm-ID: 460093  Cd Length: 57  Bit Score: 107.40  E-value: 1.71e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 41056193   466 MDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQLTQLTTQIH 522
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPEQLEQLSSQLQ 57
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 198-335 3.98e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 39.79  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056193   198 PHTDSGYISAPSNPPVElQQHPFGIAPQNPFGDAKSPSMPSTTQPQPFYAGKPLQKPVQVLQTLVTDYRAQHQPPGSPVV 277
Cdd:TIGR01628 385 LPMGSPMGGAMGQPPYY-GQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVM 463

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41056193   278 ---SVATLPLVTPLTQgpspimtPAAGGVHLLGMGLPISQPEHA-VQPGMGMVAQALAPLIQ 335
Cdd:TIGR01628 464 yppNYQSLPLSQDLPQ-------PQSTASQGGQNKKLAQVLASAtPQMQKQVLGERLFPLVE 518
 
Name Accession Description Interval E-value
ZIP_TSC22D2 cd21939
leucine zipper domain found in TSC22 domain family protein 2; TSC22 domain family protein 2 ...
 465-527 1.10e-35

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: 127.77  E-value: 1.10e-35
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41056193 465 AMDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQLTQLTTQIHNPSST 527
Cdd:cd21939   1 AMDLVKSHLMYAVREEVEVLKEQIKELIERNSLLERENALLKSLSNNDQLSQLSTQQGNPSST 63
ZIP_TSC22D4 cd21941
leucine zipper domain found in TSC22 domain family protein 4; TSC22 domain family protein 4 ...
 456-529 1.05e-28

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: 108.87  E-value: 1.05e-28
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41056193 456 VAIDNKIEQAMDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQLTQLTTQIHNPSSTSP 529
Cdd:cd21941   1 VAIDNKIEQAMDLVKSHLLFAVREEVEVLKEQIKELSERNAALEQENSLLRSLATPQQLSRLQSRQPTSRKPAP 74
TSC22 pfam01166
TSC-22/dip/bun family;
466-522 1.71e-28

TSC-22/dip/bun family;


Pssm-ID: 460093  Cd Length: 57  Bit Score: 107.40  E-value: 1.71e-28
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 41056193   466 MDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQLTQLTTQIH 522
Cdd:pfam01166   1 MDLVKSHLMYAVREEVEVLKEQIKELEERNSQLEEENSILRANASPEQLEQLSSQLQ 57
ZIP_TSC22D1 cd21938
leucine zipper domain found in TSC22 domain family protein 1; TSC22 domain family protein 1 ...
 461-533 1.18e-27

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: 106.00  E-value: 1.18e-27
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41056193 461 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQLTQLTTQIHN---PSSTSPQQTT 533
Cdd:cd21938   1 KIEQAMDLVKSHLMYAVREEVEVLKEQIKELIEKNSQLEQENNLLKTLASPEQLAQFQAQLQTgspPSSSQPPGTT 76
ZIP_TSC22D cd21936
leucine zipper domain found in the TSC22 domain family of leucine zipper transcription factors; ...
 465-513 9.41e-27

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: 102.26  E-value: 9.41e-27
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 41056193 465 AMDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQ 513
Cdd:cd21936   1 AMDLVKSHLMFAVREEVDVLKEQIAELEERISQLERENSLLRSNAPPEV 49
ZIP_TSC22D3 cd21940
leucine zipper domain found in TSC22 domain family protein 3; TSC22 domain family protein 3 ...
 465-542 7.89e-25

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: 98.10  E-value: 7.89e-25
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41056193 465 AMDLVKSHLMYAVREEVEVLKEQIKELYERNSVLERENAVLKSLANNEQLTQLttQIHNPSSTSPQQTTVNAILQEAS 542
Cdd:cd21940   1 AMDLVKNHLMYAVREEVEVLKEQIKELVEKNSQLERENSLLKTLASPEQLEKF--QSRLPSEETAPETPLDAQPAEHS 76
ZIP_TSC22D-like cd21927
leucine zipper found in the TSC22 domain leucine zipper transcription factors, c-Myc-binding ...
 466-513 3.46e-16

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: 72.55  E-value: 3.46e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 41056193 466 MDLVKSHLMYAVREE--VEVLKEQIKELYERNSVLERENAVLKSLANNEQ 513
Cdd:cd21927   2 LDFLKHHLGAATPENpeIELLRLELAEMKEKYEAIVEENKKLKAKLAQYE 51
ZIP_MycBP-like cd21937
leucine zipper domain found in c-Myc-binding protein and similar proteins; MycBP, also called ...
 465-507 2.93e-05

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: 41.77  E-value: 2.93e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 41056193 465 AMDLVKSHL--MYAVREEVEVLKEQIKELYERNSVLERENAVLKS 507
Cdd:cd21937   3 ALDFIKQHLgaPGPEDADVEALRLENEELKQKNEELEEENKELKA 47
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 479-523 1.38e-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: 37.63  E-value: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 41056193   479 EEVEVLKEQIKELYERNSVLERENAVLKslANNEQLTQLTTQIHN 523
Cdd:pfam06005  18 DTIALLQMENEELKEENEELKEEANELE--EENQQLKQERNQWQE 60
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 198-335 3.98e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 39.79  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41056193   198 PHTDSGYISAPSNPPVElQQHPFGIAPQNPFGDAKSPSMPSTTQPQPFYAGKPLQKPVQVLQTLVTDYRAQHQPPGSPVV 277
Cdd:TIGR01628 385 LPMGSPMGGAMGQPPYY-GQGPQQQFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNAVRAPSRNAQNAAQKPPMQPVM 463

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41056193   278 ---SVATLPLVTPLTQgpspimtPAAGGVHLLGMGLPISQPEHA-VQPGMGMVAQALAPLIQ 335
Cdd:TIGR01628 464 yppNYQSLPLSQDLPQ-------PQSTASQGGQNKKLAQVLASAtPQMQKQVLGERLFPLVE 518
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 457-520 8.79e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 38.68  E-value: 8.79e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41056193   457 AIDNKIEQAMDLVKSHLMYAVREEVEVLKEQIKELYErnsVLERE----NAVLKSLANNEQ-LTQLTTQ 520
Cdd:pfam06160 241 QLEEQLEENLALLENLELDEAEEALEEIEERIDQLYD---LLEKEvdakKYVEKNLPEIEDyLEHAEEQ 306
 
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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